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(([(1E)-phenylmethylidene]amino)oxy)acetic acid + ascorbate + O2
(2R)-hydroxy(([(1E)-phenylmethylidene]amino)oxy)ethanoic acid + ?
non-enzymatic dealkylation yields benzaldoxime and glyoxylate
-
-
?
2,6-difluorohippuric acid + ascorbate + O2
?
-
-
-
?
2-aminohippuric acid + ascorbate + O2
?
-
-
-
?
2-hydroxyhippuric acid + ascorbate + O2
?
-
-
-
?
2-iodohippuric acid + ascorbate + O2
?
-
-
-
?
2-methylhippuric acid + ascorbate + O2
?
-
-
-
?
2-propylmercaptoacetylglycine + ascorbate + O2
?
-
-
-
?
2-pyridylmercaptoacetylglycine + ascorbate + O2
?
-
-
-
?
3-(2-furyl)acryloylglycine + ascorbate + O2
?
-
-
-
?
3-chlorohippuric acid + ascorbate + O2
?
-
-
-
?
3-indolylacetylglycine + ascorbate + O2
?
-
-
-
?
3-methylhippuric acid + ascorbate + O2
?
-
-
-
?
3-phenylthiopropionylglycine + ascorbate + O2
?
-
-
-
?
4-aminohippuric acid + ascorbate + O2
?
-
-
-
?
4-bromohippuric acid + ascorbate + O2
?
-
-
-
?
4-chlorohippuric acid + ascorbate + O2
?
-
-
-
?
4-dimethylaminoazobenzene-4'-sulfonyl-Gly-L-Phe-Gly + ascorbate + O2
4-dimethylaminoazobenzene-4'-sulfonyl-Gly-L-Phe-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
4-ethylhippuric acid + ascorbate + O2
?
-
-
-
?
4-hydroxyhippuric acid + ascorbate + O2
?
-
-
-
?
4-methoxyhippuric acid + ascorbate + O2
?
-
-
-
?
4-methylhippuric acid + ascorbate + O2
?
-
-
-
?
4-nitrobenzoyl-Gly-Gly + ascorbate + O2
?
-
-
-
?
4-nitrohippuric acid + ascorbate + O2
?
-
-
-
?
4-phenylbutyrylglycine + ascorbate + O2
?
-
-
-
?
4-propylhippuric acid + ascorbate + O2
?
-
-
-
?
4-trifluoromethylhippuric acid + ascorbate + O2
?
-
-
-
?
5-phenylpentanoylglycine + ascorbate + O2
?
-
-
-
?
6-phenylhexanoylglycine + ascorbate + O2
?
-
-
-
?
8-phenyloctanoylglycine + ascorbate + O2
?
-
-
-
?
Ac-Tyr-Val-Gly + ascorbate + O2
Ac-Tyr-Val-(2-OH-Gly) + dehydroascorbate + H2O
-
-
-
?
acetyl-D-alanine + ascorbate + O2
?
-
-
-
?
acetyl-Gly-Gly + ascorbate + O2
?
-
-
-
?
acetyl-glycine + ascorbate + O2
?
-
-
-
?
acetyl-L-Tyr-L-Phe-Gly + ascorbate + O2
acetyl-L-Tyr-L-Phe-2-hydroxyglycine + dehydroascorbate + H2O
acetyl-L-Tyr-L-Val-Gly + ascorbate + O2
?
-
-
-
-
?
adrenocorticotrophic hormone(9-14) + ascorbate + O2
adrenocorticotrophic hormone(9-13)-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
Ala-Ile-Gly-Val-Gly-Ala-Pro-Gly + ascorbate + O2
Ala-Ile-Gly-Val-Gly-Ala-Pro-2-hydroxyglycine + dehydroascorbate + H2O
alanyl-L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
-
?
alanyl-L-prolylglycine + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
-
?
alanylglycyl-L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
-
?
alanylglycyl-L-prolylglycine + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
-
?
alanylglycylvalyl-L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
-
?
alanylglycylvalyl-L-prolylglycine + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
-
?
alpha-N-acetyl-adrenocorticotrophic hormone(1-14) + ascorbate + O2
alpha-N-acetyl-adrenocorticotrophic hormone(1-13)-2-hydroxyglycine + dehydroascorbate + H2O
alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
benzaldehyde imino-oxy acetic acid + O2
benzaldoxime + glyoxylate
assay at 37°C, pH 6.0
-
-
?
benzoyl-D-alanine + ascorbate + O2
?
-
-
-
?
calcitonin + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
?
CBZ-D-alanine + ascorbate + O2
?
-
-
-
?
CBZ-glycine + ascorbate + O2
?
-
-
-
?
chloroacetyl-Gly-Gly + ascorbate + O2
?
-
-
-
?
chromogranin A + ascorbate + O2
? + dehydroascorbate + H2O
cinnamoylglycine + ascorbate + O2
?
-
-
-
?
D-iodo-Tyr-Val-Gly + ascorbate + O2
D-iodo-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
labeled substrate
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
D-Tyr-Pro-Gly-Gly + ascorbate + O2
D-Tyr-Pro-Gly-2-hydroxyglycine + dehydroascorbate + H2O
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-NH2 + glyoxylate + dehydroascorbate + H2O
dansyl-D-Tyr-Val-Gly + ascorbate + O2
dansyl-D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
dansyl-D-Tyr-Val-Gly + H2O2
dansyl-D-Tyr-Val-2-hydroxyglycine + H2O
-
peptidylglycine monooxygenase is able to catalyze the hydroxylation of peptidylglycine substrates starting from the oxidized enzyme and using hydrogen peroxide as the only source of oxygen
-
-
?
dansyl-Gly-Gly-Ser-CO-NH-CH2-COOH + ascorbate + O2
?
-
substrate contains either protium or deuterium at the CH2-group
-
-
?
dansyl-L-Tyr-L-Val-Gly + ascorbate + O2
?
dansyl-YVG + ascorbate + O2
?
-
-
-
-
?
dansyl-YVG-COOH + ascorbate + O2
dansyl-YV-NH2 + dehydroascorbate + H2O
diiodotyrosylglycine + ascorbate + O2
diiodotyrosyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
gamma-Glu-Gly-Gly + ascorbate + O2
gamma-Glu-Gly-NH2 + glyoxylate + dehydroascorbate + H2O
-
-
-
-
?
glutathione + ascorbate + O2
gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
-
-
-
-
?
glyoxylic acid phenylhydrazone + ascorbate + O2
oxalate phenylhydrazide + dehydroascorbate + H2O
-
competitive substrate, inhibitory
-
?
hippuric acid + ascorbate + O2
?
-
-
-
?
hippuric acid + ascorbate + O2
? + dehydroascorbate + H2O
hippuric acid + ascorbate + O2
alpha-hydroxyhippuric acid + dehydroascorbate + H2O
hippuric acid + ascorbate + O2
benzamide + glyoxylate + dehydroascorbate + H2O
-
-
-
?
hippuric acid + ferrocyanide + O2
alpha-hydroxyhippuric acid + ? + H2O
-
-
-
-
?
hippuryl-Gly + ascorbate + O2
?
-
-
-
?
hippuryl-Gly-Gly + ascorbate + O2
?
-
-
-
?
HOOC-NH-CH2-COOH + ascorbate + O2
?
-
substrate contains either protium or deuterium at the CH2-group
-
-
?
hydrocinnamoylglycine + ascorbate + O2
?
-
-
-
?
insulin + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
?
insulin glargine + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
?
isocaproylglycine + ascorbate + O2
?
-
-
-
?
L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
-
?
L-prolylglycine + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
-
?
L-pyroglutamyl-Gly + ascorbate + O2
?
-
-
-
?
leukotriene C4 + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
-
?
monoiodo-alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
monoiodo-alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
monoiodo-D-Tyr-Val-Gly + ascorbate + O2
monoiodo-D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
synthetic peptid
-
?
N-(2,4,6-trinitrophenyl)-D-Tyr-Val-Gly + ascorbate + O2
N-(2,4,6-trinitrophenyl)-D-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
-
?
N-(2-furoyl)glycine + ascorbate + O2
?
-
-
-
?
N-(2-thienylcarbonyl)glycine + ascorbate + O2
?
-
-
-
?
N-(4-amino-6-methyl-3-oxoheptanoyl)-L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
-
?
N-(4-amino-6-methyl-3-oxoheptanoyl)glycylglycine + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
-
?
N-(4-nitrobenzyl)glycine + ascorbate + O2
nitrobenzylamine + glyoxylate + dehydroascorbate + H2O
-
-
-
?
N-(alpha-methylhydrocinnamoyl)glycine + ascorbate + O2
?
-
-
-
?
N-(phenylacetyl)glycine + ascorbate + O2
?
-
-
-
?
N-(phenylacetyl)glycine + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
-
?
N-acetyl-Arg-Gly-Gly + ascorbate + O2
N-acetyl-Arg-Gly-hydroxyglycin + dehydroascorbate + H2O
-
-
-
-
?
N-acetyl-Gln-Lys-Glu-Ser-Thr-Leu-His-Leu-Val-Leu-Arg-Leu-Arg-Gly-Gly + ascorbate + O2
N-acetyl-Leu-Arg-Gly-hydroxyglycin + dehydroascorbate + H2O
-
-
-
-
?
N-acetyl-L-Phe-Gly + ascorbate + O2
N-acetyl-L-Phe-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
-
?
N-acetyl-L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
-
?
N-acetyl-Leu-Arg-Gly-Gly + ascorbate + O2
N-acetyl-Leu-Arg-Gly-hydroxyglycin + dehydroascorbate + H2O
-
-
-
-
?
N-acetyl-Leu-Arg-Leu-Arg-Gly-Gly + ascorbate + O2
N-acetyl-Leu-Arg-Gly-hydroxyglycin + dehydroascorbate + H2O
-
-
-
-
?
N-acetyl-Leu-His-Leu-Val-Leu-Arg-Leu-Arg-Gly-Gly + ascorbate + O2
N-acetyl-Leu-Arg-Gly-hydroxyglycin + dehydroascorbate + H2O
-
-
-
-
?
N-acetyl-Tyr-Val-Gly + ascorbate + O2
N-acetyl-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
-
?
N-acetylglycine + 2 ascorbate + O2
N-acetyl-2-hydroxyglycine + 2 semidehydroascorbate + H2O
-
-
-
-
?
N-acetylglycine + ascorbate + O2
?
-
-
-
?
N-acetylglycine + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
-
?
N-acetylglycine + ascorbate + O2
acetylamine + glyoxylate + dehydroascorbate + H2O
-
-
-
-
?
N-acetylglycine + ascorbate + O2
N-acetyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
-
?
N-acetylglycylglycine + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
-
?
N-benzoylglycine + ascorbate + O2
N-benzoyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
-
?
N-butyrylglycine + 2 ascorbate + O2
N-butyryl-2-hydroxyglycine + 2 semidehydroascorbate + H2O
-
-
-
-
?
N-Dan-Tyr-Val-Gly + ascorbate + O2
N-Dan-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
N-DANSYL-D-Tyr-L-Val-Gly + ascorbate + O2
N-DANSYL-D-Tyr-L-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
-
?
N-dansyl-L-Tyr-L-Phe-Gly + ascorbate + O2
N-dansyl-L-Tyr-L-Phe-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
-
r
N-dansyl-L-Tyr-L-Val-Gly + ascorbate + O2
N-dansyl-L-Tyr-L-Val-2-hydroxyglycine + dehydroascorbate + H2O
N-dansyl-Tyr-Val-D-Ala + ascorbate + O2
?
-
-
-
?
N-dansyl-Tyr-Val-Gly + ascorbate + O2
(S)-N-dansyl-Tyr-Val-alpha-hydroxyglycine + dehydroascorbate + H2O
-
-
-
ir
N-dansyl-Tyr-Val-Gly + ascorbate + O2
N-dansyl-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
N-decanoylglycine + 2 ascorbate + O2
N-decanoyl-2-hydroxyglycine + 2 semidehydroascorbate + H2O
-
-
-
-
?
N-decanoylglycine + ascorbate + O2
?
-
-
-
-
?
N-decanoylglycine + ascorbate + O2
decanoylamine + glyoxylate + dehydroascorbate + H2O
-
-
-
-
?
N-hexanoylglycine + 2 ascorbate + O2
N-hexanoyl-2-hydroxyglycine + 2 semidehydroascorbate + H2O
-
-
-
-
?
N-hexanoylglycine + ascorbate + O2
hexanoylamine + glyoxylate + dehydroascorbate + H2O
-
-
-
-
?
N-octanoylglycine + 2 ascorbate + O2
N-octanoyl-2-hydroxyglycine + 2 semidehydroascorbate + H2O
-
-
-
-
?
N-propionylglycine + 2 ascorbate + O2
N-propionyl-2-hydroxyglycine + 2 semidehydroascorbate + H2O
-
-
-
-
?
N-trifluoroacetylglycine + ascorbate + O2
N-trifluoroacetyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
-
?
N-trinitrophenyl-D-Tyr-Val-Gly + ascorbate + O2
N-trinitrophenyl-D-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
N-trinitrophenyl-D-Tyr-Val-Gly + ascorbate + O2
N-trinitrophenyl-D-Tyr-Val-NH2 + glyoxylate + dehydroascorbate + H2O
-
synthetic substrate
-
-
?
N-[(2-phenylcyclopropyl)carbonyl]glycine + ascorbate + O2
N-[(2-phenylcyclopropyl)carbonyl]-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
r
N-[(benzylmercapto)carbonyl]glycine + ascorbate + O2
?
-
-
-
?
N-[(phenylcyclopropyl)carbonyl]glycine + ascorbate + O2
?
-
-
-
?
N-[3-(1-leucylpyrrolidin-2-yl)-3-oxopropanoyl]-L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
-
?
N-[3-(1-leucylpyrrolidin-2-yl)-3-oxopropanoyl]glycylglycine + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
-
?
nicotinuric acid + ascorbate + O2
?
-
-
-
?
O-acetyl-L-mandelyl-Gly + ascorbate + O2
O-acetyl-L-mandelyl-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
-
?
oxytoxin + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
?
peptidyl-glycine + ascorbate + O2
peptidyl-(2-hydroxylglycine) + dehydroascorbate + H2O
peptidylglycine + 2 ascorbate + O2
peptidyl(2-hydroxyglycine) + 2 semidehydroascorbate + H2O
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl (S)-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl alpha-hydroxyglycine + semidehydroascorbate + H2O
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxylglycine) + dehydroascorbate + H2O
-
peptidylglycine alpha-hydroxylating monooxygenase reaction
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
Phe-Gly-Phe-Gly + ascorbate + O2
Phe-Gly-Phe-(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
-
?
Phe-Gly-Phe-Gly + ascorbate + O2
Phe-Gly-Phe-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
phenylhydantoic acid + ascorbate + O2
?
-
-
-
?
phenylmercaptoacetylglycine + ascorbate + O2
?
-
-
-
?
phenylthioacetylglycine + ascorbate + O2
?
-
-
-
?
proopiomelanocortin peptide + ascorbate + O2
proopiomelanocortin peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
R-CO-NH-CH2-COOH + ascorbate + O2
R-CO-NH2 + CHO-COOH + dehydroascorbate + H2O
S-(1,2-dicarboxyethyl)-glutathione + ascorbate + O2
S-(1,2-dicarboxyethyl)-gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
-
-
-
-
?
S-(4-nitrobenzyl)-glutathione + ascorbate + O2
S-(4-nitrobenzyl)-gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
-
-
-
-
?
S-butyl-glutathione + ascorbate + O2
S-butyl-gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
-
-
-
-
?
S-decyl-glutathione + ascorbate + O2
S-decyl-gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
-
-
-
-
?
S-ethyl-glutathione + ascorbate + O2
S-ethyl-gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
-
-
-
-
?
S-hexyl-glutathione + ascorbate + O2
S-hexyl-gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
-
-
-
-
?
S-methyl-glutathione + ascorbate + O2
S-methyl-gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
-
-
-
-
?
S-octyl-glutathione + ascorbate + O2
S-octyl-gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
-
-
-
-
?
S-propyl-glutathione + ascorbate + O2
S-propyl-gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
-
-
-
-
?
substance P + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
?
tBOC-Gly + ascorbate + O2
?
-
-
-
?
tBOC-Gly-Gly + ascorbate + O2
?
-
-
-
?
thyrotropin + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
?
trinitrophenyl-D-Tyr-Val-Gly + ascorbate + O2
?
-
activity assay
-
-
?
trinitrophenyl-D-Tyr-Val-Gly + ascorbate + O2
trinitrophenyl-D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
COOH-terminal glycine
-
-
?
ubiquitin + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
-
?
[(4-nitrobenzyl)oxy]acetic acid + ascorbate + O2
nitrobenzyl alcohol + glyoxylate + dehydroascorbate + H2O
-
-
-
?
additional information
?
-
acetyl-L-Tyr-L-Phe-Gly + ascorbate + O2
acetyl-L-Tyr-L-Phe-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
-
r
acetyl-L-Tyr-L-Phe-Gly + ascorbate + O2
acetyl-L-Tyr-L-Phe-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
-
r
Ala-Ile-Gly-Val-Gly-Ala-Pro-Gly + ascorbate + O2
Ala-Ile-Gly-Val-Gly-Ala-Pro-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
Ala-Ile-Gly-Val-Gly-Ala-Pro-Gly + ascorbate + O2
Ala-Ile-Gly-Val-Gly-Ala-Pro-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
alpha-N-acetyl-adrenocorticotrophic hormone(1-14) + ascorbate + O2
alpha-N-acetyl-adrenocorticotrophic hormone(1-13)-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
alpha-N-acetyl-adrenocorticotrophic hormone(1-14) + ascorbate + O2
alpha-N-acetyl-adrenocorticotrophic hormone(1-13)-2-hydroxyglycine + dehydroascorbate + H2O
-
inhibitory substrate
-
r
alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
-
?
alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
chromogranin A + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
?
chromogranin A + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
?
chromogranin A + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
?
D-Tyr-Pro-Gly-Gly + ascorbate + O2
D-Tyr-Pro-Gly-2-hydroxyglycine + dehydroascorbate + H2O
-
synthetic peptide
-
?
D-Tyr-Pro-Gly-Gly + ascorbate + O2
D-Tyr-Pro-Gly-2-hydroxyglycine + dehydroascorbate + H2O
-
optimal activity in sulfonic acid buffers
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
synthetic peptid
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
synthetic peptid
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-NH2 + glyoxylate + dehydroascorbate + H2O
-
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-NH2 + glyoxylate + dehydroascorbate + H2O
-
synthetic substrate
-
-
?
dansyl-D-Tyr-Val-Gly + ascorbate + O2
dansyl-D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
-
?
dansyl-D-Tyr-Val-Gly + ascorbate + O2
dansyl-D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
-
?
dansyl-D-Tyr-Val-Gly + ascorbate + O2
dansyl-D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
dansyl-D-Tyr-Val-Gly + ascorbate + O2
dansyl-D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
stereospecific
-
-
?
dansyl-D-Tyr-Val-Gly + ascorbate + O2
dansyl-D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
-
?
dansyl-L-Tyr-L-Val-Gly + ascorbate + O2
?
-
-
-
-
?
dansyl-L-Tyr-L-Val-Gly + ascorbate + O2
?
-
-
-
-
?
dansyl-YVG-COOH + ascorbate + O2
dansyl-YV-NH2 + dehydroascorbate + H2O
-
-
-
-
?
dansyl-YVG-COOH + ascorbate + O2
dansyl-YV-NH2 + dehydroascorbate + H2O
-
-
-
-
?
hippuric acid + ascorbate + O2
? + dehydroascorbate + H2O
-
C-H bond cleavage is irreversible, protiated and dideuterated substrate
-
-
ir
hippuric acid + ascorbate + O2
? + dehydroascorbate + H2O
-
synthetic substrate
-
-
ir
hippuric acid + ascorbate + O2
alpha-hydroxyhippuric acid + dehydroascorbate + H2O
-
-
-
-
?
hippuric acid + ascorbate + O2
alpha-hydroxyhippuric acid + dehydroascorbate + H2O
-
i.e. N-benzoylglycine
-
?
hippuric acid + ascorbate + O2
alpha-hydroxyhippuric acid + dehydroascorbate + H2O
-
i.e. N-benzoylglycine
-
?
monoiodo-alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
monoiodo-alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
monoiodo-alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
monoiodo-alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
monoiodo-alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
monoiodo-alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
?
N-Dan-Tyr-Val-Gly + ascorbate + O2
N-Dan-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
the product is unstable and dismutates to N-Dan-Tyr-Val-NH2 and glyoxylate (EC4.3.2.5)
-
-
?
N-Dan-Tyr-Val-Gly + ascorbate + O2
N-Dan-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
PAM activity assay, the product is unstable and dismutates to N-Dan-Tyr-Val-NH2 and glyoxylate (EC4.3.2.5)
-
-
?
N-dansyl-L-Tyr-L-Val-Gly + ascorbate + O2
N-dansyl-L-Tyr-L-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
-
r
N-dansyl-L-Tyr-L-Val-Gly + ascorbate + O2
N-dansyl-L-Tyr-L-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
-
?
N-dansyl-L-Tyr-L-Val-Gly + ascorbate + O2
N-dansyl-L-Tyr-L-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
-
-
-
r
N-trinitrophenyl-D-Tyr-Val-Gly + ascorbate + O2
N-trinitrophenyl-D-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
N-trinitrophenyl-D-Tyr-Val-Gly + ascorbate + O2
N-trinitrophenyl-D-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
-
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
peptidyl-glycine + ascorbate + O2
peptidyl-(2-hydroxylglycine) + dehydroascorbate + H2O
-
-
-
-
?
peptidyl-glycine + ascorbate + O2
peptidyl-(2-hydroxylglycine) + dehydroascorbate + H2O
-
PHM catalyzes the stereospecific hydroxylation of the glycine alpha-carbon of all peptidylglycine substrates
-
-
?
peptidylglycine + ascorbate + O2
peptidyl alpha-hydroxyglycine + semidehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl alpha-hydroxyglycine + semidehydroascorbate + H2O
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
requirement for O2
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
peptidylglycine alpha-hydroxylating monooxygenase PHM reaction
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
requirement for O2
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
amidation of neurohormonal peptides
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
peptidylglycine alpha-hydroxylating monooxygenase reaction
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
most mammalian bioactive peptides possess a C-terminal amino acid amide moiety. Amidated peptides are produced in vivo by the enzymatic cleavage of a precursor with a C-terminal glycine residue. The enzyme catalyzes the key step in the oxidation of the glycine-extended precursors to the alpha-amidated peptide
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
peptidylglycine alpha-hydroxylating monooxygenase reaction
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
requirement for O2
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
requirement for O2
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
requirement for O2
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
requirement for O2
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
semidehydroascorbate
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
peptidylglycine alpha-hydroxylating monooxygenase reaction
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
2 Cu2+, A and B, are involved in the catalytic reaction
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
C-H bond cleavage is irreversible, activation of molecular O2 and of the C-H bond of the substrate, mechanism, reductive activation of Cu(II)-OOH to generate a reactive copper-oxo species
-
-
ir
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
formation of a CuIIM-OOH intermediate, intramolecular electron transfer
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
peptidylglycine alpha-hydroxylating monooxygenase reaction, diverse glycine derivatives or substitutes
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
the enzyme catalyzes the final reaction in the maturation of alpha-amidated peptide hormones
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
requirement for O2
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
diverse synthetic substrates with C-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
proopiomelanocortin peptide + ascorbate + O2
proopiomelanocortin peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
a POMC 18-kDa fragment
-
-
?
proopiomelanocortin peptide + ascorbate + O2
proopiomelanocortin peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
a POMC 18-kDa fragment, establishment of an assay method
-
-
?
proopiomelanocortin peptide + ascorbate + O2
proopiomelanocortin peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
a POMC 18-kDa fragment
-
-
?
proopiomelanocortin peptide + ascorbate + O2
proopiomelanocortin peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
a POMC 18-kDa fragment, establishment of an assay method
-
-
?
R-CO-NH-CH2-COOH + ascorbate + O2
R-CO-NH2 + CHO-COOH + dehydroascorbate + H2O
-
-
-
-
?
R-CO-NH-CH2-COOH + ascorbate + O2
R-CO-NH2 + CHO-COOH + dehydroascorbate + H2O
-
via hydroxylated reaction intermediates
-
-
?
additional information
?
-
-
EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PMH) and 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
-
?
additional information
?
-
-
EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PMH) and 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
-
?
additional information
?
-
-
acetyl-L-Phe-Gly, acetyl-L-Phe-L-Phe-Gly, or (S)-O-acetyl-mandelyl-Gly, and stereoisomers are alpha-hydroxylated but not alpha-amidated
-
-
?
additional information
?
-
-
PAM catalyzes: 1. sulfoxidation of e.g. (4-nitrobenzyl) thioacetic acid to the analogous sulfoxide, 2. amine N-dealkylation of e.g. N-(4-nitrobenzyl)glycine to 4-nitrobenzylamine and glyoxylate, 3. O-dealkylation of e.g. [(4-nitrobenzyl)oxy]acetic acid to 4-nitrobenzyl alcohol and glyoxylate, 4. transformation of hippuric acid and several ring-substituted derivatives to the corresponding benzoamides and glyoxylic acid
-
-
?
additional information
?
-
-
PAM carries out two functions, peptidyl alpha-hydroxylating monooxygenase and peptidylamido-glycolate lyase activities
-
-
?
additional information
?
-
-
PAM carries out two functions, peptidyl alpha-hydroxylating monooxygenase and peptidylamido-glycolate lyase activities
-
-
?
additional information
?
-
C-terminally amidation of a range of peptides by the copper-dependent enzyme, peptidylglycine alpha-amidating monooxygenase, PAM. PAM-dependent amidation of POMC peptides in AtT20 cells
-
-
?
additional information
?
-
enzyme is required for amidation of the C-terminus of neuropeptides
-
-
?
additional information
?
-
-
at alkaline pH spontaneous conversion
-
-
?
additional information
?
-
-
EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PMH) and 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
-
?
additional information
?
-
-
enzyme is required for amidation of autocrine growth factors causing proliferation in tumor cells
-
-
?
additional information
?
-
-
PHM replaces the pro-(S) hydrogen of the carboxy-terminal glycine with a hydroxyl group to form an alpha-hydroxyglycine intermediate
-
-
?
additional information
?
-
-
the enzyme peptidylglycine alpha-amidating monooxygenase consists of two subunits: peptidylglycine alpha-hydroxylating monooxygenase that initiates formation of a radical at a substrate's C-terminal glycine alpha-carbon to then give an alpha-hydroxylated glycine derivative, and peptidylamidoglycolate lyase which catalyzes cleavage of this hydroxyglycine intermediate to give the amidated product with consequent release of glyoxylate
-
-
?
additional information
?
-
C-terminally amidation of a range of peptides by the copper-dependent enzyme, peptidylglycine alpha-amidating monooxygenase, PAM
-
-
?
additional information
?
-
constitutive-like secretion of POMC products in recombinant enzyme-expressing cells
-
-
?
additional information
?
-
-
enzyme is involved in peptide posttranslational activation
-
-
?
additional information
?
-
-
PAM is the only enzyme capable of amidating peptides, amidated peptides are numerous
-
-
?
additional information
?
-
C-terminally amidation of a range of peptides by the copper-dependent enzyme, peptidylglycine alpha-amidating monooxygenase, PAM
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
specificity
-
-
?
additional information
?
-
-
cleavage of C-H bond in the second reaction step is irreversible
-
-
?
additional information
?
-
-
endorphins are inhibitory substrates
-
-
?
additional information
?
-
-
EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PMH) and 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
-
?
additional information
?
-
-
EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PMH) and 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
-
?
additional information
?
-
-
EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PMH) and 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
-
?
additional information
?
-
-
substrates are also physiologically relevant peptides related to alpha-melanotropine
-
-
?
additional information
?
-
-
tunneling of hydrogen ion, relatively flexible
-
-
?
additional information
?
-
-
cleavage of CN bond in N-acetylated glycines, R-CO-NH-CH2-COOH, e.g. found in neuropeptide prohormones, inhibition of the enzyme leads to a decrease in alpha-aminated peptide production and accumulation of glycine-extended precursors
-
-
?
additional information
?
-
-
enzyme catalyzes the biosynthesis of peptide hormones through radical cleavage of the C-terminal glycine residues of the corresponding prohormones
-
-
?
additional information
?
-
-
enzyme catalyzes the production of neurohormones and neurotransmitters
-
-
?
additional information
?
-
-
enzyme is involved in peptide posttranslational activation
-
-
?
additional information
?
-
-
enzyme is required for amidation of autocrine growth factors causing proliferation in tumor cells
-
-
?
additional information
?
-
-
enzyme might be involved in secretory vesicle budding and fusion in the cardiac ANP-secretory pathway
-
-
?
additional information
?
-
-
substrate specificity, cleavage of CN bond in N-acetylated glycines, R-CO-NH-CH2-COOH, e.g. found in neuropeptide prohormones
-
-
?
additional information
?
-
-
substrate specificity, effects of substitutions on the glycine substrate, overview
-
-
?
additional information
?
-
-
long distance electron-transfer mechanism between the two distant copper cations, a perfect fitting for a water bridge, molecular dynamics simulations using wild-type and mutant enzymes, overview
-
-
?
additional information
?
-
-
PAM is the rate-limiting enzyme for the generation of carboxy-terminal alpha-amidated neuropeptides
-
-
?
additional information
?
-
constitutive-like secretion of POMC products in recombinant enzyme-expressing cells
-
-
?
additional information
?
-
peptidylglycine alpha-hydroxylating monooxygenase (PHM) catalyzes stereospecific alpha-C hydroxylation of C-terminal glycines, the first step in the alpha-amidation of hormones, growth factors and neurotransmitters. The molecular oxygen-dependent reaction requires two equivalents of ascorbate as exogenous reductant, releasing water and semidehydroascorbate as byproducts
-
-
?
additional information
?
-
-
substrates are also physiologically relevant peptides related to alpha-melanotropine
-
-
?
additional information
?
-
-
substrates are also physiologically relevant peptides related to alpha-melanotropine
-
-
?
additional information
?
-
-
EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PMH) and 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
-
?
additional information
?
-
-
EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PMH) and 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
-
?
additional information
?
-
-
EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PMH) and 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
-
?
additional information
?
-
-
EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PMH) and 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
-
?
additional information
?
-
-
EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PMH) and 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
-
?
additional information
?
-
-
peptide alpha-amidation, enzyme is responsible for formation of peptide C-terminal amide
-
-
?
additional information
?
-
-
peptide alpha-amidation, the N-terminal substrate structure affects the interaction with the active site of the enzyme
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
calcitonin + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
?
glutathione + ascorbate + O2
gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
-
-
-
-
?
insulin + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
?
oxytoxin + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
?
peptidyl-glycine + ascorbate + O2
peptidyl-(2-hydroxylglycine) + dehydroascorbate + H2O
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl alpha-hydroxyglycine + semidehydroascorbate + H2O
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxylglycine) + dehydroascorbate + H2O
-
peptidylglycine alpha-hydroxylating monooxygenase reaction
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
proopiomelanocortin peptide + ascorbate + O2
proopiomelanocortin peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
R-CO-NH-CH2-COOH + ascorbate + O2
R-CO-NH2 + CHO-COOH + dehydroascorbate + H2O
-
-
-
-
?
substance P + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
?
thyrotropin + ascorbate + O2
? + dehydroascorbate + H2O
-
-
-
?
additional information
?
-
peptidylglycine + ascorbate + O2
peptidyl alpha-hydroxyglycine + semidehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl alpha-hydroxyglycine + semidehydroascorbate + H2O
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
amidation of neurohormonal peptides
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
most mammalian bioactive peptides possess a C-terminal amino acid amide moiety. Amidated peptides are produced in vivo by the enzymatic cleavage of a precursor with a C-terminal glycine residue. The enzyme catalyzes the key step in the oxidation of the glycine-extended precursors to the alpha-amidated peptide
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
peptidylglycine alpha-hydroxylating monooxygenase reaction
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
peptidylglycine alpha-hydroxylating monooxygenase reaction
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
the enzyme catalyzes the final reaction in the maturation of alpha-amidated peptide hormones
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
-
-
?
proopiomelanocortin peptide + ascorbate + O2
proopiomelanocortin peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
a POMC 18-kDa fragment
-
-
?
proopiomelanocortin peptide + ascorbate + O2
proopiomelanocortin peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
a POMC 18-kDa fragment
-
-
?
additional information
?
-
C-terminally amidation of a range of peptides by the copper-dependent enzyme, peptidylglycine alpha-amidating monooxygenase, PAM. PAM-dependent amidation of POMC peptides in AtT20 cells
-
-
?
additional information
?
-
enzyme is required for amidation of the C-terminus of neuropeptides
-
-
?
additional information
?
-
-
enzyme is required for amidation of autocrine growth factors causing proliferation in tumor cells
-
-
?
additional information
?
-
-
PHM replaces the pro-(S) hydrogen of the carboxy-terminal glycine with a hydroxyl group to form an alpha-hydroxyglycine intermediate
-
-
?
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C-terminally amidation of a range of peptides by the copper-dependent enzyme, peptidylglycine alpha-amidating monooxygenase, PAM
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constitutive-like secretion of POMC products in recombinant enzyme-expressing cells
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enzyme is involved in peptide posttranslational activation
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PAM is the only enzyme capable of amidating peptides, amidated peptides are numerous
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C-terminally amidation of a range of peptides by the copper-dependent enzyme, peptidylglycine alpha-amidating monooxygenase, PAM
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additional information
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cleavage of CN bond in N-acetylated glycines, R-CO-NH-CH2-COOH, e.g. found in neuropeptide prohormones, inhibition of the enzyme leads to a decrease in alpha-aminated peptide production and accumulation of glycine-extended precursors
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enzyme catalyzes the biosynthesis of peptide hormones through radical cleavage of the C-terminal glycine residues of the corresponding prohormones
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enzyme catalyzes the production of neurohormones and neurotransmitters
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enzyme is involved in peptide posttranslational activation
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enzyme is required for amidation of autocrine growth factors causing proliferation in tumor cells
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enzyme might be involved in secretory vesicle budding and fusion in the cardiac ANP-secretory pathway
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PAM is the rate-limiting enzyme for the generation of carboxy-terminal alpha-amidated neuropeptides
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constitutive-like secretion of POMC products in recombinant enzyme-expressing cells
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additional information
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peptide alpha-amidation, enzyme is responsible for formation of peptide C-terminal amide
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1988
Rattus norvegicus
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C-Terminal amide formation in peptide hormones
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Bos taurus
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Post-translational processing in Xenopus oocytes includes carboxyl-terminal amidation
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Tissue distribution and characterization of peptide C-terminal alpha-amidating activity in rat
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Novel substrates and inhibitors of peptidylglycine alpha-amidating monooxygenase
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Bos taurus
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Purification and characterization of a peptide C-terminal alpha-amidating enzyme from porcine atrium
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105
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1989
Sus scrofa
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Tajima, M.; Iida, T.; Yoshida, S.; Komatsu, K.; Namba, R.; Yanagi, M.; Noguchi, M.; Okamoto, H.
The reaction product of peptidylglycine alpha-amidating enzyme is a hydroxyl derivative at alpha-carbon of the carboxyl-terminal glycine
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1990
Equus caballus
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Scopsi, L.; Lee, R.; Gullo, M.; Collini, P.; Husten, E.J.; Eipper, B.A.
Peptidylglycine alpha-amidating monooxygenase in neuroendocrine tumors: its identification, characterization, quantification, and relation to the grade of morphologic differentiation, amidated peptide content, and granin immunocytochemistry
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6
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1998
Homo sapiens
-
brenda
Chikuma, T.; Kocha, T.; Hanaoka, K.; Kato, T.; Ishii, Y.; Tanaka, A.
Characterization of peptidylglycine alpha-amidating monooxygenase in bovine hypothalamus
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25
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Bos taurus
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Tissue-specific molecular diversity of amidating enzymes (peptidylglycine alpha-hydroxylating monooxygenase and peptidylhydroxyglycine N-C lyase) in Xenopus laevis
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Xenopus laevis
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Functional expression and characterization of a Xenopus laevis peptidylglycine alpha-amidating monooxygenase, AE-II, in insect-cell culture
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213
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Xenopus laevis
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Characterization of a Xenopus laevis skin peptidylglycine alpha-hydroxylating monooxygenase expressed in insect-cell culture
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Xenopus laevis
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Identification, purification, and characterization of the molecular forms of Aplysia californica peptidylglycine alpha-amidating enzyme
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Rattus norvegicus
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Characterization and regulation of peptidylglycine alpha-amidating monooxygenase (PAM) expression in H9c2 cardiac myoblasts
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Rattus norvegicus
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Structural and functional investigations on the role of zinc in bifunctional rat peptidylglycine alpha-amidating enzyme
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36
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1997
Rattus norvegicus (P14925)
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Reaction versus subsite stereospecificity of peptidylglycine alpha-monooxygenase and peptidylamidoglycolate lyase, the two enzymes involved in peptide amidation
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Bos taurus
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Characterization of a half-apo derivative of peptidylglycine monooxygenase. Insight into the reactivity of each active site copper
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2001
Rattus norvegicus
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Kinetic mechanism and intrinsic isotope effects for the peptidylglycine alpha-amidating enzyme reaction
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1998
Rattus norvegicus
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The catalytic role of the copper ligand H172 of peptidylglycine alpha-hydroxylating monooxygenase (PHM): a spectroscopic study of the H172A mutant
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2002
Rattus norvegicus
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Hydrogen tunneling in peptidylglycine alpha-hydroxylating monooxygenase
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Expression and characterization of human bifunctional peptidylglycine alpha-amidating monooxygenase
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Homo sapiens (P19021), Homo sapiens
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Glutathione, S-substituted glutathiones, and leukotriene C4 as substrates for peptidylglycine alpha-amidating monooxygenase
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Peptidylglycine-alpha-amidating monooxygenase activity and protein are lower in copper-deficient rats and suckling copper-deficient mice
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Oxygen and hydrogen isotope effects in an active site tyrosine to phenylalanine mutant of peptidylglycine alpha-hydroxylating monooxygenase: mechanistic implications
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Rattus norvegicus
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Mechanistic investigation of peptidylglycine alpha-hydroxylating monooxygenase via intrinsic tryptophan fluorescence and mutagenesis
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Rattus norvegicus
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Peptidyl-glycine alpha-amidating monooxygenase targeting and shaping of atrial secretory vesicles: inhibition by mutated N-terminal ProANP and PBA
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Dugesia japonica (Q4W7B5)
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Investigation of the pathway for inter-copper electron transfer in peptidylglycine alpha-amidating monooxygenase
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Rattus norvegicus
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Inhibition of peptidylglycine alpha-amidating monooxygenase by exploitation of factors affecting the stability and ease of formation of glycyl radicals
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Rattus norvegicus
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Oxygen activation by the noncoupled binuclear copper site in peptidylglycine alpha-hydroxylating monooxygenase. Reaction mechanism and role of the noncoupled nature of the active site
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Rattus norvegicus
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A new proposal for the mechanism of glycine hydroxylation as catalyzed by peptidylglycine alpha-hydroxylating monooxygenase (PHM)
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2004
Rattus norvegicus
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Sunman, J.A.; Foster, M.S.; Folse, S.L.; May, S.W.; Matesic, D.F.
Reversal of the transformed phenotype and inhibition of peptidylglycine alpha-monooxygenase in Ras-transformed cells by 4-phenyl-3-butenoic acid
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Homo sapiens
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Takahashi, K.; Satani, M.; Harada, S.; Noguchi, M.
Expression and characterization of frog peptidylglycine alpha-hydroxylating monooxygenase
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27
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Xenopus laevis
brenda
Bauman, A.T.; Jaron, S.; Yukl, E.T.; Burchfiel, J.R.; Blackburn, N.J.
pH Dependence of peptidylglycine monooxygenase. Mechanistic implications of Cu-methionine binding dynamics
Biochemistry
45
11140-11150
2006
Rattus norvegicus
brenda
Evans, J.P.; Blackburn, N.J.; Klinman, J.P.
The catalytic role of the copper ligand H172 of peptidylglycine alpha-hydroxylating monooxygenase: A kinetic study of the H172A mutant
Biochemistry
45
15419-15429
2006
Cricetulus griseus
brenda
Prohaska, J.R.; Broderius, M.
Plasma peptidylglycine alpha-amidating monooxygenase (PAM) and ceruloplasmin are affected by age and copper status in rats and mice
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Mus musculus, Rattus norvegicus
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Bos taurus
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The catalytic mechanism of peptidylglycine alpha-hydroxylating monooxygenase investigated by computer simulation
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Rattus norvegicus (P14925)
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Klinman, J.P.
The copper-enzyme family of dopamine b-monooxygenase and peptidylglycine a-hydroxylating monooxygenase: Resolving the chemical pathway for substrate hydroxylation
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Homo sapiens
brenda
Bauman, A.T.; Yukl, E.T.; Alkevich, K.; McCormack, A.L.; Blackburn, N.J.
The hydrogen peroxide reactivity of peptidylglycine monooxygenase supports a Cu(II)-superoxo catalytic intermediate
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281
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Rattus norvegicus
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Bauer, J.D.; Sunman, J.A.; Foster, M.S.; Thompson, J.R.; Ogonowski, A.A.; Cutler, S.J.; May, S.W.; Pollock, S.H.
Anti-inflammatory effects of 4-phenyl-3-butenoic acid and 5-(acetylamino)-4-oxo-6-phenyl-2-hexenoic acid methyl ester, potential inhibitors of neuropeptide bioactivation
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2007
Rattus norvegicus
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Driscoll, W.J.; Hill, D.; Smalstig, A.; Mueller, G.P.
Murine atrial HL-1 cells express highly active peptidylglycine alpha-amidating enzyme
Peptides
27
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Mus musculus
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Bauman, A.T.; Ralle, M.; Blackburn, N.J.
Large scale production of the copper enzyme peptidylglycine monooxygenase using an automated bioreactor
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2007
Rattus norvegicus
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Long distance electron-transfer mechanism in peptidylglycine alpha-hydroxylating monooxygenase: a perfect fitting for a water bridge
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Rattus norvegicus
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Mus musculus
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Imino-oxy acetic acid dealkylation as evidence for an inner-sphere alcohol intermediate in the reaction catalyzed by peptidylglycine alpha-hydroxylating monooxygenase
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Rattus norvegicus (P14925)
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Sharma, S.D.; Raghuraman, G.; Lee, M.S.; Prabhakar, N.R.; Kumar, G.K.
Intermittent hypoxia activates peptidylglycine alpha-amidating monooxygenase in rat brain stem via reactive oxygen species-mediated proteolytic processing
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2009
Rattus norvegicus
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Trendel, J.A.; Ellis, N.; Sarver, J.G.; Klis, W.A.; Dhananjeyan, M.; Bykowski, C.A.; Reese, M.D.; Erhardt, P.W.
Catalytically active peptidylglycine alpha-amidating monooxygenase in the media of androgen-independent prostate cancer cell lines
J. Biomol. Screen.
13
804-809
2008
Homo sapiens
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Bousquet-Moore, D.; Prohaska, J.R.; Nillni, E.A.; Czyzyk, T.; Wetsel, W.C.; Mains, R.E.; Eipper, B.A.
Interactions of peptide amidation and copper: Novel biomarkers and mechanisms of neural dysfunction
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2010
Mus musculus
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Langella, E.; Pierre, S.; Ghattas, W.; Giorgi, M.; Reglier, M.; Saviano, M.; Esposito, L.; Hardre, R.
Probing the peptidylglycine alpha-hydroxylating monooxygenase active site with novel 4-phenyl-3-butenoic acid based inhibitors
ChemMedChem
5
1568-1576
2010
Sus scrofa
brenda
Chufan, E.E.; Prigge, S.T.; Siebert, X.; Eipper, B.A.; Mains, R.E.; Amzel, L.M.
Differential reactivity between two copper sites in peptidylglycine alpha-hydroxylating monooxygenase
J. Am. Chem. Soc.
132
15565-15572
2010
Rattus norvegicus
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McIntyre, N.R.; Lowe, E.W.; Belof, J.L.; Ivkovic, M.; Shafer, J.; Space, B.; Merkler, D.J.
Evidence for substrate preorganization in the peptidylglycine alpha-amidating monooxygenase reaction describing the contribution of ground state structure to hydrogen tunneling
J. Am. Chem. Soc.
132
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2010
Rattus norvegicus
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Bousquet-Moore, D.; Mains, R.E.; Eipper, B.A.
Peptidylgycine alpha-amidating monooxygenase and copper: a gene-nutrient interaction critical to nervous system function
J. Neurosci. Res.
88
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2010
Mus musculus
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Foster, M.; Oldham, C.; May, S.
Looking glass mechanism-based inhibition of peptidylglycine alpha-amidating monooxygenase
Tetrahedron Asymmetry
22
283-293
2011
Xenopus laevis
-
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Handa, S.; Spradling, T.J.; Dempsey, D.R.; Merkler, D.J.
Production of the catalytic core of human peptidylglycine alpha-hydroxylating monooxygenase (hPHMcc) in Escherichia coli
Protein Expr. Purif.
84
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Homo sapiens (P19021), Homo sapiens
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Bauman, A.T.; Broers, B.A.; Kline, C.D.; Blackburn, N.J.
A copper-methionine interaction controls the pH-dependent activation of peptidylglycine monooxygenase
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2011
Homo sapiens
brenda
Kline, C.D.; Mayfield, M.; Blackburn, N.J.
HHM motif at the CuH-site of peptidylglycine monooxygenase is a pH-dependent conformational switch
Biochemistry
52
2586-2596
2013
Homo sapiens
brenda
Morris, K.M.; Cao, F.; Onagi, H.; Altamore, T.M.; Gamble, A.B.; Easton, C.J.
Prohormone-substrate peptide sequence recognition by peptidylglycine alpha-amidating monooxygenase and its reflection in increased glycolate inhibitor potency
Bioorg. Med. Chem. Lett.
22
7015-7018
2012
Homo sapiens
brenda
Otoikhian, A.; Barry, A.N.; Mayfield, M.; Nilges, M.; Huang, Y.; Lutsenko, S.; Blackburn, N.J.
Lumenal loop M672-P707 of the Menkes protein (ATP7A) transfers copper to peptidylglycine monooxygenase
J. Am. Chem. Soc.
134
10458-10468
2012
Mus musculus
brenda
Gaier, E.D.; Miller, M.B.; Ralle, M.; Aryal, D.; Wetsel, W.C.; Mains, R.E.; Eipper, B.A.
Peptidylglycine alpha-amidating monooxygenase heterozygosity alters brain copper handling with region specificity
J. Neurochem.
127
605-619
2013
Mus musculus
brenda
Cao, F.; Gamble, A.; Kim, H.; Onagi, H.; Gresser, M.; Kerr, J.; Easton, C.
Potent and selective inhibitors of human peptidylglycine alpha-amidating monooxygenase
MedChemComm
2
760-763
2011
Homo sapiens
-
brenda
Attenborough, R.M.; Hayward, D.C.; Kitahara, M.V.; Miller, D.J.; Ball, E.E.
A neural enzyme in nonbilaterian animals and algae: preneural origins for peptidylglycine alpha-amidating monooxygenase
Mol. Biol. Evol.
29
3095-3109
2012
Acropora millepora (J9QK52), Acropora millepora (J9QL63)
brenda
Ul-Hasan, S.; Burgess, D.M.; Gajewiak, J.; Li, Q.; Hu, H.; Yandell, M.; Olivera, B.M.; Bandyopadhyay, P.K.
Characterization of the peptidylglycine alpha-amidating monooxygenase (PAM) from the venom ducts of neogastropods, Conus bullatus and Conus geographus
Toxicon
74
215-224
2013
Conus geographus, Conus bullatus
brenda
Chauhan, S.; Kline, C.D.; Mayfield, M.; Blackburn, N.J.
Binding of copper and silver to single-site variants of peptidylglycine monooxygenase reveals the structure and chemistry of the individual metal centers
Biochemistry
53
1069-1080
2014
Rattus norvegicus (P14925)
brenda
Chauhan, S.; Hosseinzadeh, P.; Lu, Y.; Blackburn, N.J.
Stopped-flow studies of the reduction of the copper centers suggest a bifurcated electron transfer pathway in peptidylglycine monooxygenase
Biochemistry
55
2008-2021
2016
Rattus norvegicus (P14925)
brenda
Kline, C.D.; Blackburn, N.J.
Substrate-induced carbon monoxide reactivity suggests multiple enzyme conformations at the catalytic copper M-center of peptidylglycine monooxygenase
Biochemistry
55
6652-6661
2016
Rattus norvegicus (P14925)
brenda
Yoo, H.J.; Kim, M.; Kim, M.; Chae, J.S.; Lee, S.H.; Lee, J.H.
The peptidylglycine-alpha-amidating monooxygenase (PAM) gene rs13175330 A>G polymorphism is associated with hypertension in a Korean population
Hum. Genomics
11
29
2017
Homo sapiens (P19021)
brenda
Martin-Diaconescu, V.; Chacon, K.N.; Delgado-Jaime, M.U.; Sokaras, D.; Weng, T.C.; DeBeer, S.; Blackburn, N.J.
Kbeta valence to core X-ray emission studies of Cu(I) binding proteins with mixed methionine-histidine coordination. Relevance to the reactivity of the M- and H-sites of peptidylglycine monooxygenase
Inorg. Chem.
55
3431-3439
2016
Rattus norvegicus (P14925)
brenda
Vishwanatha, K.; Baeck, N.; Mains, R.E.; Eipper, B.A.
A histidine-rich linker region in peptidylglycine alpha-amidating monooxygenase has the properties of a pH sensor
J. Biol. Chem.
289
12404-12420
2014
Mus musculus (P97467)
brenda
Abad, E.; Rommel, J.B.; Kaestner, J.
Reaction mechanism of the bicopper enzyme peptidylglycine alpha-hydroxylating monooxygenase
J. Biol. Chem.
289
13726-13738
2014
Rattus norvegicus (P14925)
brenda
Bonnemaison, M.L.; Baeck, N.; Duffy, M.E.; Ralle, M.; Mains, R.E.; Eipper, B.A.
Adaptor protein-1 complex affects the endocytic trafficking and function of peptidylglycine alpha-amidating monooxygenase, a luminal cuproenzyme
J. Biol. Chem.
290
21264-21279
2015
Homo sapiens (P19021), Rattus norvegicus (P14925)
brenda
Simpson, P.D.; Eipper, B.A.; Katz, M.J.; Gandara, L.; Wappner, P.; Fischer, R.; Hodson, E.J.; Ratcliffe, P.J.; Masson, N.
Striking oxygen sensitivity of the peptidylglycine alpha-amidating monooxygenase (PAM) in neuroendocrine cells
J. Biol. Chem.
290
24891-24901
2015
Drosophila melanogaster (O01404), Homo sapiens (P19021), Mus musculus (P97467)
brenda
McIntyre, N.R.; Lowe, E.W.; Battistini, M.R.; Leahy, J.W.; Merkler, D.J.
Inactivation of peptidylglycine alpha-hydroxylating monooxygenase by cinnamic acid analogs
J. Enzyme Inhib. Med. Chem.
31
551-562
2016
Rattus norvegicus (P14925), Homo sapiens (P19021)
brenda
Zielinski, M.; Wojtowicz-Krawiec, A.; Mikiewicz, D.; Kesik-Brodacka, M.; Cecuda-Adamczewska, V.; Marciniak-Rusek, A.; Sokolowska, I.; Lukasiewicz, N.; Gurba, L.; Odrowaz-Sypniewski, M.; Baran, P.; Plucienniczak, G.; Plucienniczak, A.; Borowicz, P.; Szewczyk, B.
Expression of recombinant human bifunctional peptidylglycine alpha-amidating monooxygenase in CHO cells and its use for insulin analogue modification
Protein Expr. Purif.
119
102-109
2016
Homo sapiens (P19021)
brenda