Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S,S)-S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
first half-reaction is reversible, the second one is irreversible, enzyme does not react with the (R,S)-diastereomer of S-adenosyl-L-methionine
i.e. 7,8-diaminopelargonic acid
-
?
2,3-butanedione + (S)-(-)-1-phenylpropylamine
?
2,3-dihydroxypropanaldehyde + (S)-(-)-1-phenylethylamine
?
2,3-hexanedione + (S)-(-)-1-phenylethylamine
?
2,3-pentanedione + (S)-(-)-1-phenylethylamine
?
-
-
-
?
2-oxo-2-phenylacetaldehyde + (S)-(-)-1-phenylethylamine
?
-
-
-
?
benzaldehyde + (S)-(-)-1-phenylethylamine
propiophenone + ?
-
-
-
?
DL-lysine + 8-amino-7-oxononanoate
? + (7S,8R)-diaminononanoate
-
L-lysine is preferred
-
-
?
glyoxylate + (S)-(-)-1-phenylethylamine
?
-
-
-
?
hexanaldehyde + (S)-(-)-1-phenylethylamine
?
-
-
-
?
isobutyraldehyde + (S)-(-)-1-phenylethylamine
acetophenone + ?
molecular docking study
-
-
?
isobutyraldehyde + (S)-(-)-1-phenylpropylamine
acetophenone + ?
-
-
-
?
pimeloyl-[acyl-carrier protein] + L-alanine
8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
propanaldehyde + (S)-(-)-1-phenylethylamine
?
-
-
-
?
pyruvaldehyde + (S)-(-)-1-phenylethylamine
?
-
-
-
?
S-2-aminoethyl-L-cysteine + 8-amino-7-oxononanoate
? + (7S,8R)-diaminononanoate
-
-
-
-
?
S-adenosyl-(5')-3-methylthiopropylamine + 8-amino-7-oxononanoate
? + (7S,8R)-diaminononanoate
decarboxylated S-adenosyl-L-methionine is as reactive as S-adenosyl-L-methionine
-
-
r
S-adenosyl-L-methionine + (S)-8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
S-adenosyl-L-methionine + (S)-8-amino-7-oxononanoic acid
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 7,8-diketopelargonic acid
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
S-adenosyl-L-methionine + 7-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
S-adenosyl-L-methionine + sinefungin
S-adenosyl-4-methylthio-2-oxobutanoate + ?
additional information
?
-
2,3-butanedione + (S)-(-)-1-phenylpropylamine
?
-
-
-
?
2,3-butanedione + (S)-(-)-1-phenylpropylamine
?
-
-
-
?
2,3-butanedione + (S)-(-)-1-phenylpropylamine
?
-
-
-
?
2,3-butanedione + (S)-(-)-1-phenylpropylamine
?
-
-
-
?
2,3-butanedione + (S)-(-)-1-phenylpropylamine
?
-
-
-
?
2,3-dihydroxypropanaldehyde + (S)-(-)-1-phenylethylamine
?
-
-
-
?
2,3-dihydroxypropanaldehyde + (S)-(-)-1-phenylethylamine
?
-
-
-
?
2,3-dihydroxypropanaldehyde + (S)-(-)-1-phenylethylamine
?
-
-
-
?
2,3-dihydroxypropanaldehyde + (S)-(-)-1-phenylethylamine
?
-
-
-
?
2,3-dihydroxypropanaldehyde + (S)-(-)-1-phenylethylamine
?
-
-
-
?
2,3-hexanedione + (S)-(-)-1-phenylethylamine
?
-
-
-
?
2,3-hexanedione + (S)-(-)-1-phenylethylamine
?
-
-
-
?
2,3-hexanedione + (S)-(-)-1-phenylethylamine
?
-
-
-
?
2,3-hexanedione + (S)-(-)-1-phenylethylamine
?
-
-
-
?
2,3-hexanedione + (S)-(-)-1-phenylethylamine
?
-
-
-
?
pimeloyl-[acyl-carrier protein] + L-alanine
8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
-
-
-
?
pimeloyl-[acyl-carrier protein] + L-alanine
8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
-
-
-
?
S-adenosyl-L-methionine + (S)-8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
enzyme only uses (S)-8-amino-7-oxononanoate as substrate
-
-
?
S-adenosyl-L-methionine + (S)-8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
enzyme only uses (S)-8-amino-7-oxononanoate as substrate
-
-
?
S-adenosyl-L-methionine + 7,8-diketopelargonic acid
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 7,8-diketopelargonic acid
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
-
?
S-adenosyl-L-methionine + 7-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
1% of the activity of 8-amino-7-oxononanoate
-
-
?
S-adenosyl-L-methionine + 7-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
1% of the activity of 8-amino-7-oxononanoate
-
-
?
S-adenosyl-L-methionine + 7-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
S-adenosyl-4-methylthio-2-oxobutanoate may be decomposed nonenzymatically to form 5'-methylthioadenosine and 2-oxo-3-butenoic acid
?
S-adenosyl-L-methionine + 7-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
S-adenosyl-4-methylthio-2-oxobutanoate may be decomposed nonenzymatically to form 5'-methylthioadenosine and 2-oxo-3-butenoic acid
?
S-adenosyl-L-methionine + 7-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
synonym: 7,8-diaminopelargonic acid
?
S-adenosyl-L-methionine + 7-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
1% of the activity of 8-amino-7-oxononanoate
-
-
?
S-adenosyl-L-methionine + 7-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
1% of the activity of 8-amino-7-oxononanoate
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
enzyme is obligate catalyzing the second step in the biosynthesis of vitamin H, i.e. biotin
-
-
r
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
involved in the biosynthesis of biotin
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
second of 4 steps in the biosynthesis of vitamin H, i.e. biotin
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
second of 4 steps in the biosynthesis of vitamin H, i.e. biotin
-
-
r
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
first half-reaction is reversible, the second one is irreversible
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
stereospecific amination
-
-
r
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
the aminotransferase half-reaction is reversible, substrate binding structure
-
-
r
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
involved in the biosynthesis of biotin
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus
-
biotin synthesis
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus IAM 1257
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus IAM 1257
-
biotin synthesis
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus IAM 1257
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus IAM 1257
-
biotin synthesis
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus IAM 1257
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus IAM 1257
-
biotin synthesis
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
biotin synthesis
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
biotin synthesis
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
no substrates: S-adenosyl-L-ethionine, S-adenosyl-L-homocysteine, S-adenosyl-L-(2-4-methylthio)butyric acid, S-methyl-L-methionine, adenosine, methionine
S-adenosyl-4-methylthio-2-oxobutanoate may be decomposed nonenzymatically to form 5'-methylthioadenosine and 2-oxo-3-butenoic acid, synonym: 7,8-diaminopelargonic acid
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
transfer of alpha-amino group from S-adenosyl-L-methionine to KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
S-adenosyl-4-methylthio-2-oxobutanoate may be decomposed nonenzymatically to form 5'-methylthioadenosine and 2-oxo-3-butenoic acid
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
S-adenosyl-4-methylthio-2-oxobutanoate may be decomposed nonenzymatically to form 5'-methylthioadenosine and 2-oxo-3-butenoic acid
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
synonym: 7,8-diaminopelargonic acid
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
biotin synthesis
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
biotin synthesis
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
biotin synthesis
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
ping pong bi bi kinetic mechanism with strong substrate inhibition
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
biotin synthesis
-
-
?
S-adenosyl-L-methionine + sinefungin
S-adenosyl-4-methylthio-2-oxobutanoate + ?
-
-
-
?
S-adenosyl-L-methionine + sinefungin
S-adenosyl-4-methylthio-2-oxobutanoate + ?
-
-
-
?
additional information
?
-
no substrates: L-Asp, L-Glu, L-Met, L-Lys, S-adenosylhomocysteine, and 5'-deoxy-5'-methylthioadenosine
-
-
?
additional information
?
-
-
no substrates: L-Asp, L-Glu, L-Met, L-Lys, S-adenosylhomocysteine, and 5'-deoxy-5'-methylthioadenosine
-
-
?
additional information
?
-
the bifunctional enzyme catalyzes both diaminopelargonic acid aminotransferase and dethiobiotin synthetase reactions in vitro. In the course of the reaction, the diaminopelargonic acid intermediate is directly transferred from the diaminopelargonic acid aminotransferase active site to the dethiobiotin synthetase active site. The overall reaction is rate limited by the diaminopelargonic acid aminotransferase activity
-
-
?
additional information
?
-
-
the bifunctional enzyme catalyzes both diaminopelargonic acid aminotransferase and dethiobiotin synthetase reactions in vitro. In the course of the reaction, the diaminopelargonic acid intermediate is directly transferred from the diaminopelargonic acid aminotransferase active site to the dethiobiotin synthetase active site. The overall reaction is rate limited by the diaminopelargonic acid aminotransferase activity
-
-
?
additional information
?
-
the BIO3-BIO1 fusion protein is the sole protein form produced by the BIO3-BIO1 locus in Arabidopsis. The enzyme catalyzes both diaminopelargonic acid aminotransferase and dethiobiotin synthetase reactions in vitro. In the course of the reaction, the diaminopelargonic acid intermediate is directly transferred from the both diaminopelargonic acid aminotransferase active site to the dethiobiotin synthetase active site
-
-
?
additional information
?
-
-
the BIO3-BIO1 fusion protein is the sole protein form produced by the BIO3-BIO1 locus in Arabidopsis. The enzyme catalyzes both diaminopelargonic acid aminotransferase and dethiobiotin synthetase reactions in vitro. In the course of the reaction, the diaminopelargonic acid intermediate is directly transferred from the both diaminopelargonic acid aminotransferase active site to the dethiobiotin synthetase active site
-
-
?
additional information
?
-
the BIO3-BIO1 fusion protein is the sole protein form produced by the BIO3-BIO1 locus in Arabidopsis. The enzyme catalyzes both diaminopelargonic acid aminotransferase and dethiobiotin synthetase reactions in vitro. In the course of the reaction, the diaminopelargonic acid intermediate is directly transferred from the both diaminopelargonic acid aminotransferase active site to the dethiobiotin synthetase active site. The enzyme exhibits a kinetic cooperativity with respect to all tested substrates and for both reactions
-
-
?
additional information
?
-
-
the BIO3-BIO1 fusion protein is the sole protein form produced by the BIO3-BIO1 locus in Arabidopsis. The enzyme catalyzes both diaminopelargonic acid aminotransferase and dethiobiotin synthetase reactions in vitro. In the course of the reaction, the diaminopelargonic acid intermediate is directly transferred from the both diaminopelargonic acid aminotransferase active site to the dethiobiotin synthetase active site. The enzyme exhibits a kinetic cooperativity with respect to all tested substrates and for both reactions
-
-
?
additional information
?
-
-
enzyme does not utilize S-adenosyl-L-methionine, Nalpha-acetyl-L-lysine, Nepsilon-acetyl-L-lysine, Nepsilon-methyl-L-lysine, glycine-lysine dipeptide, lysine-glycine dipeptide, and diaminopimelic acid as amino donors
-
-
?
additional information
?
-
the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis
-
-
-
additional information
?
-
the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis
-
-
-
additional information
?
-
the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis
-
-
-
additional information
?
-
the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis
-
-
-
additional information
?
-
the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis
-
-
-
additional information
?
-
the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis
-
-
-
additional information
?
-
the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis
-
-
-
additional information
?
-
7,8-diaminopelargonic acid transaminase (synthase), previously considered to be highly specific, is able to convert (S)-(-)-1-phenylethylamine and a number of aldehydes and diketones. Only a weak activity towards pyruvate is detected. The enzyme shows (S)-amine transaminase activity. The Pcryo361 affinity towards (S)-(-)-1-phenylethylamine arises from the recognition of the hydrophobic parts of the specific substrates, S-adenosyl-L-methionine and 7-keto-8-aminopelargonic acid, and from the flexibility of the active site. Analysis of the half-transamination reaction measuring a decrease in aldimine concentration in the presence of different concentrations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, L-lysine, and (S)-(-)-1,2-diaminopropane, substrate specificity of enzyme Pcryo361 in the half and the overall reactions, overview. No activity towards 2,4-pentanedione, 2-oxobutyrate, or acetone as amine acceptor substrates, poor activity with pyruvate, no activity with (R)-(-)-1-phenylethylamine as amine donor substrate
-
-
-
additional information
?
-
-
7,8-diaminopelargonic acid transaminase (synthase), previously considered to be highly specific, is able to convert (S)-(-)-1-phenylethylamine and a number of aldehydes and diketones. Only a weak activity towards pyruvate is detected. The enzyme shows (S)-amine transaminase activity. The Pcryo361 affinity towards (S)-(-)-1-phenylethylamine arises from the recognition of the hydrophobic parts of the specific substrates, S-adenosyl-L-methionine and 7-keto-8-aminopelargonic acid, and from the flexibility of the active site. Analysis of the half-transamination reaction measuring a decrease in aldimine concentration in the presence of different concentrations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, L-lysine, and (S)-(-)-1,2-diaminopropane, substrate specificity of enzyme Pcryo361 in the half and the overall reactions, overview. No activity towards 2,4-pentanedione, 2-oxobutyrate, or acetone as amine acceptor substrates, poor activity with pyruvate, no activity with (R)-(-)-1-phenylethylamine as amine donor substrate
-
-
-
additional information
?
-
7,8-diaminopelargonic acid transaminase (synthase), previously considered to be highly specific, is able to convert (S)-(-)-1-phenylethylamine and a number of aldehydes and diketones. Only a weak activity towards pyruvate is detected. The enzyme shows (S)-amine transaminase activity. The Pcryo361 affinity towards (S)-(-)-1-phenylethylamine arises from the recognition of the hydrophobic parts of the specific substrates, S-adenosyl-L-methionine and 7-keto-8-aminopelargonic acid, and from the flexibility of the active site. Analysis of the half-transamination reaction measuring a decrease in aldimine concentration in the presence of different concentrations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, L-lysine, and (S)-(-)-1,2-diaminopropane, substrate specificity of enzyme Pcryo361 in the half and the overall reactions, overview. No activity towards 2,4-pentanedione, 2-oxobutyrate, or acetone as amine acceptor substrates, poor activity with pyruvate, no activity with (R)-(-)-1-phenylethylamine as amine donor substrate
-
-
-
additional information
?
-
7,8-diaminopelargonic acid transaminase (synthase), previously considered to be highly specific, is able to convert (S)-(-)-1-phenylethylamine and a number of aldehydes and diketones. Only a weak activity towards pyruvate is detected. The enzyme shows (S)-amine transaminase activity. The Pcryo361 affinity towards (S)-(-)-1-phenylethylamine arises from the recognition of the hydrophobic parts of the specific substrates, S-adenosyl-L-methionine and 7-keto-8-aminopelargonic acid, and from the flexibility of the active site. Analysis of the half-transamination reaction measuring a decrease in aldimine concentration in the presence of different concentrations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, L-lysine, and (S)-(-)-1,2-diaminopropane, substrate specificity of enzyme Pcryo361 in the half and the overall reactions, overview. No activity towards 2,4-pentanedione, 2-oxobutyrate, or acetone as amine acceptor substrates, poor activity with pyruvate, no activity with (R)-(-)-1-phenylethylamine as amine donor substrate
-
-
-
additional information
?
-
7,8-diaminopelargonic acid transaminase (synthase), previously considered to be highly specific, is able to convert (S)-(-)-1-phenylethylamine and a number of aldehydes and diketones. Only a weak activity towards pyruvate is detected. The enzyme shows (S)-amine transaminase activity. The Pcryo361 affinity towards (S)-(-)-1-phenylethylamine arises from the recognition of the hydrophobic parts of the specific substrates, S-adenosyl-L-methionine and 7-keto-8-aminopelargonic acid, and from the flexibility of the active site. Analysis of the half-transamination reaction measuring a decrease in aldimine concentration in the presence of different concentrations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, L-lysine, and (S)-(-)-1,2-diaminopropane, substrate specificity of enzyme Pcryo361 in the half and the overall reactions, overview. No activity towards 2,4-pentanedione, 2-oxobutyrate, or acetone as amine acceptor substrates, poor activity with pyruvate, no activity with (R)-(-)-1-phenylethylamine as amine donor substrate
-
-
-
additional information
?
-
7,8-diaminopelargonic acid transaminase (synthase), previously considered to be highly specific, is able to convert (S)-(-)-1-phenylethylamine and a number of aldehydes and diketones. Only a weak activity towards pyruvate is detected. The enzyme shows (S)-amine transaminase activity. The Pcryo361 affinity towards (S)-(-)-1-phenylethylamine arises from the recognition of the hydrophobic parts of the specific substrates, S-adenosyl-L-methionine and 7-keto-8-aminopelargonic acid, and from the flexibility of the active site. Analysis of the half-transamination reaction measuring a decrease in aldimine concentration in the presence of different concentrations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, L-lysine, and (S)-(-)-1,2-diaminopropane, substrate specificity of enzyme Pcryo361 in the half and the overall reactions, overview. No activity towards 2,4-pentanedione, 2-oxobutyrate, or acetone as amine acceptor substrates, poor activity with pyruvate, no activity with (R)-(-)-1-phenylethylamine as amine donor substrate
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
the enzyme belongs to class III of the superfamily of aminotransferases (transaminase, TA)
evolution
-
the enzyme belongs to class III of the superfamily of aminotransferases (transaminase, TA)
-
evolution
-
the enzyme belongs to class III of the superfamily of aminotransferases (transaminase, TA)
-
evolution
-
the enzyme belongs to class III of the superfamily of aminotransferases (transaminase, TA)
-
evolution
-
the enzyme belongs to class III of the superfamily of aminotransferases (transaminase, TA)
-
malfunction
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT-deleted GAD strain NCgl2515 remains unaltered when pH is maintained at pH 7.5-8.0, demonstrating that GABA decomposition is reduced
malfunction
-
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT-deleted GAD strain NCgl2515 remains unaltered when pH is maintained at pH 7.5-8.0, demonstrating that GABA decomposition is reduced
-
malfunction
-
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT-deleted GAD strain NCgl2515 remains unaltered when pH is maintained at pH 7.5-8.0, demonstrating that GABA decomposition is reduced
-
malfunction
-
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT-deleted GAD strain NCgl2515 remains unaltered when pH is maintained at pH 7.5-8.0, demonstrating that GABA decomposition is reduced
-
malfunction
-
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT-deleted GAD strain NCgl2515 remains unaltered when pH is maintained at pH 7.5-8.0, demonstrating that GABA decomposition is reduced
-
malfunction
-
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT-deleted GAD strain NCgl2515 remains unaltered when pH is maintained at pH 7.5-8.0, demonstrating that GABA decomposition is reduced
-
malfunction
-
deletion of the gabT gene encoding GABA-T cannot prevent GABA from decomposing at neutral pH. An additional transaminase gene, NCgl2515, is deleted in a gabT-deleted GAD strain, but the GABA concentration in this gabT-deleted GAD strain NCgl2515 remains unaltered when pH is maintained at pH 7.5-8.0, demonstrating that GABA decomposition is reduced
-
metabolism
enzyme 7,8-diaminopelargonic acid aminotransferase (BioA) in Mycobacterium tuberculosis is primarily involved in the lipid biosynthesis pathway
metabolism
unlike GabT (EC 2.6.1.19), which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH), GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
metabolism
-
unlike GabT (EC 2.6.1.19), which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH), GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
-
metabolism
-
unlike GabT (EC 2.6.1.19), which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH), GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
-
metabolism
-
unlike GabT (EC 2.6.1.19), which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH), GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
-
metabolism
-
enzyme 7,8-diaminopelargonic acid aminotransferase (BioA) in Mycobacterium tuberculosis is primarily involved in the lipid biosynthesis pathway
-
metabolism
-
unlike GabT (EC 2.6.1.19), which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH), GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
-
metabolism
-
enzyme 7,8-diaminopelargonic acid aminotransferase (BioA) in Mycobacterium tuberculosis is primarily involved in the lipid biosynthesis pathway
-
metabolism
-
unlike GabT (EC 2.6.1.19), which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH), GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
-
metabolism
-
unlike GabT (EC 2.6.1.19), which exhibits high GABA-T activity and utilizes only 2-oxoglutarate as amino acceptor, the purified NCgl2515 protein exhibits very low GABA-T activity only when coupled with succinate-semialdehyde dehydrogenase (SSADH), GabD, but can utilize both 2-oxoglutarate and pyruvate as amino acceptor
-
additional information
the conversion of amines is a promiscuous activity of many transaminases of class III and is independent from their natural function. Molecular docking calculations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, and its quinonoid intermediates in the active site of the enzyme
additional information
-
the conversion of amines is a promiscuous activity of many transaminases of class III and is independent from their natural function. Molecular docking calculations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, and its quinonoid intermediates in the active site of the enzyme
additional information
-
the conversion of amines is a promiscuous activity of many transaminases of class III and is independent from their natural function. Molecular docking calculations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, and its quinonoid intermediates in the active site of the enzyme
-
additional information
-
the conversion of amines is a promiscuous activity of many transaminases of class III and is independent from their natural function. Molecular docking calculations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, and its quinonoid intermediates in the active site of the enzyme
-
additional information
-
the conversion of amines is a promiscuous activity of many transaminases of class III and is independent from their natural function. Molecular docking calculations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, and its quinonoid intermediates in the active site of the enzyme
-
additional information
-
the conversion of amines is a promiscuous activity of many transaminases of class III and is independent from their natural function. Molecular docking calculations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, and its quinonoid intermediates in the active site of the enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Izumi, Y.; Tani, Y.; Ogata, K.
Microbiological biosynthesis of biotin
Methods Enzymol.
62
326-338
1979
Bacillus roseus, Corynebacterium glutamicum, Kocuria rosea, Salmonella enterica subsp. enterica serovar Typhimurium, Bacillus roseus IAM 1257
brenda
Stoner, G.L.; Eisenberg, M.A.
Purification and properties of 7,8-diaminopelargonic acid aminotransferase
J. Biol. Chem.
250
4029-4036
1975
Escherichia coli
brenda
Izumi, Y.; Sato, K.; Tani, Y.; Ogata, K.
Biosynthesis of biotin by microorganisms. XV. 7,8-Diaminopelargonic acid aminotransferase, an enzyme involved in biotin biosynthesis by microorganisms
Agric. Biol. Chem.
39
175-181
1975
Bacillus roseus, Corynebacterium glutamicum, Escherichia coli, Kocuria rosea, Salmonella enterica subsp. enterica serovar Typhimurium, Escherichia coli AKV 0015, Corynebacterium glutamicum NRRL 2311, Bacillus roseus IAM 1257
-
brenda
Izumi, Y.; Sato, K.; Tani, Y.; Ogata, K.
7,8-Diaminopelargonic acid aminotransferase, an enzyme involved in biotin biosynthesis by microorganisms
Agric. Biol. Chem.
37
2683-2684
1973
Bacillus roseus, Corynebacterium glutamicum, Escherichia coli, Kocuria rosea, Salmonella enterica subsp. enterica serovar Typhimurium, Bacillus roseus IAM 1257
-
brenda
Stoner, G.L.; Eisenberg, M.A.
Biosynthesis of 7,8-diaminopelargonic acid from 7-keto-8-aminopelargonic acid and S-adenosyl-L-methionine. The kinetics of the reaction
J. Biol. Chem.
250
4037-4043
1975
Corynebacterium glutamicum, Escherichia coli, Corynebacterium glutamicum NRRL 2311
brenda
Eisenberg, M.A.; Stoner, G.L.
7,8-Diaminopelargonic acid aminotransferase
Methods Enzymol.
62
342-347
1979
Escherichia coli
brenda
Eliot, A.C.; Sandmark, J.; Schneider, G.; Kirsch, J.F.
The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation
Biochemistry
41
12582-12589
2002
Escherichia coli
brenda
Kck, H.; Gibson, K.J.; Gatenby, A.A.; Schneider, G.; Lindqvist, Y.
Purification and preliminary x-ray crystallographic studies of recombinant 7,8-diaminopelargonic acid synthase from Escherichia coli
Acta Crystallogr. Sect. D
54
1397-1398
1998
Escherichia coli
brenda
Kck, H.; Sandmark, J.; Gibson, K.; Schneider, G.; Lindqvist, Y.
Crystal structure of diaminopelargonic acid synthase: evolutionary relationships between pyridoxal-5'-phosphate-dependent enzymes
J. Mol. Biol.
291
857-876
1999
Escherichia coli
brenda
Eliot, A.C.; Kirsch, J.F.
Avoiding the road less traveled: how the topology of enzyme-substrate complexes can dictate product selection
Acc. Chem. Res.
36
757-765
2003
Escherichia coli
brenda
Mann, S.; Marquet, A.; Ploux, O.
Inhibition of 7,8-diaminopelargonic acid aminotransferase by amiclenomycin and analogues
Biochem. Soc. Trans.
33
802-805
2005
Escherichia coli, Mycobacterium tuberculosis
brenda
Sandmark, J.; Eliot, A.C.; Famm, K.; Schneider, G.; Kirsch, J.F.
Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis
Biochemistry
43
1213-1222
2004
Escherichia coli (P12995), Escherichia coli
brenda
Van Arsdell, S.W.; Perkins, J.B.; Yocum, R.R.; Luan, L.; Howitt, C.L.; Chatterjee, N.P.; Pero, J.G.
Removing a bottleneck in the Bacillus subtilis biotin pathway: bioA utilizes lysine rather than S-adenosylmethionine as the amino donor in the KAPA-to-DAPA reaction
Biotechnol. Bioeng.
91
75-83
2005
Bacillus subtilis
brenda
Breen, R.S.; Campopiano, D.J.; Webster, S.; Brunton, M.; Watt, R.; Baxter, R.L.
The mechanism of 7,8-diaminopelargonate synthase; the role of S-adenosylmethionine as the amino donor
Org. Biomol. Chem.
1
3498-3499
2003
Escherichia coli
brenda
Mann, S.; Ploux, O.
7,8-Diaminoperlargonic acid aminotransferase from Mycobacterium tuberculosis, a potential therapeutic target. Characterization and inhibition studies
FEBS J.
273
4778-4789
2006
Mycobacterium tuberculosis, Mycobacterium tuberculosis (P9WQ81), Mycobacterium tuberculosis ATCC 25618 (P9WQ81)
brenda
Mann, S.; Colliandre, L.; Labesse, G.; Ploux, O.
Inhibition of 7,8-diaminopelargonic acid aminotransferase from Mycobacterium tuberculosis by chiral and achiral anologs of its substrate: biological implications
Biochimie
91
826-834
2009
Mycobacterium tuberculosis, Mycobacterium tuberculosis (P9WQ81), Mycobacterium tuberculosis ATCC 25618 (P9WQ81)
brenda
Dey, S.; Lane, J.M.; Lee, R.E.; Rubin, E.J.; Sacchettini, J.C.
Structural characterization of the Mycobacterium tuberculosis biotin biosynthesis enzymes 7,8-diaminopelargonic acid synthase and dethiobiotin synthetase
Biochemistry
49
6746-6760
2010
Mycobacterium tuberculosis (P9WQ80), Mycobacterium tuberculosis, Mycobacterium tuberculosis CDC 1551 (P9WQ80)
brenda
Mann, S.; Eveleigh, L.; Lequin, O.; Ploux, O.
A microplate fluorescence assay for DAPA aminotransferase by detection of the vicinal diamine 7,8-diaminopelargonic acid
Anal. Biochem.
432
90-96
2013
Mycobacterium tuberculosis, Mycobacterium tuberculosis (P9WQ81), Mycobacterium tuberculosis ATCC 25618 (P9WQ81)
brenda
Cobessi, D.; Dumas, R.; Pautre, V.; Meinguet, C.; Ferrer, J.L.; Alban, C.
Biochemical and structural characterization of the Arabidopsis bifunctional enzyme dethiobiotin synthetase-diaminopelargonic acid aminotransferase: evidence for substrate channeling in biotin synthesis
Plant Cell
24
1608-1625
2012
Arabidopsis thaliana (B0F481), Arabidopsis thaliana
brenda
Shi, C.; Aldrich, C.C.
Design and synthesis of potential mechanism-based inhibitors of the aminotransferase BioA involved in biotin biosynthesis
J. Org. Chem.
77
6051-6058
2012
Mycobacterium tuberculosis (P9WQ81), Mycobacterium tuberculosis ATCC 25618 (P9WQ81)
brenda
Dai, R.; Wilson, D.J.; Geders, T.W.; Aldrich, C.C.; Finzel, B.C.
Inhibition of Mycobacterium tuberculosis transaminase BioA by aryl hydrazines and hydrazides
ChemBioChem
15
575-586
2014
Mycobacterium tuberculosis (P9WQ81), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WQ81)
brenda
Dai, R.; Geders, T.W.; Liu, F.; Park, S.W.; Schnappinger, D.; Aldrich, C.C.; Finzel, B.C.
Fragment-based exploration of binding site flexibility in Mycobacterium tuberculosis BioA
J. Med. Chem.
58
5208-5217
2015
Mycobacterium tuberculosis (P9WQ81), Mycobacterium tuberculosis H37Rv (P9WQ81)
brenda
Billones, J.B.; Carrillo, M.C.; Organo, V.G.; Sy, J.B.; Clavio, N.A.; Macalino, S.J.; Emnacen, I.A.; Lee, A.P.; Ko, P.K.; Concepcion, G.P.
In silico discovery and in vitro activity of inhibitors against Mycobacterium tuberculosis 7,8-diaminopelargonic acid synthase (Mtb BioA)
Drug Des. Devel. Ther.
11
563-574
2017
Mycobacterium tuberculosis (A5U255), Mycobacterium tuberculosis (P9WQ81), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25177 (A5U255), Mycobacterium tuberculosis H37Rv (P9WQ81), Mycobacterium tuberculosis ATCC 25618 (P9WQ81)
brenda
Bezsudnova, E.Y.; Stekhanova, T.N.; Popinako, A.V.; Rakitina, T.V.; Nikolaeva, A.Y.; Boyko, K.M.; Popov, V.O.
Diaminopelargonic acid transaminase from Psychrobacter cryohalolentis is active towards (S)-(-)-1-phenylethylamine, aldehydes and alpha-diketones
Appl. Microbiol. Biotechnol.
102
9621-9633
2018
Psychrobacter cryohalolentis (Q1QDV8), Psychrobacter cryohalolentis, Psychrobacter cryohalolentis DSM 17306 (Q1QDV8), Psychrobacter cryohalolentis K5 (Q1QDV8), Psychrobacter cryohalolentis VKM B-2378 (Q1QDV8), Psychrobacter cryohalolentis ATCC BAA-1226 (Q1QDV8)
brenda
Shi, F.; Si, H.; Ni, Y.; Zhang, L.; Li, Y.
Transaminase encoded by NCgl2515 gene of Corynebacterium glutamicum ATCC13032 is involved in gamma-aminobutyric acid decomposition
Process Biochem.
55
55-60
2017
Corynebacterium glutamicum (P46395), Corynebacterium glutamicum LMG 3730 (P46395), Corynebacterium glutamicum BCRC 11384 (P46395), Corynebacterium glutamicum ATCC 13032 (P46395), Corynebacterium glutamicum JCM 1318 (P46395), Corynebacterium glutamicum NCIMB 10025 (P46395), Corynebacterium glutamicum DSM 20300 (P46395)
-
brenda