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Information on EC 1.1.1.57 - fructuronate reductase
for references in articles please use BRENDA:EC1.1.1.57
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.57 fructuronate reductase
IUBMB Comments
Also reduces D-tagaturonate.
The enzyme appears in viruses and cellular organisms
showSynonyms
mannonate oxidoreductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-mannonate dehydrogenase
-
-
-
-
D-mannonate:NAD+ oxidoreductase
-
-
-
-
fructuronate reductase
-
-
-
-
mannonate oxidoreductase
-
-
-
-
mannonic dehydrogenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-mannonate + NAD+ = D-fructuronate + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
D-fructuronate degradation
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SYSTEMATIC NAME
IUBMB Comments
D-mannonate:NAD+ 5-oxidoreductase
Also reduces D-tagaturonate.
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CAS REGISTRY NUMBER
COMMENTARY
9028-44-8
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-mannonate + NADP+
D-fructuronate + NADPH
-
Substrates: 5% of activity compared with NAD+ as cofactor
Products: -
Products: -
r
D-altronate + NAD+
D-tagaturonate + NADH
-
Substrates: approximately equal activity towards both fructuronate and tagaturonate in the forward reaction, and towards D-mannonate and D-altronate in the reverse reaction
Products: -
Products: -
r
D-altronate + NAD+
D-tagaturonate + NADH
-
Substrates: D-tagaturonate and D-altronate are 20% as active as D-fructuronate and D-mannonate
Products: -
Products: -
r
D-mannonate + NAD+
D-fructuronate + NADH
-
Substrates: -
Products: -
Products: -
r
D-mannonate + NAD+
D-fructuronate + NADH
-
Substrates: involved in hexuronate pathway
Products: -
Products: -
r
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-mannonate + NAD+
D-fructuronate + NADH
-
Substrates: -
Products: -
Products: -
r
D-mannonate + NAD+
D-fructuronate + NADH
-
Substrates: involved in hexuronate pathway
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuribenzoate
-
complete inhibition at 0.005 mM, non-competive, Ki: 0.0001 mM
additional information
-
product inhibition with all products in forward and reverse reaction
-
additional information
-
product inhibition with all products in forward and reverse reaction
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). UXUB_THEMA
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
539
0
61432
Swiss-Prot
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
53
53
-
loss of activity, NADH, NADPH, fructuronate, tagaturonate, NAD+, mannonate and altronate protect against inactivation
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 10 mM sodium phosphate buffer, pH 7, no loss of activity of the purified enzyme within 3 weeks
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hickman, J.; Ashwell, G.
Uronic acid metabolism in bacteria. II Purification and properties of D-altronic acid and D-mannonic acid dehydrogenase in Escherichia coli
J. Biol. Chem.
235
1566-1570
1960
Escherichia coli
brenda
Portalier, R.; Stoeber, F.
D-Mannonate and D-altronate-NAD dehydrogenases from Escherichia coli
Methods Enzymol.
89
210-218
1982
Escherichia coli
brenda
Portalier, R.C.; Stoeber, F.R.
Colorimetric determinations of aldonate oxidoreductases of Escherichia coli K 12: applications
Biochim. Biophys. Acta
289
19-27
1972
Escherichia coli
brenda
Mandrand-Berthelot, M.A.; Lagarde, A.E.
Hit-and-run mechanism for D-glucuronate reduction catalyzed by D-mannonate:NAD oxidoreductase of Escherichia coli
Biochim. Biophys. Acta
483
6-23
1977
Escherichia coli
brenda
Portalier, R.C.
D-Mannonate: NAD-oxidoreductase from Escherichia coli K12. Kinetic studies of the enzymatic mechanism
Eur. J. Biochem.
30
220-233
1972
Escherichia coli
brenda
Portalier, R.C.; Stoeber, F.R.
D-Mannonate: NAD oxidoreductase from Escherichia coli K12. Purification, properties and specificity
Eur. J. Biochem.
26
290-300
1972
Escherichia coli
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.57)
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