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Information on EC 1.1.1.414 - L-galactonate 5-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.414
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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
1.1.1.414 L-galactonate 5-dehydrogenase
IUBMB Comments
The enzyme, reported from the human gut bacteria Escherichia coli and Bacteroides vulgatus, participates in an L-galactonate degradation pathway.
The enzyme appears in viruses and cellular organisms
showSynonyms
l-galactonate dehydrogenase, bvu0222, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Bvu0222
L-galactonate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-galactonate + NAD+ = D-tagaturonate + NADH + H+
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-galactonate:NAD+ 5-oxidoreductase
The enzyme, reported from the human gut bacteria Escherichia coli and Bacteroides vulgatus, participates in an L-galactonate degradation pathway.
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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
L-gulonate + NAD+
D-fructuronate + NADH + H+
Substrates: -
Products: -
Products: -
?
D-tagaturonate + NADH + H+
L-galactonate + NAD+
Substrates: -
Products: -
Products: -
?
D-tagaturonate + NADH + H+
L-galactonate + NAD+
Substrates: -
Products: -
Products: -
?
L-galactonate + NAD+
D-tagaturonate + NADH + H+
Substrates: preferred substrate
Products: -
Products: -
?
L-galactonate + NAD+
D-tagaturonate + NADH + H+
-
Substrates: the enzyme participates in an L-galactonate degradation pathway
Products: -
Products: -
?
L-galactonate + NAD+
D-tagaturonate + NADH + H+
-
Substrates: no activity with NADP+
Products: -
Products: -
?
L-galactonate + NAD+
D-tagaturonate + NADH + H+
Substrates: the enzyme participates in an L-galactonate degradation pathway
Products: -
Products: -
?
L-galactonate + NAD+
D-tagaturonate + NADH + H+
Substrates: -
Products: -
Products: -
?
L-galactonate + NAD+
D-tagaturonate + NADH + H+
Substrates: the enzyme participates in an L-galactonate degradation pathway
Products: -
Products: -
?
L-galactonate + NAD+
D-tagaturonate + NADH + H+
Substrates: -
Products: -
Products: -
?
L-gluconate + NAD+
?
Substrates: the value of kcat/Km for the oxidation of L-galactonate is 2 orders of magnitude greater than the oxidation of L-gluconate
Products: -
Products: -
?
L-gluconate + NAD+
?
Substrates: the value of kcat/Km for the oxidation of L-galactonate is 2 orders of magnitude greater than the oxidation of L-gluconate
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme YjjN is an L-galactonate 5-dehydrogenase having activity also for L-gulonate. Reaction product identification by GC/MS analysis. No activity with substrates of similar structure, L-fuconate and L-lyxonate. And no activity with L-mannonate, L-rhamnonate, D-gulonate, D-galacturonate, D-glucuronate, D-gluconate, D-lyxonate, D-xylonate, D-ribonate, D-arabonate, D-mannonate, D-erythronate, D-glucose, D-xylitol, D-sorbitol, glucooctanic acid, and meso-galactarate. The hydroxyl group at the C6 seems to be essential for the activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme YjjN is an L-galactonate 5-dehydrogenase having activity also for L-gulonate. Reaction product identification by GC/MS analysis. No activity with substrates of similar structure, L-fuconate and L-lyxonate. And no activity with L-mannonate, L-rhamnonate, D-gulonate, D-galacturonate, D-glucuronate, D-gluconate, D-lyxonate, D-xylonate, D-ribonate, D-arabonate, D-mannonate, D-erythronate, D-glucose, D-xylitol, D-sorbitol, glucooctanic acid, and meso-galactarate. The hydroxyl group at the C6 seems to be essential for the activity
Products: -
Products: -
?
additional information
?
-
Substrates: no oxidation of D-arabinonate and L-xylonate
Products: -
Products: -
?
additional information
?
-
-
Substrates: no oxidation of D-arabinonate and L-xylonate
Products: -
Products: -
?
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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
L-gulonate + NAD+
D-fructuronate + NADH + H+
Substrates: -
Products: -
Products: -
?
L-galactonate + NAD+
D-tagaturonate + NADH + H+
Substrates: preferred substrate
Products: -
Products: -
?
L-galactonate + NAD+
D-tagaturonate + NADH + H+
-
Substrates: the enzyme participates in an L-galactonate degradation pathway
Products: -
Products: -
?
L-galactonate + NAD+
D-tagaturonate + NADH + H+
Substrates: the enzyme participates in an L-galactonate degradation pathway
Products: -
Products: -
?
L-galactonate + NAD+
D-tagaturonate + NADH + H+
Substrates: the enzyme participates in an L-galactonate degradation pathway
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19.5
L-galactonate
pH 8.0, temperature not specified in the publication, recombinant enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.51
L-galactonate
pH 8.0, temperature not specified in the publication, recombinant enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
L-galactonate
pH 8.0, temperature not specified in the publication, recombinant enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 9
the optimum pH for the activity with L-galactonate is pH 8.0 while the remaining activity at pH 7.0, pH 7.5, and pH 9.0 is 73%, 97%, and 0 %, respectively
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
the strain O157:H7 shows the ability to grow on L-galactonate as a sole carbon source
brenda
additional information
-
the strain O157:H7 shows the ability to grow on L-galactonate as a sole carbon source
brenda
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.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
YjjN belongs to the zinc-containing alcohol dehydrogenase family. This protein family contains dimeric or tetrameric proteins that coordinate two zinc atoms per subunit. Four conserved cysteine residues, that coordinate the zinc atoms and an aspartate residue predicting NAD+ specificity are found from the YjjN sequence (C92, C95, C98, C106, and D193)
metabolism
metabolism
the enzyme catalyzes the first step in the hexuronate catabolism in Escherichia coli, overview
metabolism
the enzyme participates in an L-galactonate degradation pathway
metabolism
-
the enzyme participates in an L-galactonate degradation pathway
metabolism
-
the enzyme participates in an L-galactonate degradation pathway
-
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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). LGOD_ECOLI
Escherichia coli (strain K12)
340
0
36448
Swiss-Prot
other Location (Reliability: 1)
A6KWY5_PHOV8
Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC 11154)
339
0
36705
TrEMBL
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
up
-
the enzyme is present in cells grown on L-galactonate, or on glycerol plus L-galactonate, at specific activity of 0.00013 mM/min*mg protein, When the cells are grown on glycerol or galacturonate, no L-galactonate oxidoreductase activity can be detected, suggesting that it is an inducible enzyme
additional information
additional information
deletion of the gene results in a strain with the impaired ability to grow on L-galactonate as a sole carbon source
additional information
-
deletion of the gene results in a strain with the impaired ability to grow on L-galactonate as a sole carbon source
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified recombinant His-tagged enzyme, stability of enzyme YjjN seems to be rather poor since the activity of purified protein decreases dramatically when stored at 4°C overnight
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DH3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene yjjN, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DH3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
YjjN can be applied for a quantitative L-galactonate and L-gulonate detection in a coupled reaction with diaphorase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kuivanen, J.; Richard, P.
The yjjN of E. coli codes for an L-galactonate dehydrogenase and can be used for quantification of L-galactonate and L-gulonate
Appl. Biochem. Biotechnol.
173
1829-1835
2014
Escherichia coli (Q8XB60), Escherichia coli
brenda
Hobbs, M.E.; Williams, H.J.; Hillerich, B.; Almo, S.C.; Raushel, F.M.
L-Galactose metabolism in Bacteroides vulgatus from the human gut microbiota
Biochemistry
53
4661-4670
2014
Phocaeicola vulgatus (A6KWY5), Phocaeicola vulgatus, Phocaeicola vulgatus DSM 1447 (A6KWY5)
brenda
Cooper, R.
The pathway for L-galactonate catabolism in Escherichia coli K-12
FEBS Lett.
103
216-220
1979
Escherichia coli
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.414)
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