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Enzyme Nomenclature
Information on EC 1.1.1.380 - L-gulonate 5-dehydrogenase
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1.1.1.380 L-gulonate 5-dehydrogenaseIUBMB Comments
The enzyme, characterized from the bacterium Halomonas elongata, participates in a pathway for L-gulonate degradation.
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The enzyme appears in viruses and cellular organisms
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HeGulDH
L-gulonate oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-gulonate + NAD+ = D-fructuronate + NADH + H+
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-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
L-gulonate:NAD+ 5-oxidoreductase
The enzyme, characterized from the bacterium Halomonas elongata, participates in a pathway for L-gulonate degradation.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-galactonate + NAD+
D-tagaturonate + NADH + H+
preferred substrate
-
-
?
additional information
?
-
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
-
-
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
-
the enzyme participates in a pathway for L-gulonate degradation
-
-
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
the enzyme participates in a pathway for L-gulonate degradation
-
-
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
the enzyme participates in a pathway for L-gulonate degradation
-
-
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
-
-
-
-
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
-
the enzyme participates in a pathway for L-gulonate degradation
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-galactonate + NAD+
D-tagaturonate + NADH + H+
preferred substrate
-
-
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
-
the enzyme participates in a pathway for L-gulonate degradation
-
-
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
the enzyme participates in a pathway for L-gulonate degradation
-
-
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
the enzyme participates in a pathway for L-gulonate degradation
-
-
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
-
the enzyme participates in a pathway for L-gulonate degradation
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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
the strain O157:H7 shows the ability to grow on L-galactonate as a sole carbon source
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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 participates in a pathway for L-gulonate degradation
metabolism
-
the enzyme participates in a pathway for L-gulonate degradation
metabolism
the enzyme participates in a pathway for L-gulonate degradation
metabolism
the enzyme catalyzes the first step in the hexuronate catabolism in Escherichia coli, overview
metabolism
-
the enzyme participates in a pathway for L-gulonate degradation
-
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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). E1V4Y1_HALED
Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9)
340
0
36349
TrEMBL
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Wichelecki, D.; Vendiola, J.; Jones, A.; Al-Obaidi, N.; Almo, S.; Gerlt, J.
Investigating the physiological roles of low-efficiency D-mannonate and D-gluconate dehydratases in the enolase superfamily: Pathways for the catabolism of L-gulonate and L-idonate
Biochemistry
53
5692-5699
2014
Halomonas elongata (E1V4Y1), Halomonas elongata DSM 2581 (E1V4Y1)
brenda
Cooper, R.
The pathway for L-gulonate catabolism in Escherichia coli K-12 and Salmonella typhimurium LT-2
FEBS Lett.
115
63-67
1980
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
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)
brenda
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