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Information on EC 1.1.1.380 - L-gulonate 5-dehydrogenase for references in articles please use BRENDA:EC1.1.1.380
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EC Tree
IUBMB Comments The enzyme, characterized from the bacterium Halomonas elongata, participates in a pathway for L-gulonate degradation.
The enzyme appears in viruses and cellular organisms
Synonyms
HeGulDH, L-gulonate oxidoreductase, YjjN,
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L-gulonate oxidoreductase
HeGulDH
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L-gulonate oxidoreductase
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L-gulonate oxidoreductase
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L-gulonate oxidoreductase
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L-gulonate + NAD+ = D-fructuronate + NADH + H+
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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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L-galactonate + NAD+
D-tagaturonate + NADH + H+
preferred substrate
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L-gulonate + NAD+
D-fructuronate + NADH + H+
additional information
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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
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L-gulonate + NAD+
D-fructuronate + NADH + H+
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L-gulonate + NAD+
D-fructuronate + NADH + H+
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L-gulonate + NAD+
D-fructuronate + NADH + H+
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the enzyme participates in a pathway for L-gulonate degradation
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L-gulonate + NAD+
D-fructuronate + NADH + H+
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L-gulonate + NAD+
D-fructuronate + NADH + H+
the enzyme participates in a pathway for L-gulonate degradation
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L-gulonate + NAD+
D-fructuronate + NADH + H+
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L-gulonate + NAD+
D-fructuronate + NADH + H+
the enzyme participates in a pathway for L-gulonate degradation
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L-gulonate + NAD+
D-fructuronate + NADH + H+
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L-gulonate + NAD+
D-fructuronate + NADH + H+
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the enzyme participates in a pathway for L-gulonate degradation
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L-gulonate + NAD+
D-fructuronate + NADH + H+
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L-gulonate + NAD+
D-fructuronate + NADH + H+
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the enzyme participates in a pathway for L-gulonate degradation
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L-galactonate + NAD+
D-tagaturonate + NADH + H+
Q8XB60
preferred substrate
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L-gulonate + NAD+
D-fructuronate + NADH + H+
L-gulonate + NAD+
D-fructuronate + NADH + H+
Q8XB60
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L-gulonate + NAD+
D-fructuronate + NADH + H+
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the enzyme participates in a pathway for L-gulonate degradation
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L-gulonate + NAD+
D-fructuronate + NADH + H+
E1V4Y1
the enzyme participates in a pathway for L-gulonate degradation
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L-gulonate + NAD+
D-fructuronate + NADH + H+
E1V4Y1
the enzyme participates in a pathway for L-gulonate degradation
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L-gulonate + NAD+
D-fructuronate + NADH + H+
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the enzyme participates in a pathway for L-gulonate degradation
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L-gulonate + NAD+
D-fructuronate + NADH + H+
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the enzyme participates in a pathway for L-gulonate degradation
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additional information
no activity with NADP+
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NAD+
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Zn2+
required, zinc enzyme
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1.8
L-gulonate
pH 7.9, 25°C
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0.6
L-gulonate
pH 7.9, 25°C
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8
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assay at
8
with L-galactonate, recombinant enzyme
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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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UniProt
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UniProt
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additional information
the strain O157:H7 shows the ability to grow on L-galactonate as a sole carbon source
brenda
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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
the enzyme participates in a pathway for L-gulonate degradation
metabolism
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the enzyme participates in a pathway for L-gulonate degradation
metabolism
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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
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the enzyme participates in a pathway for L-gulonate degradation
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metabolism
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the enzyme participates in a pathway for L-gulonate degradation
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A0A1Y0YE20_BACLI
338
0
36358
TrEMBL
A0A1I9ZFZ9_9NOCA
338
0
36021
TrEMBL
A0A1Y0WKL8_BACIU
339
0
36845
TrEMBL
A0A1C6Z0E4_HAFAL
339
0
37093
TrEMBL
E1V4Y1_HALED
Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9)
340
0
36349
TrEMBL
A0A369QFU2_9BACT
384
0
41424
TrEMBL
A0A2H1INB7_BRELN
68
0
7432
TrEMBL
Q8XB60_ECO57
340
0
36376
TrEMBL
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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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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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recombinant His-tagged enzyme from Escherichia coli strain BL21(DH3) by nickel affinity chromatography
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gene yjjN, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DH3)
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transcription of yjjN is upregulated during growth on L-galactonate
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analysis
YjjN can be applied for a quantitative L-galactonate and L-gulonate detection in a coupled reaction with diaphorase
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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)
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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, Salmonella enterica subsp. enterica serovar Typhimurium LT2
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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)
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1.1.1.380 L-gulonate 5-dehydrogenase
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