Any feedback?
No. of entries
Information on EC 1.1.1.380 - L-gulonate 5-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.380
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.380 L-gulonate 5-dehydrogenase
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
showSynonyms
HeGulDH, L-gulonate oxidoreductase, YjjN, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HeGulDH
L-gulonate oxidoreductase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-gulonate + NAD+ = D-fructuronate + NADH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
MetaCyc
L-gulonate degradation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-galactonate + NAD+
D-tagaturonate + NADH + H+
Substrates: preferred substrate
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: -
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
-
Substrates: the enzyme participates in a pathway for L-gulonate degradation
Products: -
Products: -
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
Substrates: -
Products: -
Products: -
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
Substrates: the enzyme participates in a pathway for L-gulonate degradation
Products: -
Products: -
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
Substrates: -
Products: -
Products: -
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
Substrates: the enzyme participates in a pathway for L-gulonate degradation
Products: -
Products: -
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
Substrates: -
Products: -
Products: -
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
-
Substrates: the enzyme participates in a pathway for L-gulonate degradation
Products: -
Products: -
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-galactonate + NAD+
D-tagaturonate + NADH + H+
Substrates: preferred substrate
Products: -
Products: -
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
-
Substrates: the enzyme participates in a pathway for L-gulonate degradation
Products: -
Products: -
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
Substrates: -
Products: -
Products: -
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
Substrates: the enzyme participates in a pathway for L-gulonate degradation
Products: -
Products: -
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
Substrates: the enzyme participates in a pathway for L-gulonate degradation
Products: -
Products: -
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
-
Substrates: the enzyme participates in a pathway for L-gulonate degradation
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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 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
-
Please 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). E1V4Y1_HALED
Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9)
340
0
36349
TrEMBL
-
Q8XB60_ECO57
340
0
36376
TrEMBL
other Location (Reliability: 1)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DH3) by nickel affinity chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene yjjN, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DH3)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
EXTERNAL LINKS (specific for EC-Number 1.1.1.380)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
