Information on EC 1.1.1.B62 - L-galactonate 5-dehydrogenase (NAD+)

for references in articles please use BRENDA:EC1.1.1.B62
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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
1.1.1.B62
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
L-galactonate 5-dehydrogenase (NAD+)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-galactonate + NAD+ = D-tagaturonate + NADH + H+
show the reaction diagram
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-
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SYSTEMATIC NAME
IUBMB Comments
L-galactonate:NAD+ 5-oxidoreductase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
the enzyme catalyzes the first step in the hexuronate catabolism in Escherichia coli, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-galactonate + NAD+
D-tagaturonate + NADH + H+
show the reaction diagram
preferred substrate
-
-
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
show the reaction diagram
-
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-galactonate + NAD+
D-tagaturonate + NADH + H+
show the reaction diagram
Q8XB60
preferred substrate
-
-
?
L-gulonate + NAD+
D-fructuronate + NADH + H+
show the reaction diagram
Q8XB60
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
required, zinc enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19.5
L-galactonate
pH 8.0, temperature not specified in the publication, recombinant enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.51
L-galactonate
pH 8.0, temperature not specified in the publication, recombinant enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
L-galactonate
pH 8.0, temperature not specified in the publication, recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
with L-galactonate, recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DH3) by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene yjjN, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DH3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcription of yjjN is upregulated during growth on L-galactonate
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
YjjN can be applied for a quantitative L-galactonate and L-gulonate detection in a coupled reaction with diaphorase