Information on EC 1.1.1.65 - pyridoxine 4-dehydrogenase

for references in articles please use BRENDA:EC1.1.1.65
Word Map on EC 1.1.1.65
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:

The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
1.1.1.65
-
top print hide
RECOMMENDED NAME
GeneOntology No.
pyridoxine 4-dehydrogenase
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
pyridoxine + NADP+ = pyridoxal + NADPH + H+
show the reaction diagram
-
-
-
-
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
top print hide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-amino-2-methyl-5-diphosphomethylpyrimidine biosynthesis (yeast)
-
-
pyridoxal 5'-phosphate salvage II (plants)
-
-
Vitamin B6 metabolism
-
-
Metabolic pathways
-
-
top print hide
SYSTEMATIC NAME
IUBMB Comments
pyridoxine:NADP+ 4-oxidoreductase
Also oxidizes pyridoxine phosphate.
top
top print hide
CAS REGISTRY NUMBER
COMMENTARY hide
9028-64-2
-
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
top print hide
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-nitrobenzaldehyde + NADPH
2-nitrobenzyl alcohol + NADP+
show the reaction diagram
-
-
-
?
pyridoxine + NADP+
pyridoxal + NADPH
show the reaction diagram
pyridoxine phosphate + NADP+
pyridoxal 5'-phosphate + NADPH
show the reaction diagram
-
-
-
-
-
top print hide
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
pyridoxine + NADP+
pyridoxal + NADPH
show the reaction diagram
top print hide
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
top print hide
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ZnCl2
-
0.1 mM: activation, 10 mM: inhibition
top print hide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
p-Chloromercuriphenyl sulfonic acid
-
-
ZnCl2
-
0.1 mM: activation, 10 mM: inhibition
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.096
2-nitrobenzaldehyde
-
0.9 - 1.6
pyridoxal
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
for formation of pyridoxine
7.5 - 8.5
for formation of pyridoxal
top print hide
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
-
at pH 5.0 and 8.0 about 50% of activity maximum
top print hide
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
gel filtration
top print hide
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme very unstable but can be stabilized by low concentrations of various detergents such as Tween 40
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
top
Show AA Sequence (195 entries)
Please use the Sequence Search for a specific query.
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.65)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)