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Information on EC 1.1.1.65 - pyridoxine 4-dehydrogenase

for references in articles please use BRENDA:EC1.1.1.65

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EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.1.1 With NAD⁺ or NADP⁺ as acceptor

1.1.1.65 pyridoxine 4-dehydrogenase

IUBMB Comments

Also oxidizes pyridoxine phosphate.

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1.1.1.65
pyridoxal
5'-phosphate
pyridoxamine
reductases
vitamers
salvage
pombe
voltage-gated
schizosaccharomyces
aldose
interconvertible

The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

Reaction Schemes

Synonyms

dehydrogenase, pyridoxol 4-, PL reductase, PL-red, pyridoxin dehydrogenase, pyridoxine dehydrogenase, pyridoxol dehydrogenase, show all synonyms

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SYNONYM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

dehydrogenase, pyridoxol 4-

PL reductase

PL-red

pyridoxin dehydrogenase

pyridoxine dehydrogenase

pyridoxol dehydrogenase

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

pyridoxine + NADP+ = pyridoxal + NADPH + H+

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REACTION TYPE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

oxidation

redox reaction

reduction

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PATHWAY SOURCE

PATHWAYS

KEGG

Microbial metabolism in diverse environments, Vitamin B6 metabolism

, Microbial metabolism in diverse environments

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SYSTEMATIC NAME

IUBMB Comments

pyridoxine:NADP+ 4-oxidoreductase

Also oxidizes pyridoxine phosphate.

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CAS REGISTRY NUMBER

COMMENTARY

9028-64-2

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SUBSTRATE

PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

Reversibility
r=reversible
ir=irreversible
?=not specified

2-nitrobenzaldehyde + NADPH

2-nitrobenzyl alcohol + NADP+

Schizosaccharomyces pombe

O14295

287236

pyridoxine + NADP+

pyridoxal + NADPH

2 entries

pyridoxine phosphate + NADP+

pyridoxal 5'-phosphate + NADPH

Saccharomyces cerevisiae

287235

pyridoxine + NADP+

pyridoxal + NADPH

Saccharomyces cerevisiae

pyridoxine is identical with pyridoxol, equilibrium lies far to the side of pyridoxol

287235

pyridoxine + NADP+

pyridoxal + NADPH

Schizosaccharomyces pombe

O14295

287236

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

pyridoxine + NADP+

pyridoxal + NADPH

2 entries

pyridoxine + NADP+

pyridoxal + NADPH

Saccharomyces cerevisiae

pyridoxine is identical with pyridoxol, equilibrium lies far to the side of pyridoxol

287235

pyridoxine + NADP+

pyridoxal + NADPH

Schizosaccharomyces pombe

O14295

287236

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

NADP+

Schizosaccharomyces pombe

O14295

287236

NADPH

Schizosaccharomyces pombe

O14295

287236

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

ZnCl2

Saccharomyces cerevisiae

0.1 mM: activation, 10 mM: inhibition

287235

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

CoCl2

Saccharomyces cerevisiae

287235

CuSO4

Saccharomyces cerevisiae

287235

MnCl2

Saccharomyces cerevisiae

287235

p-chloromercuriphenyl sulfonic acid

Saccharomyces cerevisiae

287235

SO32-

Saccharomyces cerevisiae

287235

ZnCl2

Saccharomyces cerevisiae

0.1 mM: activation, 10 mM: inhibition

287235

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.096

2-nitrobenzaldehyde

Schizosaccharomyces pombe

O14295

287236

0.02

NADP+

Saccharomyces cerevisiae

287235

0.002

NADPH

Saccharomyces cerevisiae

287235

0.9 - 1.6

pyridoxal

2 entries

pyridoxol

Saccharomyces cerevisiae

287235

0.9

pyridoxal

Schizosaccharomyces pombe

O14295

287236

1.6

pyridoxal

Saccharomyces cerevisiae

287235

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Saccharomyces cerevisiae

287235

6.5 - 7.5

Schizosaccharomyces pombe

O14295

for formation of pyridoxine

287236

7.5 - 8.5

Schizosaccharomyces pombe

O14295

for formation of pyridoxal

287236

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pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

5 - 8

Saccharomyces cerevisiae

at pH 5.0 and 8.0 about 50% of activity maximum

287235

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

Saccharomyces cerevisiae

287235

brenda

Schizosaccharomyces pombe

287236

O14295

Uniprot

brenda

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

41000

Schizosaccharomyces pombe

O14295

gel filtration

287236

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

purified enzyme very unstable but can be stabilized by low concentrations of various detergents such as Tween 40

Schizosaccharomyces pombe

O14295

287236

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

2 entries

Saccharomyces cerevisiae

287235

Schizosaccharomyces pombe

O14295

287236

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

expression in Escherichia coli

Schizosaccharomyces pombe

O14295

287236

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

287235

Holzer, H.; Schneider, S.

Purification and characterization of a TPN-dependent pyridoxol dehydrogenase from brewers yeast

Biochim. Biophys. Acta

71-76

1961

Saccharomyces cerevisiae

13715611

brenda

287236

Nakano, M.; Morita, T.; Yamamoto, T.; Sano, H.; Ashiuchi, M.; Masui, R.; Kuramitsu, S.; Toshiharu, Y.

Purification, molecular cloning, and catalytic activity of Schizosaccharomyces pombe pyridoxal reductase

J. Biol. Chem.

274

23185-23190

1999

Schizosaccharomyces pombe (O14295), Schizosaccharomyces pombe

10438489

brenda

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EXTERNAL LINKS (specific for EC-Number 1.1.1.65)

NCBI: PubMed, Protein, Nucleotide, Structure, Gene, OMIM

IUBMB Enzyme Nomenclature

UniProt

PDB

PROSITE Database of protein families and domains

InterPro (database of protein families, domains and functional sites)

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