Information on EC 1.1.1.301 - D-arabitol-phosphate dehydrogenase

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

D-arabitol 1-phosphate + NAD+

D-xylulose 5-phosphate + NADH + H+

additional information

D-arabitol 1-phosphate + NAD+

D-xylulose 5-phosphate + NADH + H+

Substrates: -
Products: -

D-arabitol 1-phosphate + NAD+

D-xylulose 5-phosphate + NADH + H+

Substrates: -
Products: -

additional information

Substrates: participates in arabitol catabolism via the arabitol phosphate route
Products: -

additional information

Substrates: participates in arabitol catabolism via the arabitol phosphate route
Products: -

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

NAD+

the rates of both reductive and oxidative reactions with NAD+ and NADH as cofactors are about 14 times higher than with NADP+ and NADPH

NADH

NADP+

the rates of both reductive and oxidative reactions with NAD+ and NADH as cofactors are about 14 times higher than with NADP+ and NADPH

NADPH

the rates of both reductive and oxidative reactions with NAD+ and NADH as cofactors are about 14 times higher than with NADP+ and NADPH

NADH

NADH

the rates of both reductive and oxidative reactions with NAD+ and NADH as cofactors are about 14 times higher than with NADP+ and NADPH

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Mn2+

required. Pure APDH contains 4.05 ions of Mn2+

additional information

additional information

no requirement for Zn2+

additional information

no requirement for Zn2+

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

EDTA

xylulose 5-phosphate does not protect the enzyme from EDTA inactivation. Addition of Mn2+ at concentrations of up to 2 mM results in complete reactivation of APDH

Hg2+

2 mM, complete inactivation

PHMB

2 mM, complete inactivation

Zn2+

2 mM, complete inactivation

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

2.9 - 3.6

D-arabitol 1-phosphate

0.63

D-arabitol 5-phosphate

20°C, pH 8.5, cofactor: NAD+

0.23 - 0.65

D-xylulose 5-phosphate

0.71 - 0.8

NAD+

0.021

NADH

20°C, pH 7.2, cosubstrate: D-xylulose 5-phosphate

2.7

NADP+

20°C, pH 8.5, cosubstrate: D-arabitol 1-phosphate

0.24

NADPH

20°C, pH 7.2, cosubstrate: D-xylulose 5-phosphate

2.9

D-arabitol 1-phosphate

20°C, pH 8.5, cofactor: NAD+

3.6

D-arabitol 1-phosphate

20°C, pH 8.5, cofactor: NADP+

0.23

D-xylulose 5-phosphate

20°C, pH 7.2, cofactor: NADH

0.65

D-xylulose 5-phosphate

20°C, pH 7.2, cofactor NADPH

0.71

NAD+

20°C, pH 8.5: cosubstrate: D-arabitol 5-phosphate

0.8

NAD+

20°C, pH 8.5, cosubstrate: D-arabitol 1-phosphate

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.05

crude extracts of Bacillus methanolicus cells grown on arabitol, pH 7.2, 30°C

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

6.8 - 7.4

reduction of D-xylulose 5-phosphate with NADH or NADPH

7.2

assay at

8.3 - 8.6

oxidation of D-arabitol 1-phosphate with NAD+ or NADP+

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay at

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pI VALUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

6.4

isoelectric focusing

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only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

brenda

brenda

SwissProt

brenda

brenda

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only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

culture condition:D-arabitol-grown cell

culture condition:D-arabitol-grown cell

D-arabitol is a carbon source of Bacillus methanolicus

culture condition:D-arabitol-grown cell

brenda

D-arabitol is a carbon source of Bacillus methanolicus

brenda

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

metabolism

metabolism

identification of genes coding for arabitol utilization pathway, overview. Bacillus methanolicus possesses an arabitol inducible operon encoding, amongst others, a putative PTS system and an arabitol phosphate dehydrogenase for uptake and activation of arabitol as growth substrate. Model of the pathways for arabitol catabolism in bacteria, overview

metabolism

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

160000

non-denaturing PAGE

41000

4 * 41000, SDS-PAGE

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

tetramer

4 * 41000, SDS-PAGE

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

Go to Cloned (commentary) Search

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

expression in Bacillus subtilis. Expression of the D-arabitol phosphate dehydrogenase gene of Enterococcus avium in the D-ribulose- and D-xylulose-producing strain results in a strain of Bacillus subtilis capable of converting D-glucose to D-arabitol with a high yield (28%) and little by-product formation

gene atlD, cloning of genes coding for arabitol utilization pathway, arabitol utilization genes are co-transcribed in an operon, a gene cluster comprising eight genes that is upregulated during growth with arabitol as a sole carbon source, transcriptional organization of the gene cluster, transcriptome sequencing, and real-time quantitative reverse transcription PCR enzyme expression analysis. Recombinant expression of atlD in Corynebacterium glutamicum strain ATCC 13032 mtlD deletion mutant complements the mutant and restores growth of the Corynebacterium glutamicum DELTAmtlD mutant with arabitol

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EXPRESSION

ORGANISM

UNIPROT

LITERATURE

the enzyme is induced by D-arabitol

the enzyme is induced by D-arabitol

the enzyme is induced by D-arabitol

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

biotechnology

expression of the D-arabitol phosphate dehydrogenase gene of Enterococcus avium in the D-ribulose- and D-xylulose-producing strain results in a strain of Bacillus subtilis capable of converting D-glucose to D-arabitol with a high yield (28%) and little by-product formation

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

Povelainen, M.; Eneyaskaya, E.V.; Kulminskaya, A.A.; Ivanen, D.R.; Kalkinnen, N.; Neustroev, K.N.; Miasnikov, A.N.

Biochemical and genetic characterization of a novel enzyme of pentitol metabolism: D-arabitol-phosphate dehydrogenase

Biochem. J.

371

191-197

2003

Enterococcus avium (Q8KQL2), Enterococcus avium

12467497

brenda

Povelainen, M.; Miasnikov, A.N.

Production of D-arabitol by a metabolic engineered strain of Bacillus subtilis

Biotechnol. J.

214-219

2006

Enterococcus avium

16892251

brenda