Information on EC 1.1.1.54 - allyl-alcohol dehydrogenase

Substrates: (R)-carvone, (S)-carvone, (1S,5S)-verbenone, (1R,5R)-verbenone, oxalacetic acid, and (2S,4S)-carveol do not serve as substrate
Products: -

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

3-methyl-2-buten-1-ol + NAD+

3-methyl-2-buten-1-al + NADH

allyl alcohol + NADP+

acrolein + NADPH

3-methyl-2-buten-1-ol + NAD+

3-methyl-2-buten-1-al + NADH

Substrates: can use substrate as sole carbon source
Products: -

3-methyl-2-buten-1-ol + NAD+

3-methyl-2-buten-1-al + NADH

Pseudomonas putida MB-1

Substrates: can use substrate as sole carbon source
Products: -

allyl alcohol + NADP+

acrolein + NADPH

Substrates: -
Products: -

allyl alcohol + NADP+

acrolein + NADPH

Substrates: -
Products: -

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

NAD(P)H

NAD+

exhibits less than 5% of the activity with NADP+

NADP+

NAD(P)H

NAD(P)H

NADP+

NADP+

specific for

NADP+

activity 4times greater than with NAD+

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

additional information

additional information

is sensitive against metal ion chelators

additional information

is not sensitive against metal ion chelators

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

3-methyl-2-buten-1-al

product inhibition, therefore the product must be removed via reaction with hydrazine during the enzyme assay

cyanide

dipyridyl

dithiothreitol

EDTA

N-ethylmaleimide

p-chloromercuribenzoate

can be overcome by addition of gluthathione

additional information

not: monoiodoacetate

EDTA

EDTA

only at concentration of 100 mM 50% reduction

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.012

(R)-(+)-perillyl alcohol

0.025 - 1.4

(R)-pulegone

8.3

(S)-pulegone

recombinant enzyme, pH 7.0, 35°C

1.1

1-butanol

0.044

2-Buten-1-ol

0.011

3-aminobenzyl alcohol

0.007

3-chloro-2-buten-1-ol

0.27

3-methyl-1-butanol

0.04

3-methyl-2-buten-1-ol

1.7

3-methyl-3-buten-1-ol

allyl-alcohol

0.007

benzyl alcohol

0.036

cinnamyl alcohol

0.064 - 0.118

NAD+

0.04

NADP+

0.025

(R)-pulegone

native enzyme, pH 7.0, 35°C

1.4

(R)-pulegone

recombinant enzyme, pH 7.0, 35°C

0.064

NAD+

with 3-methyl-2-buten-1-ol

0.118

NAD+

with benzyl alcohol

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

3.3

(R)-pulegone

recombinant enzyme, pH 7.0, 35°C

2.8

(S)-pulegone

recombinant enzyme, pH 7.0, 35°C

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.05

purified enzyme, substrate 1-butanol

0.08

purified enzyme, substrate 3-methyl-3-buten-1-ol

0.11

0.2

purified enzyme, substrate 3-methyl-1-butanol

purified enzyme, substrate 3-chlor-2-buten-1-ol

19.3

purified enzyme, in glycine buffer pH 9.4

purified enzyme, substrate benzyl alcohol

3.7

purified enzyme, substrate cinnamyl alcohol

purified enzyme, substrate aromatic 3-aminobenzyl alcohol

38.8

purified enzyme, in bis-Tris-propane-hydrazine buffer pH 9.4

4.6

purified enzyme, substrate 2-buten-1-ol

7.7

purified enzyme, substrate 3-methyl-2-buten-1-ol

8.8

purified enzyme, substrate (R)-(+)-perillyl alcohol

additional information

about 70,1 unit of enzyme activity defined as amount of enzyme which causes a change in optical density of 0.001 per minute

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

for oxidation

5.4

for reduction

assay pH

7.4

reduction of carbonyl group of (S)-carvone

7.7

in Tris-buffer

dehydrogenation of (S)-carveol

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

assay temperature

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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

UniProt

brenda

brenda

Pseudomonas putida MB-1

brenda

Saccharomyces cerevisiae

brenda

brenda

UniProt

brenda

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

physiological function

Fusarium oxysporum

E3UTQ9

interruption of the coding region of the Adh1 gene causes resistance to allyl alcohol, deficiency in alcohol dehydrogenase activity, as well as alteration of different physiological parameters related to carbon and energy metabolism, including the ability to use ethanol as a carbon source under aerobic conditions, impaired growth under hypoxic conditions with glucose as the carbon source, and diminished production of ethanol in glucose-containing medium

725090

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Show AA Sequence and Transmembrane Helices (248 entries)
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PDB

SCOP

CATH

UNIPROT

ORGANISM

11 entries

Homo sapiens

6t27, download, 3D-view

6t3p, download, 3D-view

6t5g, download, 3D-view

6t7q, download, 3D-view

6td8, download, 3D-view

6tuc, download, 3D-view

6tuf, download, 3D-view

6txp, download, 3D-view

6xum, download, 3D-view

6y03, download, 3D-view

6y1p, download, 3D-view

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

151000

gel filtration

36300

2 * 36300, SDS-PAGE, native mass by gel filtration

37000

2 * 37000, SDS-PAGE and amino acid sequence analysis

37700

4 * 37700, SDS-PAGE

38482

2 * 38482, recombinant protein, MALDI TOF-MS, native mass by gel filtration

38487

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2 * 38487, recombinant protein, calculated from the deduced amino acid sequence, native mass by gel filtration

74000

74000

gel filtration

74000

gel filtration

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

dimer

4 entries

tetramer

dimer

2 * 37000, SDS-PAGE and amino acid sequence analysis

dimer

2 * 36300, SDS-PAGE, native mass by gel filtration

dimer

2 * 38482, recombinant protein, MALDI TOF-MS, native mass by gel filtration

dimer

2 * 38487, recombinant protein, calculated from the deduced amino acid sequence, native mass by gel filtration

tetramer

4 * 37700, SDS-PAGE

tetramer

Pseudomonas putida MB-1

4 * 37700, SDS-PAGE

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

additional information

Saccharomyces cerevisiae

isoform ADH1 oxidizes allyl alcohol to toxic acrolein. Use of the reaction to isolate mutations in the ADH1 gene that lead to decreased ADH activity. These yeast may grow more slowly due to slower reduction of acetaldehyde and a higher NADH/NAD+ ratio, which should decrease the oxidation of allyl alcohol

724009

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pH STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

9.4

stability at pH 9.4, 25°C much higher than at reactions optimal pH of 10.0

287114

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STORAGE STABILITY

ORGANISM

UNIPROT

LITERATURE

-70°C, 50-65% ethylene glycol (v/v), frozen in liquid nitrogen, stable for several month

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

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native enzyme, recombinant enzyme purified using GST-tag

partial

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CLONED (Commentary)

ORGANISM

UNIPROT

LITERATURE

GST-fusion protein expressed in Escherichia coli BL21

sequence homology with other NADPH-dependent oxidoreductases from plants

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

Otsuka, K.

Triphosphopyridine nucleotide-allyl and -ethyl alcohol dehydrogenases from Escherichia coli (preliminary report)

J. Gen. Appl. Microbiol.

211-215

1958

Escherichia coli

brenda

Hirata, T.; Tamura, Y.; Yokobatake, N.; Shimoda, K.; Ashida, Y.

A 38 kDa allylic alcohol dehydrogenase from the cultured cells of Nicotiana tabacum

Phytochemistry

297-303

2000

Nicotiana tabacum

11117876

brenda

Malone, V.F.; Chastian, A.J.; Ohlsson, J.T.; Poneleit, L.S.; Nemecek-Marshall, M.; Fall, R.

Characterization of a Pseudomonas putida allylic alcohol dehydrogenase induced by growth on 2-methyl-3-buten-2-ol

Appl. Environ. Microbiol.

2622-2630

1999

Pseudomonas putida, Pseudomonas putida MB-1

10347052

brenda