Information on EC 1.14.13.5 - imidazoleacetate 4-monooxygenase

Substrates: -
Products: -

imidazolelactate + NADH + O2 + H+

5-hydroxyimidazolelactate + NAD+ + H2O

Substrates: 4% relative activity to 4-imidazoleacetate
Products: -

imidazolepropionate + NAD(P)H + O2 + H+

5-hydroxyimidazolepropionate + NAD(P)+ + H2O

Substrates: -
Products: -

imidazolepropionate + NAD(P)H + O2 + H+

5-hydroxyimidazolepropionate + NAD(P)+ + H2O

Substrates: 9.5% relative activity to 4-imidazoleacetate
Products: -

imidazolepropionate + NAD(P)H + O2 + H+

5-hydroxyimidazolepropionate + NAD(P)+ + H2O

Substrates: 10% relative activity to 4-imidazoleacetate
Products: -

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

4-imidazoleacetate + NADH + O2

5-hydroxy-4-imidazoleacetate + NAD+ + H2O

4-imidazoleacetate + NADH + O2

5-hydroxy-4-imidazoleacetate + NAD+ + H2O

390101, 390103, 390104, 390105

Substrates: -
Products: -

4-imidazoleacetate + NADH + O2

5-hydroxy-4-imidazoleacetate + NAD+ + H2O

390102, 390106

Substrates: the enzyme is part of the histidine catabolic pathway in which imidazaloneacetate is converted to aspartic acid by way of formiminoaspartic acid
Products: -

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

FAD

3 entries

NADH

390101, 390102, 390103, 390104, 390105, 390106

NADPH

3 entries

additional information

the enzyme contains 2 mol of titratable suflhydryl groups, one of which is essential, possibly as a substrate-binding site, for the oxygenation of imidazoleacetate

FAD

1 mol per mol enzyme

390102, 390103, 390104, 390105, 390106

FAD

FAD is the only prosthetic group

390102

FAD

cannot be replaced by FMN or riboflavin

390104, 390106

NADPH

beta-NADPH is approximately 13% as active as beta-NADH

NADPH

less efficient than NADH

390102, 390103

NADPH

alpha-NADH cannot replace beta-NADH at 0.2 mM

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

5-hydroxyindoleacetate

11% inhibition at 4.5 mM

dihydroxymandelate

53% inhibition at 4.5 mM

Dihydroxyphenylacetate

66% inhibition at 4.5 mM

ethyl-mercuric chloride

homogentisate

50% inhibition at 4.5 mM

homovanillic acid

5% inhibition at 4.5 mM

Imidazolepyruvate

56% inhibition at 4.5 mM

indoleacetate

m-hydroxyphenylacetate

79% inhibition at 4.5 mM

mercury compounds

methyl-mercuric chloride

N-methylimidazoleacetate

11% inhibition at 4.5 mM

nicotinate

65% inhibition at 20 mM

p-chloromercuribenzoate

p-hydroxybenzoate

38% inhibition at 4.5 mM

p-hydroxyphenylacetate

47% inhibition at 4.5 mM

phenyl-mercuric acetate

phenylacetate

silver compounds

390103, 390104, 390105

Sodium mersalyl

vanillyl mandelic acid

9% inhibition at 4.5 mM

indoleacetate

22% inhibition at 4.5 mM

indoleacetate

30% inhibition at 10 mM

mercury compounds

mercury compounds

maximum inactivation at a ratio about 2 mol of AgNO3 per mol of enzyme

p-chloromercuribenzoate

390102, 390103, 390104

p-chloromercuribenzoate

maximum inactivation at a ratio about 2 mol of p-chloromercuribenzoate per mol of enzyme

phenylacetate

25% inhibition at 4.5 mM

phenylacetate

79% inhibition at 20 mM

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

5-hydroxyindoleacetate

0.3 - 0.5

imidazoleacetate

4 entries

indoleacetate

N-methylimidazoleacetate

0.002 - 0.03

NADH

5 entries

0.02

0.01

Sodium diethyldithiocarbamate

polarographic method

0.3

imidazoleacetate

0.3

imidazoleacetate

spectrophotometric method

0.48

imidazoleacetate

0.5

imidazoleacetate

polarographic method

0.002

NADH

0.002 - 0.01

NADH

0.01

NADH

spectrophotometric method

0.015

NADH

substrate: sodium diethyldithiocarbamate, polarographic method

0.03

NADH

polarographic method

0.02

0.02

substrate: imidazoleacetate or sodium diethyldithiocarbamate, polarographic method

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

37.7

imidazoleacetate

show all columns Go to Specific Activity Search

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SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

390103, 390104, 390106

additional information

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

show all columns Go to Organism Search

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

390101, 390102, 390103, 390104, 390105, 390106

brenda

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show all columns Go to Molecular Weight Search

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

87000 - 90000

sedimentation equilibrium, gel filtration

390102, 390103, 390104, 390105, 390106

Go to Crystallization (commentary) Search

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

390102, 390103, 390104, 390105, 390106

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

2% loss of activity, 0.1 M potassium phosphate, pH 7.2, 5 min

50% loss of activity, 0.1 M potassium phosphate, pH 7.2, 5 min

95% loss of activity, 0.1 M potassium phosphate, pH 7.2, 5 min

Go to Storage Stability Search

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STORAGE STABILITY

ORGANISM

UNIPROT

LITERATURE

-20°C, potassium phosphate buffer, pH 7.2, no loss of activity for at least 1 month

-20°C, stable for at least 6 months

4°C, 5-100 mM potassium phosphate buffer, pH 7.2, almost full activity retained for several days

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

partial, using ammonium sulfate precipitation and column chromatography on DEAE-Sephadex A-50

using protamine sulfate treatment, ammonium sulfate fractionation, chromatography on TEAE-cellulose column, calcium phosphate gel treatment and chromatography on DEAE-Sephadex column

top print hide References Search

390103, 390104, 390106

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

Watanabe, T.; Kambe, H.; Imamura, I.; Taguchi, Y.; Tamura, T.; Wada, H.

Method for enzymatic determination of imidazole acetic acid

Anal. Biochem.

130

321-327

1983

Pseudomonas sp.

6869819

brenda

390102

Flashner, M.S.; Massey, V.

Flavoprotein oxygenases

Mol. Mech. Oxygen Activ. (Hayaishi, O., ed.) Academic Press, New York

245-283

1974

Pseudomonas sp.

brenda

Nozaki, M.

Imidazolacetate monooxygenase (Pseudomonas)

Methods Enzymol.

17B

773-777

1971

Pseudomonas sp.

brenda

Maki, Y.; Yamamoto, S.; Nozaki, M.; Hayaishi, O.

Studies on monooxygenases. II. Crystallization and some properties of imidazole acetate monooxygenase

J. Biol. Chem.

244

2942-2950

1969

Pseudomonas sp.

5772468

brenda