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Ligand p-hydroxyphenylacetaldoxime

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (5 results)

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Show Natural Substrate (5 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.14.37

(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2 = (S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O

723366, 739318, 660217

-

1.14.14.37

(E)-4-Hydroxyphenylacetaldehyde oxime = (Z)-4-Hydroxyphenylacetaldehyde oxime

739318

-

1.14.14.37

2 entries

1.14.14.40

(E)-4-hydroxyphenylacetaldoxime + O2 + [reduced NADPH-hemoprotein reductase] = 1-aci-nitro-2-(4-hydroxyphenyl)-ethane + H2O + [oxidized NADPH-hemoprotein reductase]

739318

-

1.14.14.45

(E)-4-hydroxyphenylacetaldoxime + O2 + [reduced NADPH-hemoprotein reductase] = 1-aci-nitro-2-(4-hydroxyphenyl)-ethane + H2O + [oxidized NADPH-hemoprotein reductase]

743473

-

1.14.14.45

(E)-p-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + glutathione + O2 = S-[(Z)-N-hydroxy(p-hydroxyphenyl)acetimidoyl]-L-glutathione + [oxidized NADPH-hemoprotein reductase] + 2 H2O

741195

-

1.14.14.45

2 entries

In Vivo Product in Enzyme-catalyzed Reactions (2 results)

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Show Natural Product (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.14.36

L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase] = (E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O

-

-

1.14.14.36

N,N-dihydroxy-L-tyrosine = (E)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O

-

-

1.14.14.36

2 entries

Substrate in Enzyme-catalyzed Reactions (11 results)

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Show Substrate (11 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.14.37

(E)-4-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + O2 = (S)-4-hydroxymandelonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O

285331, 285332, 285333, 660217, 723366, 739318, 739339, 390081

-

1.14.14.37

(E)-4-Hydroxyphenylacetaldehyde oxime = (Z)-4-Hydroxyphenylacetaldehyde oxime

739318, 739339

-

1.14.14.37

2 entries

1.14.14.40

(E)-4-hydroxyphenylacetaldoxime + O2 + [reduced NADPH-hemoprotein reductase] = 1-aci-nitro-2-(4-hydroxyphenyl)-ethane + H2O + [oxidized NADPH-hemoprotein reductase]

739318

-

1.14.14.43

(E)-4-hydroxyphenylacetaldoxime + O2 + [reduced NADPH-hemoprotein reductase] = 1-aci-nitro-2-(4-hydroxyphenyl)-ethane + H2O + [oxidized NADPH-hemoprotein reductase]

741196, 741195

-

1.14.14.44

4-hydroxyphenylacetaldoxime + [reduced NADPH-hemoprotein reductase] + O2 = hydroxy(4-hydroxyphenyl)acetonitrile + [oxidized NADPH-hemoprotein reductase] + 2 H2O

741183

-

1.14.14.45

(E)-4-hydroxyphenylacetaldoxime + O2 + [reduced NADPH-hemoprotein reductase] = 1-aci-nitro-2-(4-hydroxyphenyl)-ethane + H2O + [oxidized NADPH-hemoprotein reductase]

743473, 743483

-

1.14.14.45

(E)-p-hydroxyphenylacetaldehyde oxime + [reduced NADPH-hemoprotein reductase] + glutathione + O2 = S-[(Z)-N-hydroxy(p-hydroxyphenyl)acetimidoyl]-L-glutathione + [oxidized NADPH-hemoprotein reductase] + 2 H2O

741195, 741196

-

1.14.14.45

(E)-p-hydroxyphenylacetaldoxime + NADPH + H+ + 2-mercaptoethanol = (Z)-2-hydroxyethyl N,4-dihydroxybenzene-1-carboximidothioate + NADP+ + H2O

739318

-

1.14.14.45

p-hydroxyphenylacetaldoxime + [reduced NADPH-hemoprotein reductase] + cysteine + O2 = S-(benzohydroximoyl)-L-cysteine + [oxidized NADPH-hemoprotein reductase] + 2 H2O

740669

-

1.14.14.45

p-hydroxyphenylacetaldoxime + [reduced NADPH-hemoprotein reductase] + N-acetylcysteine + O2 = S-(benzohydroximoyl)-N-acetyl-L-cysteine + [oxidized NADPH-hemoprotein reductase] + 2 H2O

740669

-

1.14.14.45

5 entries

4.99.1.6

(E,Z)-4-hydroxyphenylacetaldehyde oxime = ?

716456

-

Product in Enzyme-catalyzed Reactions (5 results)

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Show Product (5 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.14.13.148

tyramine + NADPH + H+ + O2 = 4-[(2E)-2-(hydroxyimino)ethyl]phenol + NADP+ + H2O

-

-

1.14.14.36

L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase] = (E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O

, 390080, 390081

-

1.14.14.36

N,N-dihydroxy-L-tyrosine = (E)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O

-

-

1.14.14.36

2 entries

1.14.14.37

L-tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase] = (E)-[4-hydroxyphenylacetaldehyde oxime] + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O

-

-

1.14.14.40

tyrosine + 2 O2 + 2 [reduced NADPH-hemoprotein reductase] = (E)-4-hydroxyphenylacetaldoxime + 2 [oxidized NADPH-hemoprotein reductase] + CO2 + 3 H2O

-

-

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (6 results)

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Show Turnover Number (6 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.14.14.43

0.23

-

pH 8.1, 29°C

741196

1.14.14.43

0.43

-

pH 8.1, 29°C

741196

1.14.14.43

2 entries

1.14.14.44

0.62

-

pH 7.6, 30°C

741183

1.14.14.45

0.16

-

pH 8.1, 29°C

741195

1.14.14.45

0.23

-

pH 8.1, 29°C

741196

1.14.14.45

0.27

-

pH 8.1, 29°C

740669

1.14.14.45

3 entries

K_M Value (6 results)

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Show KM Value (6 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.14.14.37

0.2

-

-

285332

1.14.14.43

0.065

-

pH 8.1, 29°C

741196

1.14.14.43

0.156

-

pH 8.1, 29°C

741196

1.14.14.43

2 entries

1.14.14.44

0.007

-

pH 7.6, 30°C

741183

1.14.14.45

0.065

-

pH 8.1, 29°C

741196

1.14.14.45

0.068

-

pH 81, 29°C

740669

1.14.14.45

2 entries

References & Links

Literature References (16)

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Show Reference (16 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

285331

237909

Conn, E.E.: The in vitro biosynthesis of dhurrin, the cyanogenic glycoside of Sorghum bicolor

1975

McFarlane, I.J.; Lees, E.M

J. Biol. Chem.

250

4708-4713

285332

193443

The enzymatic conversion of p-hydroxyphenylacetaldoxime to p-hydroxymandelonitrile

1977

Shimada, M.; Conn, E.E.

Arch. Biochem. Biophys.

180

199-207

285333

9484480

Cloning of three A-type cytochromes P450, CYP71E1, CYP98, and CYP99 from Sorghum bicolor (L:) Moench by a PCR approach and identification by expression in Escherichia coli of CYP71E1 as a multifunctional cytochrome P450 in the biosynthesis of the cyanogenic glucoside dhurrin

1998

Bak, S.; Kahn, R.A.; Nielsen, H.L.; Moeller, B.L.; Halkier, B.A.

Plant Mol. Biol.

36

393-405

390080

7574710

Purification and characterization of recombinant cytochrome P450tyr expressed at high levels in Escherichia coli

1995

Halkier, B.A.; Nielsen, H.L.; Koch, B.; Moller B.L.

Arch. Biochem. Biophys.

322

369-377

390081

10049494

Substrate specificity of the cytochrome P450 enzymes CYP79A1 and CYP71E1 involved in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench

1999

Kahn, R.A.; Fahrendorf, T.; Halkier, B.A.; Moller, B.L.

Arch. Biochem. Biophys.

363

9-18

660217

12114576

Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants

2002

Busk, P.K.; Moller, B.L.

Plant Physiol.

129

1222-1231

716456

21036375

Indolyl-3-acetaldoxime dehydratase from the phytopathogenic fungus Sclerotinia sclerotiorum: purification, characterization, and substrate specificity

2010

Pedras, M.S.; Minic, Z.; Thongbam, P.D.; Bhaskar, V.; Montaut, S.

Phytochemistry

71

1952-1962

723366

21620426

Homology modeling of the three membrane proteins of the dhurrin metabolon: catalytic sites, membrane surface association and protein-protein interactions

2011

Jensen, K.; Osmani, S.A.; Hamann, T.; Naur, P.; Moller, B.L.

Phytochemistry

72

2113-2123

739318

26361733

The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways

2015

Clausen, M.; Kannangara, R.M.; Olsen, C.E.; Blomstedt, C.K.; Gleadow, R.M.; Jorgensen, K.; Bak, S.; Motawie, M.S.; Moller, B.L.

Plant J.

84

558-573

739339

9414567

Isolation and reconstitution of cytochrome P450ox and in vitro reconstitution of the entire biosynthetic pathway of the cyanogenic glucoside dhurrin from sorghum

1997

Kahn, R.A.; Bak, S.; Svendsen, I.; Halkier, B.A.; Moller, B.L.

Plant Physiol.

115

1661-1670

740669

11333274

CYP83B1 is the oxime-metabolizing enzyme in the glucosinolate pathway in Arabidopsis

2001

Hansen, C.H.; Du, L.; Naur, P.; Olsen, C.E.; Axelsen, K.B.; Hick, A.J.; Pickett, J.A.; Halkier, B.A.

J. Biol. Chem.

276

24790-24796

741183

25015725

Identification and characterization of CYP79D16 and CYP71AN24 catalyzing the first and second steps in L-phenylalanine-derived cyanogenic glycoside biosynthesis in the Japanese apricot, Prunus mume Sieb. et Zucc

2014

Yamaguchi, T.; Yamamoto, K.; Asano, Y.

Plant Mol. Biol.

86

215-223

741195

11553739

The involvement of two p450 enzymes, CYP83B1 and CYP83A1, in auxin homeostasis and glucosinolate biosynthesis

2001

Bak, S.; Feyereisen, R.

Plant Physiol.

127

108-118

741196

12970475

CYP83A1 and CYP83B1, two nonredundant cytochrome P450 enzymes metabolizing oximes in the biosynthesis of glucosinolates in Arabidopsis

2003

Naur, P.; Petersen, B.L.; Mikkelsen, M.D.; Bak, S.; Rasmussen, H.; Olsen, C.E.; Halkier, B.A.

Plant Physiol.

133

63-72

743473

26361733

The bifurcation of the cyanogenic glucoside and glucosinolate biosynthetic pathways

2015

Clausen, M.; Kannangara, R.; Olsen, C.; Blomstedt, C.; Gleadow, R.; Jörgensen, K.; Bak, S.; Motawie, M.; Möller, B.

Plant J.

84

558-573

743483

11553739

The involvement of two p450 enzymes, CYP83B1 and CYP83A1, in auxin homeostasis and glucosinolate biosynthesis

2001

Bak, S.; Feyereisen, R.

Plant Physiol.

127

108-118

Links to other databases for p-hydroxyphenylacetaldoxime

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Show Links (1 entry)

ChEBI

PubChem

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