Substrate specificity of king cobra (Ophiophagus hannah) VENOM l-amino acid oxidase

Tan Nget-Hong, Saifuddin M. Nomanbhay

Research output: Contribution to journalArticle

39 Citations (Scopus)

Abstract

1. 1. Substrate specificity of purified king cobra (Ophiophagus hannah) venom l-amino acid oxidase was investigated. 2. 2. The enzyme was highly specific for the l-enantiomer of amino acid. Effective oxidation of l-amino acid by the enzyme requires the presence of a free primary α-amino group but the α-carboxylate group is not as critical for the catalysis. 3. 3. The enzyme was very active against l-Lys, l-Phe, l-Leu, l-Tyr, l-Tryp, l-Arg, l-Met, l-ornithine, l-norleucine and l-norvaline and moderately active against l-His, l-cystine and l-Ileu. Other l-amino acids were oxidized slowly or not oxidized. 4. 4. The data suggest the presence of a side chain binding site in the enzyme, and that the binding site comprises at least five 'subsites': the hydrophobic subsites a, b and c; and the two 'amino' binding subsites d and e. Subsite b appears to be able to accommodate two methylene/methyl carbons.

Original languageEnglish
Pages (from-to)323-327
Number of pages5
JournalInternational Journal of Biochemistry
Volume23
Issue number3
DOIs
Publication statusPublished - 01 Jan 1991

Fingerprint

Elapidae
Substrate Specificity
Oxidoreductases
Amino Acids
Substrates
Enzymes
Norleucine
Binding Sites
Ornithine
Cystine
Enantiomers
Venoms
Catalysis
Carbon
Oxidation

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

@article{4b04eb7402a94ef3a8f4457f8e6fb169,
title = "Substrate specificity of king cobra (Ophiophagus hannah) VENOM l-amino acid oxidase",
abstract = "1. 1. Substrate specificity of purified king cobra (Ophiophagus hannah) venom l-amino acid oxidase was investigated. 2. 2. The enzyme was highly specific for the l-enantiomer of amino acid. Effective oxidation of l-amino acid by the enzyme requires the presence of a free primary α-amino group but the α-carboxylate group is not as critical for the catalysis. 3. 3. The enzyme was very active against l-Lys, l-Phe, l-Leu, l-Tyr, l-Tryp, l-Arg, l-Met, l-ornithine, l-norleucine and l-norvaline and moderately active against l-His, l-cystine and l-Ileu. Other l-amino acids were oxidized slowly or not oxidized. 4. 4. The data suggest the presence of a side chain binding site in the enzyme, and that the binding site comprises at least five 'subsites': the hydrophobic subsites a, b and c; and the two 'amino' binding subsites d and e. Subsite b appears to be able to accommodate two methylene/methyl carbons.",
author = "Tan Nget-Hong and {M. Nomanbhay}, Saifuddin",
year = "1991",
month = "1",
day = "1",
doi = "10.1016/0020-711X(91)90114-3",
language = "English",
volume = "23",
pages = "323--327",
journal = "International Journal of Biochemistry and Cell Biology",
issn = "1357-2725",
publisher = "Elsevier Limited",
number = "3",

}

Substrate specificity of king cobra (Ophiophagus hannah) VENOM l-amino acid oxidase. / Nget-Hong, Tan; M. Nomanbhay, Saifuddin.

In: International Journal of Biochemistry, Vol. 23, No. 3, 01.01.1991, p. 323-327.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Substrate specificity of king cobra (Ophiophagus hannah) VENOM l-amino acid oxidase

AU - Nget-Hong, Tan

AU - M. Nomanbhay, Saifuddin

PY - 1991/1/1

Y1 - 1991/1/1

N2 - 1. 1. Substrate specificity of purified king cobra (Ophiophagus hannah) venom l-amino acid oxidase was investigated. 2. 2. The enzyme was highly specific for the l-enantiomer of amino acid. Effective oxidation of l-amino acid by the enzyme requires the presence of a free primary α-amino group but the α-carboxylate group is not as critical for the catalysis. 3. 3. The enzyme was very active against l-Lys, l-Phe, l-Leu, l-Tyr, l-Tryp, l-Arg, l-Met, l-ornithine, l-norleucine and l-norvaline and moderately active against l-His, l-cystine and l-Ileu. Other l-amino acids were oxidized slowly or not oxidized. 4. 4. The data suggest the presence of a side chain binding site in the enzyme, and that the binding site comprises at least five 'subsites': the hydrophobic subsites a, b and c; and the two 'amino' binding subsites d and e. Subsite b appears to be able to accommodate two methylene/methyl carbons.

AB - 1. 1. Substrate specificity of purified king cobra (Ophiophagus hannah) venom l-amino acid oxidase was investigated. 2. 2. The enzyme was highly specific for the l-enantiomer of amino acid. Effective oxidation of l-amino acid by the enzyme requires the presence of a free primary α-amino group but the α-carboxylate group is not as critical for the catalysis. 3. 3. The enzyme was very active against l-Lys, l-Phe, l-Leu, l-Tyr, l-Tryp, l-Arg, l-Met, l-ornithine, l-norleucine and l-norvaline and moderately active against l-His, l-cystine and l-Ileu. Other l-amino acids were oxidized slowly or not oxidized. 4. 4. The data suggest the presence of a side chain binding site in the enzyme, and that the binding site comprises at least five 'subsites': the hydrophobic subsites a, b and c; and the two 'amino' binding subsites d and e. Subsite b appears to be able to accommodate two methylene/methyl carbons.

UR - http://www.scopus.com/inward/record.url?scp=0026098709&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0026098709&partnerID=8YFLogxK

U2 - 10.1016/0020-711X(91)90114-3

DO - 10.1016/0020-711X(91)90114-3

M3 - Article

VL - 23

SP - 323

EP - 327

JO - International Journal of Biochemistry and Cell Biology

JF - International Journal of Biochemistry and Cell Biology

SN - 1357-2725

IS - 3

ER -