Substrate specificity of king cobra ( Ophiophagus hannah) VENOM l-amino acid oxidase
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 t...
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Published in | International journal of biochemistry Vol. 23; no. 3; pp. 323 - 327 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
England
Elsevier B.V
1991
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Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0020-711X |
DOI: | 10.1016/0020-711X(91)90114-3 |