Determinants of Substrate Specificity in omega-Aminotransferases

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F05%3A00016011" target="_blank" >RIV/60461373:22330/05:00016011 - isvavai.cz</a>

Result on the web

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DOI - Digital Object Identifier

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Result language

angličtina

Original language name

Determinants of Substrate Specificity in omega-Aminotransferases

Original language description

Ornithine aminotransferase and 4-aminobutyrate aminotransferase are related pyridoxal phosphate-dependent enzymes having different substrate specificities. The atomic structures of these enzymes have shown (i) that active site differences are limited tothe steric positions occupied by two tyrosine residues in ornithine aminotransferase and (ii) that, uniquely among related, structurally characterized aminotransferases, the conserved arginine that binds the alpha-carboxylate of alpha-amino acids interacts tightly with a glutamate residue. To determine the contribution of these residues to the specificities of the enzymes, we analyzed site-directed mutants of ornithine aminotransferase by rapid reaction kinetics, x-ray crystallography, and (13)C NMR spectroscopy. Mutation of one tyrosine (Tyr-85) to isoleucine, as found in aminobutyrate aminotransferase, decreased the rate of the reaction of the enzyme with ornithine 1000-fold and increased that with 4-aminobutyrate 16-fold, indicating

Czech name

Podstata substrátové specifity omega-aminotransferas.

Czech description

Podstata substrátové specifity omega-aminotransferas.Podstata substrátové specifity omega-aminotransferas.Podstata substrátové specifity omega-aminotransferas.Podstata substrátové specifity omega-aminotransferas.Podstata substrátové specifity omega-aminotransferas.Podstata substrátové specifity omega-aminotransferas.Podstata substrátové specifity omega-aminotransferas.Podstata substrátové specifity omega-aminotransferas.Podstata substrátové specifity omega-aminotransferas.Podstata substrátové specifityomega-aminotransferas.

Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EB - Genetics and molecular biology

OECD FORD branch

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Project

<a href="/en/project/GA204%2F02%2F0843" target="_blank" >GA204/02/0843: Complex cold adaptation study of enzymes on molecular level and their application in biotechnology</a><br>

Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2005

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

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Volume of the periodical

280

Issue of the periodical within the volume

43

Country of publishing house

US - UNITED STATES

Number of pages

4

Pages from-to

36-40

UT code for WoS article

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EID of the result in the Scopus database

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