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Volumn 7, Issue 2, 2011, Pages 379-384

The structure of a native l-amino acid oxidase, the major component of the Vipera ammodytes ammodytes venomic, reveals dynamic active site and quaternary structure stabilization by divalent ions

(5) Georgieva, Dessislava a,b Murakami, Mario c Perband, Markus a,d Arni, Raghuvir e Betzel, Christian a

a UNIVERSITY OF HAMBURG (Germany)

b INSTITUTE OF ORGANIC CHEMISTRY (Bulgaria)

c BRAZILIAN CENTER FOR RESEARCH IN ENERGY AND MATERIALS CNPEM (Brazil)

d UNIVERSITY MEDICAL CENTER HAMBURG EPPENDORF (Germany)

e SÃO PAULO STATE UNIVERSITY UNESP (Brazil)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID OXIDASE; DIVALENT CATION; VIPER VENOM;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; ENZYME ACTIVE SITE; ENZYMOLOGY; GLYCOSYLATION; ISOLATION AND PURIFICATION; METABOLISM; PROTEIN QUATERNARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

CATALYTIC DOMAIN; CATIONS, DIVALENT; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; GLYCOSYLATION; L-AMINO ACID OXIDASE; MODELS, MOLECULAR; PROTEIN STRUCTURE, QUATERNARY; VIPER VENOMS;

VIPERA AMMODYTES AMMODYTES;

EID: 78751662638 PISSN: 1742206X EISSN: 17422051 Source Type: Journal
DOI: 10.1039/c0mb00101e Document Type: Article

Times cited : (25)

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