Role of arginine 226 in the mechanism of tryptophan indole-lyase from Proteus vulgaris

Biochemistry (Moscow)

Volumn 68, Issue 11, 2003, Pages 1181-1188

  Kulikova, V V ^a   Zakomirdina, L N ^a   Bazhulina, N P ^a   Dementieva, I S ^a   Faleev, N G ^b   Gollnick, P D ^c   Demidkina, T V ^a  

^a ENGELHARDT INSTITUTE OF MOLECULAR BIOLOGY   (Russian Federation)

^b RUSSIAN ACADEMY OF SCIENCES   (Russian Federation)

^c UNIVERSITY AT BUFFALO   (United States)

Author keywords

Arginine 226; Pyridoxal 5 phosphate; Site directed mutagenesis; Tryptophan indole lyase from Proteus vulgaris

Indexed keywords

AMINO ACIDS; ATOMS; CATALYST ACTIVITY; COENZYMES; COMPLEXATION; ENZYME INHIBITION; ENZYME KINETICS; OXYGEN; PHOSPHORUS COMPOUNDS; PROTONS; REACTION KINETICS; SALTS;

ABSORPTION AND CIRCULAR DICHROISM; ARGININE; PROTEUS VULGARIS; PYRIDOXAL PHOSPHATE; SITE DIRECTED MUTAGENESIS; TRYTOPHAN INDOLE LYASE;

ENZYMES;

PROTEUS VULGARIS;

AMINO ACID; ARGININE; TRYPTOPHANASE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYMOLOGY; GENETICS; KINETICS; METABOLISM; MOLECULAR GENETICS; PROTEUS VULGARIS; SEQUENCE ALIGNMENT; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO ACIDS; ARGININE; CATALYTIC DOMAIN; KINETICS; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; PROTEUS VULGARIS; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY; TRYPTOPHANASE;

EID: 0742321205     PISSN: 00062979     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:BIRY.0000009131.78603.8b     Document Type: Article

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