Evolution of substrate specificity within a diverse family of β/α-barrel-fold basic amino acid decarboxylases: X-ray structure determination of enzymes with specificity for L-arginine and carboxynorspermidine

Journal of Biological Chemistry

Volumn 285, Issue 33, 2010, Pages 25708-25719

  Deng, Xiaoyi ^a   Lee, Jeongmi ^b   Michael, Anthony J ^a   Tomchick, Diana R ^a   Goldsmith, Elizabeth J ^a   Phillips, Margaret A ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

^b Sungkyunkwan University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDIC RESIDUES; ACTIVE SITE; AGMATINE; AMINO GROUP; ANALYTICAL ULTRACENTRIFUGATION; ARGININE DECARBOXYLASE; ASYMMETRIC UNIT; BACK REACTION; C-TERMINAL EXTENSIONS; DECARBOXYLASES; DIMERIC STRUCTURE; HELICAL BUNDLE; INTER-DOMAIN; L-ARGININE; LYSINE BIOSYNTHESIS; NOVEL FUNCTIONS; POLYAMINES; PRODUCT COMPLEX; PRODUCT RELEASE; SCHIFF-BASE; SEQUENCE IDENTITY; SOLUTION STRUCTURES; STRUCTURAL BASIS; SUBSTRATE SPECIFICITY; TETRAMERS; X-RAY STRUCTURE;

BIOCHEMISTRY; BIOSYNTHESIS; CARBOXYLATION; CATALYSTS; CENTRIFUGATION; DYES; ENZYMES; FUNCTIONAL GROUPS; ORGANIC ACIDS; SUBSTRATES;

AMINO ACIDS;

AGMATINE; AMINO ACID DECARBOXYLASE; ARGININE; CARBOXYNORSPERMIDINE; PYRIDOXAL 5 PHOSPHATE; SPERMIDINE DERIVATIVE; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; BETA SHEET; BINDING SITE; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME SPECIFICITY; GENE INSERTION SEQUENCE; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; STRUCTURE ANALYSIS; ULTRACENTRIFUGATION; X RAY DIFFRACTION;

AMINO ACID SEQUENCE; AMINO ACIDS, BASIC; BACTERIAL PROTEINS; CARBOXY-LYASES; CRYSTALLOGRAPHY, X-RAY; EVOLUTION, MOLECULAR; KINETICS; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS);

EID: 77955501060     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.121137     Document Type: Article

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