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Bioorganic Chemistry

Volumn 57, Issue , 2014, Pages 198-205

The role of substrate strain in the mechanism of the carbon-carbon lyases

(3) Phillips, Robert S a,b Demidkina, Tatyana V c Faleev, Nicolai G d

a UNIVERSITY OF GEORGIA (United States)

b University of Georgia (United States)

c ENGELHARDT INSTITUTE OF MOLECULAR BIOLOGY (Russian Federation)

d A N NESMEYANOV INSTITUTE OF ORGANOELEMENT COMPOUNDS (Russian Federation)

Author keywords

Acidbase catalysis; Enzyme mechanism; Pyridoxal 5' phosphate; Substrate strain; Elimination

Indexed keywords

BENZIMIDAZOLE; LYASE; PYRIDINOL; QUINONE DERIVATIVE; TRYPTOPHAN INDOLE LYASE; TYROSINE PHENOL LYASE; UNCLASSIFIED DRUG; TRYPTOPHANASE;

ARTICLE; CATALYSIS; COMPETITIVE INHIBITION; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME INHIBITION; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; HYDROGEN BOND; MUTAGENESIS; SEQUENCE HOMOLOGY; STEADY STATE; AMINO ACID SEQUENCE; BACTERIUM; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; METABOLISM; MOLECULAR GENETICS; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; BACTERIA; CRYSTALLOGRAPHY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY; TRYPTOPHANASE; TYROSINE PHENOL-LYASE;

EID: 84913532285 PISSN: 00452068 EISSN: 10902120 Source Type: Journal
DOI: 10.1016/j.bioorg.2014.06.002 Document Type: Article

Times cited : (10)

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