Catalytic activity of the anaerobic tyrosine lyase required for thiamine biosynthesis in Escherichia coli

Journal of Biological Chemistry

Volumn 285, Issue 8, 2010, Pages 5240-5248

  Challand, Martin R ^a   Martins, Filipa T ^a   Roach, Peter L ^a  

^a UNIVERSITY OF SOUTHAMPTON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVITY ASSAYS; BOND CLEAVAGES; CATALYTIC ACTIVITY; CATALYTIC BEHAVIOR; CLEAVAGE REACTION; CYCLIZATION REACTIONS; DEOXYADENOSINE; GLYOXYLATE; HETERODIMERS; NUCLEOSIDASE; P-CRESOL; PHENOLIC SUBSTRATES; PRE-STEADY STATE; PRODUCT FORMATION; PRODUCT INHIBITION; PRODUCT-FORMING PATHWAY; RATE DETERMINING STEP; REACTION PATHWAYS; REACTIVE INTERMEDIATE; REDUCTIVE CLEAVAGE; S-ADENOSYLMETHIONINE; SYNTHASES; TIME-DEPENDENT; TYROSINE ANALOGUES;

ADDITION REACTIONS; AMINO ACIDS; AMMONIUM COMPOUNDS; BIOCHEMISTRY; DIRECTION OF ARRIVAL; ESCHERICHIA COLI; PHENOLS; PHOSPHATASES; RADIO DIRECTION FINDING SYSTEMS; REACTION INTERMEDIATES; SUBSTRATES;

CYCLIZATION;

5' METHYLTHIOADENOSINE; AMMONIA; DEOXYADENOSINE DERIVATIVE; ENZYME; GLYCINE DERIVATIVE; GLYOXYLIC ACID; METHIONINE; NUCLEOSIDASE; PARA CRESOL; PHENOL DERIVATIVE; PROPIONIC ACID DERIVATIVE; RADICAL; S ADENOSYLHOMOCYSTEINE; S ADENOSYLMETHIONINE; THIAMINE; THIAZOLE; THIAZOLE SYNTHASE; TYROSINE; TYROSINE DERIVATIVE; TYROSINE LYASE; UNCLASSIFIED DRUG; CRESOL; ENZYME INHIBITOR; ESCHERICHIA COLI PROTEIN; LYASE; THIG PROTEIN, E COLI; THIH PROTEIN, E COLI;

ADDITION REACTION; ARTICLE; ASSAY; BIOSYNTHESIS; CATALYSIS; CHEMICAL REACTION; CONTROLLED STUDY; CYCLIZATION; ESCHERICHIA COLI; HYDROLYSIS; HYPOTHESIS; NONHUMAN; PRIORITY JOURNAL; ANAEROBIC GROWTH; CHEMISTRY; DRUG ANTAGONISM; ENZYME SPECIFICITY; ENZYMOLOGY; KINETICS; METABOLISM; PHYSIOLOGY;

ESCHERICHIA COLI;

ANAEROBIOSIS; CARBON-CARBON LYASES; CATALYSIS; CRESOLS; DEOXYADENOSINES; ENZYME INHIBITORS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KINETICS; S-ADENOSYLMETHIONINE; SUBSTRATE SPECIFICITY; TYROSINE;

EID: 77949318133     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.056606     Document Type: Article

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