A role for glutamate-333 of Saccharomyces cerevisiae cystathionine γ-lyase as a determinant of specificity

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1844, Issue 2, 2014, Pages 465-472

  Hopwood, Emily M S ^a   Ahmed, Duale ^a   Aitken, Susan M ^a  

^a CARLETON UNIVERSITY   (Canada)

Author keywords

Pyridoxal 5' phosphate; Reaction specificity; Structure function relationships

Indexed keywords

CYSTATHIONINE GAMMA LYASE; GLUTAMATE 333; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CHEMICAL STRUCTURE; ENZYME ACTIVITY; ENZYME STABILITY; HYDROLYSIS KINETICS; NONHUMAN; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE;

1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE; 2-(BIS(2-HYDROXYETHYL)AMINO)ACETIC ACID; 3-(CYCLOHEXYLAMINO)-1-PROPANESULFONIC ACID; 5,5′-DITHIOBIS(2-NITROBENZOIC ACID); AAT; ACCS; AMPSO; ASPARTATE AMINOTRANSFERASE; BICINE; CAPS; CBL; CGL; CGS; CYSTATHIONINE Β-LYASE; CYSTATHIONINE Γ-LYASE; CYSTATHIONINE Γ-SYNTHASE; D-2-HYDROXYISOCAPROATE DEHYDROGENASE; DTNB; HO-HXODH; IPTG; ISOPROPYL-Β-D-THIOGALACTOPYRANOSIDE; L-CTH; L-CYSTATHIONINE; L-HCYS; L-HOMOCYSTEINE; L-LACTATE DEHYDROGENASE; L-OAS; L-OSHS; LDH; METHIONINE Γ-LYASE; MGL; N-(1,1-DIMETHYL-2-HYDROXYETHYL)-3-AMINO-2-HYDROXYPROPANESULFONIC ACID; N-[TRIS(HYDROXYMETHYL)METHYL]-3-AMINOPROPANESULFONIC ACID; NADH (REDUCED FORM); NI-NITRILO TRIACETIC ACID; NI-NTA; O-ACETYL-L-SERINE; O-SUCCINYL-L-HOMOSERINE; OAS SULFHYDRYLASE; OASS; PLP; PYRIDOXAL 5'-PHOSPHATE; PYRIDOXAL 5′-PHOSPHATE; REACTION SPECIFICITY; STRUCTURE-FUNCTION RELATIONSHIPS; TAPS; Β-NICOTINAMIDE ADENINE DINUCLEOTIDE;

CATALYTIC DOMAIN; CYSTATHIONINE GAMMA-LYASE; ESCHERICHIA COLI PROTEINS; GLUTAMIC ACID; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; LYASES; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; SACCHAROMYCES CEREVISIAE; SUBSTRATE SPECIFICITY;

EID: 84891525039     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2013.11.012     Document Type: Article

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