Dissection of contributions from invariant amino acids to complex formation and catalysis in the heteromeric pyridoxal 5-phosphate synthase complex from Bacillus subtilis

Biochemistry

Volumn 48, Issue 9, 2009, Pages 1928-1935

  Wallner, Silvia ^a   Neuwirth, Martina ^a   Flicker, Karlheinz ^a   Tews, Ivo ^b   Macheroux, Peter ^a,c  

^a GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

^b UNIVERSITY OF HEIDELBERG   (Germany)

^c GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION MECHANISMS; ACTIVE SITES; BACILLUS SUBTILIS; BIOCHEMICAL CHARACTERIZATIONS; BIOCHEMICAL REACTIONS; CATALYTIC ACTIVATIONS; CATALYTIC CENTERS; COFACTORS; COMPLEX FORMATIONS; ENCOUNTER COMPLEXES; ENZYMATIC ACTIVITIES; ENZYME ACTIVATIONS; GLUTAMINASE; INTERFACE FORMATIONS; ISOTHERMAL CALORIMETRIES; L GLUTAMINES; MICHAELIS COMPLEXES; MULTI STEPS; N TERMINALS; OXYANION HOLES; PROTEIN VARIANTS; SITE-DIRECTED MUTAGENESIS; SUBSTRATE BINDINGS; SYNTHASE; VITAMIN B-6;

ACTIVATION ANALYSIS; AMINES; AMINO ACIDS; BACTERIOLOGY; BINDING SITES; BIOCHEMICAL ENGINEERING; BIOCHEMISTRY; ENZYMES; ORGANIC ACIDS; POSITIVE IONS; STRUCTURAL ANALYSIS; THREE DIMENSIONAL;

ENZYME ACTIVITY;

GLUTAMINASE; GLUTAMINE; PYRIDOXAL 5 PHOSPHATE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR PDX 1; TRANSCRIPTION FACTOR PDX2; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS SUBTILIS; CALORIMETRY; CATALYSIS; CONTROLLED STUDY; DISSECTION; ENZYME ACTIVATION; ENZYME ACTIVITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION; PROTEIN VARIANT; SITE DIRECTED MUTAGENESIS; STRUCTURE ANALYSIS; THERMODYNAMICS;

BACILLUS SUBTILIS; BACTERIAL PROTEINS; CATALYSIS; GLUTAMINASE; KINETICS; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; PYRIDOXAL PHOSPHATE; SUBSTRATE SPECIFICITY;

BACILLUS SUBTILIS;

EID: 64549111287     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801887r     Document Type: Article

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