Pyruvate carboxylase from Mycobacterium smegmatis: stabilization, rapid purification, molecular and biochemical characterization and regulation of the cellular level.

Mukhopadhyay, B; Purwantini, E

Mukhopadhyay, B; Purwantini, E.

Affiliation

Mukhopadhyay B; Department of Microbiology, University of Illinois at Urbana-Champaign, B103 Chemical and Life Sciences Laboratory, 601 S. Goodwin Avenue, Urbana, IL 61801, USA. biswarup@life.uiuc.edu

Biochim Biophys Acta ; 1475(3): 191-206, 2000 Jul 26.

Article in En | MEDLINE | ID: mdl-10913817

Subject(s)

Mycobacterium smegmatis/enzymology; Pyruvate Decarboxylase/isolation & purification; Adenosine Triphosphate/pharmacology; Amino Acid Sequence; Base Sequence; Binding Sites; Biotin; Catalysis; Cloning, Molecular; Culture Media; Enzyme Stability; Gene Expression Regulation, Enzymologic; Gene Library; Kinetics; Molecular Sequence Data; Mycobacterium smegmatis/genetics; Open Reading Frames; Pyruvate Decarboxylase/genetics; Pyruvate Decarboxylase/metabolism

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