Biochemical characterization of argininosuccinate lyase from M. tuberculosis: significance of a c‐terminal cysteine in catalysis and thermal stability

Arginine biosynthesis pathway is crucial to the survival and pathogenesis of Mycobacterium tuberculosis (Mtb). Arginine is a critical amino acid that contributes to the inflection of cellular immune responses during pathogenesis. Argininosuccinate lyase from Mtb (MtArgH), the last enzyme in the path...

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Veröffentlicht in:	IUBMB life 2017-11, Vol.69 (11), p.896-907
Hauptverfasser:	Mishra, Archita, Surolia, Avadhesha
Format:	Artikel
Sprache:	eng
Schlagworte:	Alanine Amino Acid Sequence Amino acids Arginine Arginine - metabolism arginine biosynthesis Argininosuccinate lyase Argininosuccinate Lyase - chemistry Argininosuccinate Lyase - genetics Argininosuccinate Lyase - metabolism Argininosuccinic Acid - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Binding Sites Biocatalysis Catalysis Chemical modification Cloning, Molecular Cysteine Cysteine - chemistry Cysteine - metabolism cysteine modification Enzymatic activity enzyme catalysis Enzyme Stability Enzymes Escherichia coli - genetics Escherichia coli - metabolism Gene Expression Genetic Vectors - chemistry Genetic Vectors - metabolism Immune response Immune response (cell-mediated) Kinetics Mutagenesis, Site-Directed Mycobacterium tuberculosis Mycobacterium tuberculosis - chemistry Mycobacterium tuberculosis - enzymology Pathogenesis Protein Binding Protein structure Protein Structure, Secondary Quaternary structure Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Alignment Sequence Homology, Amino Acid Serine Serine - chemistry Serine - metabolism Structure-Activity Relationship Substrate Specificity Thermal stability Thermophilic microorganisms Tuberculosis
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