Crystal Structures of Complexes of the Branched-Chain Aminotransferase from Deinococcus radiodurans with α-Ketoisocaproate and l-Glutamate Suggest the Radiation Resistance of This Enzyme for Catalysis

Branched-chain aminotransferases (BCAT), which utilize pyridoxal 5′-phosphate (PLP) as a cofactor, reversibly catalyze the transfer of the α-amino groups of three of the most hydrophobic branched-chain amino acids (BCAA), leucine, isoleucine, and valine, to α-ketoglutarate to form the respective bra...

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Veröffentlicht in:	Journal of Bacteriology 2012-11, Vol.194 (22), p.6206-6216
Hauptverfasser:	Chen, Chung-De, Lin, Chih-Hao, Chuankhayan, Phimonphan, Huang, Yen-Chieh, Hsieh, Yin-Cheng, Huang, Tien-Feng, Guan, Hong-Hsiang, Liu, Ming-Yih, Chang, Wen-Chang, Chen, Chun-Jung
Format:	Artikel
Sprache:	eng
Schlagworte:	active sites alpha-ketoglutaric acid Amino Acid Sequence Bacteriology Biological and medical sciences Catalysis catalytic activity Catalytic Domain crystal structure Crystallization Crystallography, X-Ray cysteine Deinococcus - enzymology Deinococcus radiodurans Enzyme Stability Escherichia coli extremophiles Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Bacterial Gene Expression Regulation, Enzymologic glutamic acid Glutamic Acid - chemistry hydrogen bonding hydrophobicity ionizing radiation isoleucine Keto Acids - chemistry leucine Microbiology Miscellaneous Models, Molecular Molecular Sequence Data mutation Protein Conformation radiation resistance Spectrophotometry Substrate Specificity thermal stability Thermus thermophilus transaminases Transaminases - chemistry Transaminases - metabolism valine
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