Effects of the E177K mutation in-amino acid transaminase. studies on an essential coenzyme anchoring group that contributes to stereochemical fidelity. Export

@article{van99, abstract = {D-Amino acid transaminase is a bacterial enzyme that uses pyridoxal phosphate (PLP) as a cofactor to catalyze the conversion of D-amino acids into their corresponding alpha-keto acids. This enzyme has already been established as a target for novel antibacterial agents through suicide inactivation by a number of compounds. To improve their potency and specificity, the detailed enzyme mechanism, especially the role of its PLP cofactor, is under investigation. Many PLP-dependent transaminases have a negatively charged amino acid residue forming a salt-bridge with the pyridine nitrogen of its cofactor that promotes its protonation to stabilize the formation of a ketimine intermediate, which is subsequently hydrolyzed in the normal transaminase reaction pathway. However, alanine racemase has a positively charged arginine held rigidly in place by an extensive hydrogen bond network that may destabilize the ketimine intermediate, and make it...}, address = {Northeastern University, Boston, Massachusetts 02115, USA.}, author = {van Ophem, P. W. and Peisach, D. and Erickson, S. D. and Soda, K. and Ringe, D. and Manning, J. M.}, citeulike-article-id = {388916}, editor = {1999/02/04}, journal = {Biochemistry}, keywords = {deaminase, enzyme, glu, mechanism, mutation}, number = {4}, posted-at = {2005-11-11 16:23:16}, priority = {2}, title = {Effects of the {E}177{K} mutation in-amino acid transaminase. studies on an essential coenzyme anchoring group that contributes to stereochemical fidelity.}, volume = {38}, year = {1999} }

TY - JOUR ID - van99 L3 - citeulike-article-id:388916 N2 - D-Amino acid transaminase is a bacterial enzyme that uses pyridoxal phosphate (PLP) as a cofactor to catalyze the conversion of D-amino acids into their corresponding alpha-keto acids. This enzyme has already been established as a target for novel antibacterial agents through suicide inactivation by a number of compounds. To improve their potency and specificity, the detailed enzyme mechanism, especially the role of its PLP cofactor, is under investigation. Many PLP-dependent transaminases have a negatively charged amino acid residue forming a salt-bridge with the pyridine nitrogen of its cofactor that promotes its protonation to stabilize the formation of a ketimine intermediate, which is subsequently hydrolyzed in the normal transaminase reaction pathway. However, alanine racemase has a positively charged arginine held rigidly in place by an extensive hydrogen bond network that may destabilize the ketimine intermediate, and make it... IS - 4 JF - Biochemistry AD - Northeastern University, Boston, Massachusetts 02115, USA. TI - Effects of the {E}177{K} mutation in-amino acid transaminase. studies on an essential coenzyme anchoring group that contributes to stereochemical fidelity. VL - 38 KW - deaminase KW - enzyme KW - glu KW - mechanism KW - mutation AU - van Ophem, PW AU - Peisach, D AU - Erickson, SD AU - Soda, K AU - Ringe, D AU - Manning, JM A2 - 1999/02/04 PY - 1999/// ER -