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J. Biol. Chem., Vol. 276, Issue 41, 38210-38216, October 12, 2001

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Crystal Structures of 1-Aminocyclopropane-1-carboxylate (ACC) Synthase in Complex with Aminoethoxyvinylglycine and Pyridoxal-5'-Phosphate Provide New Insight into Catalytic Mechanisms^*

Qing Huai, Yuanhong Xia, Yongquan Chen, Brian Callahan, Ning Li^§, and Hengming Ke^¶

From the  Department of Biochemistry and Biophysics and Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, North Carolina 27599-7260 and the ^§ Department of Biology, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong

The structures of tomato 1-aminocyclopropane-1-carboxylate synthase (ACS) in complex with either cofactor pyridoxal-5'-phosphate (PLP) or both PLP and inhibitor aminoethoxyvinylglycine have been determined by x-ray crystallography. The structures showed good conservation of the catalytic residues, suggesting a similar catalytic mechanism for ACS and other PLP-dependent enzymes. However, the proximity of Tyr¹⁵² to the C--S bond of model substrate S-adenosylmethionine implies its critical role in the catalysis. The concerted accomplishment of catalysis by cofactor PLP and a protein residue, as proposed on the basis of the ACS structures in this paper, may represent a general scheme for the diversity of PLP-dependent catalyses. PLP-dependent enzymes have been categorized into four types of folds. A structural comparison revealed that a core fragment of ACS in fold type I is superimposable over tryptophan synthase  subunit in fold type II and mouse ornithine decarboxylase in fold type III, thus suggesting a divergent evolution of PLP-dependent enzymes.

The atomic coordinates and the structure factors (code 1IAX and 1IAY) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

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