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A more recent version of this article appeared on October 5, 2001
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M103840200v1
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Papers In Press, published online ahead of print June 28, 2001
J. Biol. Chem, 10.1074/jbc.M103840200
Submitted on April 30, 2001
Revised on June 1, 2001
Accepted on June 28, 2001

Crystal structures of ACC synthase in complex with AVG and PLP provide new insight into catalytic mechanism

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

Biochemistry and Biophysics, Medical School, Chapel Hill, NC 27599

Corresponding Author: hke{at}med.unc.edu

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, proximity of Tyr152 to the Cg-S bond of model substrate SAM implies its critical role in the catalysis. The concerted accomplishment of catalysis by cofactor PLP and a protein residue, as proposed on 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 b subunit in fold type II and mouse ornithine decarboxylase in fold type III, thus suggesting a divergent evolution of PLP-dependent enzymes.


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