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Journal of Bacteriology, August 1999, p. 4686-4689, Vol. 181, No. 15
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Amino Acid Residues Involved in the Functional Integrity of Escherichia coli Methionine Aminopeptidase

Chen-Hsiang Chiu,1 Chao-Zong Lee,1 Kung-Shih Lin,1 Ming F. Tam,2 and Lih-Yuan Lin1,*

Institute of Radiation Biology and Department of Life Science, National Tsing Hua University, Hsinchu,1 and Institute of Molecular Biology, Academia Sinica, Nankang, Taipei,2 Taiwan, Republic of China

Received 10 March 1999/Accepted 24 May 1999

Amino acid residues in the metal-binding and putative substrate-binding sites of Escherichia coli methionine aminopeptidase (MAP) were mutated, and their effects on the function of the enzyme were investigated. Substitution of any amino acid residue at the metal-binding site resulted in complete loss of the two cobalt ions bound to the protein and diminished the enzyme activity. However, only Cys70 and Trp221 at the putative substrate-binding site are involved in the catalytic activity of MAP. Changing either of them caused partial loss of enzyme activity, while mutations at both positions abolished MAP function. Both residues are found to be conserved in type I but not type II MAPs.

* Corresponding author. Mailing address: Department of Life Science, National Tsing Hua University, Hsinchu, Taiwan, ROC. Phone: 886-3-5742693. Fax: 886-3-5715934. E-mail: lylin{at}rb.nthu.edu.tw.

Journal of Bacteriology, August 1999, p. 4686-4689, Vol. 181, No. 15
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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