Involvement of Glutamine-238 in the Substrate Specificity of Human Laeverin/Aminopeptidase Q
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- Goto Yoshikuni
- Laboratory of Cellular Biochemistry, RIKEN Faculty of Pharmaceutical Sciences, Teikyo-Heisei University
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- Yoshioka Rina
- Laboratory of Cellular Biochemistry, RIKEN
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- Arisaka Naomi
- Laboratory of Cellular Biochemistry, RIKEN
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- Hattori Akira
- Department of System Chemotherapy and Molecular Sciences, Graduate School of Pharmaceutical Sciences, Kyoto University
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- Tsujimoto Masafumi
- Laboratory of Cellular Biochemistry, RIKEN Faculty of Pharmaceutical Sciences, Teikyo-Heisei University
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Abstract
Human laeverin/aminopeptidase Q (APQ) is a novel member of the M1 family of zinc aminopeptidases and is specifically expressed on the cell surface of extravillous trophoblasts. In this study, we examined the significance of Gln-238 of laeverin/APQ, a putative S1 site residue, by site-directed mutagenesis for its enzymatic activity and substrate specificity. Replacement of Gln-238 with Ala caused a significant change in substrate specificity rather than a decrease in enzymatic activity. These results indicate that Gln-238 is important for the substrate specificity of laeverin/APQ. In addition, our data suggest that direct electrostatic interaction between substrate and S1 site of the enzyme is not involved in the mutant enzyme's preference for basic amino acids.
Journal
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- Biological and Pharmaceutical Bulletin
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Biological and Pharmaceutical Bulletin 34 (1), 24-27, 2011
The Pharmaceutical Society of Japan
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Keywords
Details 詳細情報について
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- CRID
- 1390282679602735616
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- NII Article ID
- 130000402257
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- NII Book ID
- AA10885497
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- ISSN
- 13475215
- 09186158
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- NDL BIB ID
- 10926677
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed