Full metadata record
DC FieldValueLanguage
dc.contributor.authorChang, Chin-Yuanen_US
dc.contributor.authorHsieh, Yin-Chengen_US
dc.contributor.authorWang, Ting-Yien_US
dc.contributor.authorChen, Yi-Chinen_US
dc.contributor.authorWang, Yu-Kuoen_US
dc.contributor.authorChiang, Ting-Weien_US
dc.contributor.authorChen, Yi-Juen_US
dc.contributor.authorChang, Cheng-Hsiangen_US
dc.contributor.authorChen, Chun-Jungen_US
dc.contributor.authorWu, Tung-Kungen_US
dc.date.accessioned2014-12-08T15:47:39Z-
dc.date.available2014-12-08T15:47:39Z-
dc.date.issued2010-12-01en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://dx.doi.org/10.1074/jbc.M110.139683en_US
dc.identifier.urihttp://hdl.handle.net/11536/31885-
dc.description.abstractAminoacylhistidine dipeptidases (PepD, EC 3.4.13.3) belong to the family of M20 metallopeptidases from the metallopeptidase H clan that catalyze a broad range of dipeptide and tripeptide substrates, including L-carnosine and L-homocarnosine. Homocarnosine has been suggested as a precursor for the neurotransmitter gamma-aminobutyric acid (GABA) and may mediate the antiseizure effects of GABAergic therapies. Here, we report the crystal structure of PepD from Vibrio alginolyticus and the results of mutational analysis of substrate-binding residues in the C-terminal as well as substrate specificity of the PepD catalytic domain-alone truncated protein PepD(CAT). The structure of PepD was found to exist as a homodimer, in which each monomer comprises a catalytic domain containing two zinc ions at the active site center for its hydrolytic function and a lid domain utilizing hydrogen bonds between helices to form the dimer interface. Although the PepD is structurally similar to PepV, which exists as a monomer, putative substrate-binding residues reside in different topological regions of the polypeptide chain. In addition, the lid domain of the PepD contains an "extra" domain not observed in related M20 family metallopeptidases with a dimeric structure. Mutational assays confirmed both the putative di-zinc allocations and the architecture of substrate recognition. In addition, the catalytic domain-alone truncated PepD(CAT) exhibited substrate specificity to L-homocarnosine compared with that of the wild-type PepD, indicating a potential value in applications of PepD(CAT) for GABAergic therapies or neuroprotection.en_US
dc.language.isoen_USen_US
dc.titleCrystal Structure and Mutational Analysis of Aminoacylhistidine Dipeptidase from Vibrio alginolyticus Reveal a New Architecture of M20 Metallopeptidasesen_US
dc.typeArticleen_US
dc.identifier.doi10.1074/jbc.M110.139683en_US
dc.identifier.journalJOURNAL OF BIOLOGICAL CHEMISTRYen_US
dc.citation.volume285en_US
dc.citation.issue50en_US
dc.citation.spage39500en_US
dc.citation.epage39510en_US
dc.contributor.department生物科技學系zh_TW
dc.contributor.departmentDepartment of Biological Science and Technologyen_US
Appears in Collections:Articles


Files in This Item:

  1. 000284941300076.pdf

If it is a zip file, please download the file and unzip it, then open index.html in a browser to view the full text content.