Structure, catalytic mechanism, posttranslational lysine carbamylation, and inhibition of dihydropyrimidinases

doi:10.1016/bs.apcsb.2020.05.002

中山醫學大學機構典藏 CSMUIR > 中山醫學大學研究成果 > 其他文獻 > Item 310902500/25058

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题名:	Structure, catalytic mechanism, posttranslational lysine carbamylation, and inhibition of dihydropyrimidinases
作者:	Huang, CY
日期:	2020
上传时间:	2022-08-09T09:27:45Z (UTC)
出版者:	ACADEMIC PRESS LTD-ELSEVIER SCIENCE LTD
ISSN:	1876-1623
摘要:	Dihydropyrimidinase catalyzes the reversible hydrolytic ring opening of dihydrouracil and dihydrothymine to N-carbamoyl-beta-alanine and N-carbamyl-beta-aminoisobutyrate, respectively. Dihydropyrimidinase from microorganisms is normally known as hydantoinase because of its role as a biocatalyst in the synthesis of D- and L-amino acids for the industrial production of antibiotic precursors and its broad substrate specificity. Dihydropyrimidinase belongs to the cyclic amidohydrolase family, which also includes imidase, allantoinase, and dihydroorotase. Although these metal-dependent enzymes share low levels of amino acid sequence homology, they possess similar active site architectures and may use a similar mechanism for catalysis. By contrast, the five human dihydropyrimidinase-related proteins possess high amino acid sequence identity and are structurally homologous to dihydropyrimidinase, but they are neuronal proteins with no dihydropyrimidinase activity. In this chapter, we summarize and discuss current knowledge and the recent advances on the structure, catalytic mechanism, and inhibition of dihydropyrimidinase.
URI:	http://dx.doi.org/10.1016/bs.apcsb.2020.05.002 https://www.webofscience.com/wos/woscc/full-record/WOS:000610803000003 https://ir.csmu.edu.tw:8080/handle/310902500/25058
關聯:	ADVANCES IN PROTEIN CHEMISTRY AND STRUCTURAL BIOLOGY, VOL 122 ,2020 ,v122 ,p63-96
显示于类别:	[中山醫學大學研究成果] 其他文獻

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