期刊论文详细信息
FEBS Letters
Families of zinc metalloproteases
Hooper, Nigel M.1 
[1] Department of Biochemistry and Molecular Biology, The University of Leeds, Leeds LS2 9JT, UK
关键词: Metalloproteinase;    Peptide hydrolase;    Zinc ligand;    Endopeptidase-24.11;    Aminopeptidases;    Angiotensin converting enzyme;   
DOI  :  10.1016/0014-5793(94)01079-X
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
PDF
【 摘 要 】

A scheme based on the zinc binding site [1992, FEBS Lett. 312, 110–114] has been extended to classify zinc metalloproteases into distinct families. The gluzincins, defined by the HEXXH motif and a glutamic acid as the third zinc ligand, include the thermolysin, endopeptidase-24.11, aminopeptidase, angiotensin converting enzyme, endopeptidase-24.15, and tetanus and botulinum neurotoxin families. The metzincins, defined by the HEXXH motif, a histidine as the third zinc ligand and a Met-turn, include the astacin, serralysin, reprolysin and matrixin families. The inverted zincin motif, HXXEH, defines the inverzincin family of insulin-degrading enzymes, the HXXE motif defines the carboxypeptidase family, and the HXH Motif dd-carboxypeptidase.

【 授权许可】

Unknown   

【 预 览 】
附件列表
Files Size Format View
RO201912020300224ZK.pdf 592KB PDF download
  文献评价指标  
  下载次数:21次 浏览次数:25次