Structural features of a superfamily of zinc-endopeptidases: the metzincins

by: W Stocker, W Bode

Current Opinion in Structural Biology (June 1995), pp. 383-390.

View FullText article

IngentaConnect

Reviews [Write a review of this article]

There are no reviews of this article

Find related articles from these CiteULike users

cjhall

Find related articles with these CiteULike tags

no-tag

Abstract

A large number of zinc endopeptidases contain an HEXXHXXGXXH consensus motif in their catalytic site (single letter code; X is any amino acid residue). These enzymes can be grouped into four distinct families, the astacins, the adamalysins, the serralysins and the matrix metalloproteinases (matrixins). Despite a low degree of sequence similarity, their catalytic modules are topologically similar. A topology derived sequence alignment suggests that the four families form a superfamily, called the metzincins because of a perfectly superimposable methionine residue close to the zinc-binding active site. Topological similarity to the thermolysin-like enzymes indicates that these enzymes may have had a common ancestor.

@article{citeulike:2623572, abstract = {A large number of zinc endopeptidases contain an HEXXHXXGXXH consensus motif in their catalytic site (single letter code; X is any amino acid residue). These enzymes can be grouped into four distinct families, the astacins, the adamalysins, the serralysins and the matrix metalloproteinases (matrixins). Despite a low degree of sequence similarity, their catalytic modules are topologically similar. A topology derived sequence alignment suggests that the four families form a superfamily, called the metzincins because of a perfectly superimposable methionine residue close to the zinc-binding active site. Topological similarity to the thermolysin-like enzymes indicates that these enzymes may have had a common ancestor.}, author = {Stocker, W. and Bode, W. }, citeulike-article-id = {2623572}, issn = {0959-440X}, journal = {Current Opinion in Structural Biology}, month = {June}, pages = {383--390}, posted-at = {2008-04-02 15:38:06}, priority = {2}, title = {Structural features of a superfamily of zinc-endopeptidases: the metzincins}, url = {http://www.ingentaconnect.com/content/els/0959440x/1995/00000005/00000003/art80101}, year = {1995} }

RIS record

TY - JOUR ID - citeulike:2623572 L3 - citeulike-article-id:2623572 TI - Structural features of a superfamily of zinc-endopeptidases: the metzincins JF - Current Opinion in Structural Biology SP - 383 EP - 390 SN - 0959-440X N2 - A large number of zinc endopeptidases contain an HEXXHXXGXXH consensus motif in their catalytic site (single letter code; X is any amino acid residue). These enzymes can be grouped into four distinct families, the astacins, the adamalysins, the serralysins and the matrix metalloproteinases (matrixins). Despite a low degree of sequence similarity, their catalytic modules are topologically similar. A topology derived sequence alignment suggests that the four families form a superfamily, called the metzincins because of a perfectly superimposable methionine residue close to the zinc-binding active site. Topological similarity to the thermolysin-like enzymes indicates that these enzymes may have had a common ancestor. AU - Stocker, W AU - Bode, W PY - 1995/06// UR - http://www.ingentaconnect.com/content/els/0959440x/1995/00000005/00000003/art80101 ER -

RIS BibTeX