Cloning and sequencing of<i>Serratia</i>protease gene

Nakahama, Kazuo; Yoshimura, Koji; Marumoto, Ryuji; Kikuchi, Masakazu; Lee, In Sook; Hase, Toshiharu; Matsubara, Hiroshi

doi:10.1093/nar/14.14.5843

Cited by 189 publications

(105 citation statements)

References 29 publications

(29 reference statements)

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“…haemolytica Al, like other neutral metalloproteases of bacteria, such as thermolysin (18), can be inhibited by metal ion chelators, but there is no major sequence homology with these enzymes except for the presence of a potential zinc-binding site (Fig. 6).…”

Section: Discussionmentioning

confidence: 99%

Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene

Abdullah

Mellors

1991

J Bacteriol

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Pasteurella haemolytica serotype Al secretes a glycoprotease which is specific for 0-sialoglycoproteins such as glycophorin A. The gene encoding the glycoprotease enzyme has been cloned in the recombinant plasmid pPHl, and its nucleotide sequence has been determined. The gene (designated gcp) codes for a protein of 35.2 kDa, and an active enzyme protein of this molecular mass can be observed in Escherichia coli clones carrying pPHl. In vivo labeling of plasmid-encoded proteins in E. coli maxicells demonstrated the expression of a 35-kDa protein from pPHl. The amino-terminal sequence of the heterologously expressed protein corresponds to that predicted from the nucleotide sequence. The glycoprotease is a neutral metalloprotease, and the predicted amino acid sequence of the glycoprotease contains a putative zinc-binding site. The gene shows no significant homology with the genes for other proteases of procaryotic or eucaryotic origin. However, there is substantial homology between gcp and an E. coli gene, orJX, whose product is believed to function in the regulation of macromolecule biosynthesis.

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Section: Discussionmentioning

confidence: 99%

Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene

Abdullah

Mellors

1991

J Bacteriol

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“…Serralysins: alk proteinase, alkaline proteinase from Pseudomonas aeruginosa (Okuda et al, 1990;Duong et al, 1992); Erwinia b, Erwinia chrysanthemi proteinase b (Delepelaire & Wandersman, 1989;Dahler et al, 1992); serralysin, Serratia marcescens proteinase (Nakahama et al, 1986). Adamalysins/reprolysins: adamalysin I1 from Crotalus adamanteus (Gomis-Ruth et al, 1994a); EAP I from rat epididymis (Perry et al, 1992); cyritestin from mouse testis (Heinlein et al, 1994).…”

Section: The Northern Wall Of the Active Site Cleftmentioning

confidence: 99%

“…The serralysins are a family of proteolytic enzymes (see reviews by Morihara, 1974;Hase & Finkelstein, 1994) that are secreted into their environment by various pathogenic bacteria of the genera Serratia (Nakahama et al, 1986), Pseudomonas (Okuda et al, 1990;Duong et al, 1992), and Erwinia (Delepelaire & Wandersman, 1989; Dahler et al, 1990). Besides an N-terminal extension, these proteases consist of two modules, an N-terminal proteolytic module and a C-terminal calciumbinding regulatory module (Baumann et al, 1993;Baumann, 1994).…”

mentioning

confidence: 99%

The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases

et al. 1995

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The three-dimensional structures of the zinc endopeptidases human neutrophil collagenase, adamalysin I1 from rattle snake venom, alkaline proteinase from Pseudomonas aeruginosa, and astacin from crayfish are topologically similar, with respect to a five-stranded 0-sheet and three a-helices arranged in typical sequential order. The four proteins exhibit the characteristic consensus motif HEXXHXXGXXH, whose three histidine residues are involved in binding of the catalytically essential zinc ion. Moreover, they all share a conserved methionine residue beneath the active site metal as part of a superimposable "Met-turn.'' This structural relationship is supported by a sequence alignment performed on the basis of topological equivalence showing faint but distinct sequential similarity. The alkaline proteinase is about equally distant (26% sequence identity) to both human neutrophil collagenase and astacin and a little further away from adamalysin I1 (17% identity). The pairs astacin/adamalysin 11, astacidhuman neutrophil collagenase, and adamalysin Whuman neutrophil collagenase exhibit sequence identities of 16%, 14%, and 13%, respectively. Therefore, the corresponding four distinct families of zinc peptidases, the astacins, the matrix metalloproteinases (matrixins, collagenases), the adamalysins/reprolysins (snake venom proteinases/reproductive tract proteins), and the serralysins (large bacterial proteases from Serratia, Erwinia, and Pseudomonas) appear to have originated by divergent evolution from a common ancestor and form a superfamily of proteolytic enzymes for which the designation "metzincins" has been proposed. There is also a faint but significant structural relationship of the metzincins to the thermolysin-like enzymes, which share the truncated zincbinding motif HEXXH and, moreover, similar topologies in their N-terminal domains.Keywords: crystal structure; metalloproteinase; molecular evolution; protein family; sequence alignment; topology is involved in metal binding (McKerrow, 1987;

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“…Great variability is present in the more than 30 amino acids between the second and third conserved regions. Several bacterial extracellular metalloproteases, including a protease from Serratia sp., and protease B and C from Erwinia chrysanthemi [19][20][21][22], show a closer relationship to each other than to members of the thermolysin family (Fig. 3).…”

Section: Familiesmentioning

confidence: 99%

Families of metalloendopeptidases and their relationships

1992

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Crystal structures available for four metalloendopeptidascs have revealed zinc ligands for these enzymes. New sequence information has made it possible to compare the primary structures of the zinc-binding site in metalloendapeptidases. A scheme based on the zinc-bindin8 sit~ is proposed to classify metalloendopeptidases into five distinct families: thermolysin, astacin, serratia, matrixin, and snake venom metalloproteinases. Two histidlnes and one 81utamate are zinc-ligands in the thermolysin family. Three histiciincs and one tyrosine are zinc ligands in the other four families, which are further distinguished by the identity of the residue following the third histidine and by the environment surrounding the tyro~iae.

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Cloning and sequencing ofSerratiaprotease gene

Cited by 189 publications

References 29 publications

Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene

Cloning, nucleotide sequence, and expression of the Pasteurella haemolytica A1 glycoprotease gene

The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases

Families of metalloendopeptidases and their relationships

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