1994
DOI: 10.1016/0076-6879(94)44004-2
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[2] Families of serine peptidases

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Cited by 558 publications
(448 citation statements)
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“…Although no significant protease sequence identities were found outside the catalytic sites, the MyxSP-1 protein sequence did contain the conserved catalytic triad and surrounding amino acid residues that are characteristic for serine proteases (present Fig. 2, and Rawlings & Barrett 1994, Barrett & Rawlings 1995. In addition, Rawlings & Barrett (1994) reported that a key aspect of the evolutionary division of serine proteases is based on the linear sequence arrangement of the catalytic residues.…”
Section: Discussionmentioning
confidence: 86%
See 1 more Smart Citation
“…Although no significant protease sequence identities were found outside the catalytic sites, the MyxSP-1 protein sequence did contain the conserved catalytic triad and surrounding amino acid residues that are characteristic for serine proteases (present Fig. 2, and Rawlings & Barrett 1994, Barrett & Rawlings 1995. In addition, Rawlings & Barrett (1994) reported that a key aspect of the evolutionary division of serine proteases is based on the linear sequence arrangement of the catalytic residues.…”
Section: Discussionmentioning
confidence: 86%
“…2, and Rawlings & Barrett 1994, Barrett & Rawlings 1995. In addition, Rawlings & Barrett (1994) reported that a key aspect of the evolutionary division of serine proteases is based on the linear sequence arrangement of the catalytic residues. The linear sequence data for the catalytic triad of MyxSP-1 (His-54, Asp-248, Ser-310) indicates an evolutionary affinity with chymotrypsin-like serine proteases.…”
Section: Discussionmentioning
confidence: 99%
“…In the present study, three conserved active sites associated with the enzyme activity, Cys141, His280 and Asn300, were found in CpCL. The second amino acids of CpCL mature peptide was Pro, which might be helpful to keep the N-end of the protein being unhydrolyzed [27]. In addition, six potential substrate binding sites, Leu185, Met186, Ala251, Asn278, Gly281 and Ala 327 were observed in CpCL, which exhibited a marked preference for bulky hydrophobic or aromatic residues in the sidechain position of the substrate [28].…”
Section: Discussionmentioning
confidence: 99%
“…1d) similar to other proteases, including that encoded by the homologous gene TMPRSS2, which also maps on 21q, centromeric to the DFNB10 critical region 10 . The serine protease domain (residues 217-444) is compatible with the S1 family of the PA clan of serine-type peptidases (serine or cysteine nucleophile; catalytic residues in the order His, Asp, Ser (or Cys) in sequence; all endopeptidases) for which the prototype is chymotrypsin 11 , and shows between 45 and 38% identity with other transmembrane serine proteases (Fig. 1f).…”
Section: Division Of Medical Genetics University Of Geneva Medicalmentioning
confidence: 98%