InterPro : IPR017297

Name  Peptidase S8A, DPH-A Short Name  Peptidase_S8A_DPH-A
Type  Family Description  Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes []. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identified, these being grouped into clans on the basis of structural similarity and other functional evidence []. Structures are known for members of the clans and the structures indicate that some appear to be totally unrelated, suggesting different evolutionary origins for the serine peptidases [].Not withstanding their different evolutionary origins, there are similarities in the reaction mechanisms of several peptidases. Chymotrypsin, subtilisin and carboxypeptidase C have a catalytic triad of serine, aspartate and histidine in common: serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base []. The geometric orientations of the catalytic residues are similar between families, despite different protein folds []. The linear arrangements of the catalytic residues commonly reflect clan relationships. For example the catalytic triad in the chymotrypsin clan (PA) is ordered HDS, but is ordered DHS in the subtilisin clan (SB) and SDH in the carboxypeptidase clan (SC) [, ].Limited proteolysis of most large protein precursors is carried out in vivo by the subtilisin-like pro-protein convertases. Many important biological processes such as peptide hormone synthesis, viral protein processing and receptor maturation involve proteolytic processing by these enzymes []. The subtilisin-serine protease (SRSP) family hormone and pro-protein convertases (furin, PC1/3, PC2, PC4, PACE4, PC5/6, and PC7/7/LPC) act within the secretory pathway to cleave polypeptide precursors at specific basic sites, generating their biologically active forms. Serum proteins, pro-hormones, receptors, zymogens, viral surface glycoproteins, bacterial toxins, amongst others, are activated by this route []. The SRSPs share the same domain structure, including a signal peptide, the pro-peptide, the catalytic domain, the P/middle or homo B domain, and the C terminus.This entry contains serine peptidases belonging to MEROPS peptidase family S8A (subtilisin family, clan SB). This family of serine peptidases are highly similar in both structural and enzymatic feature to SAM-P45 peptidases, which are known as a target enzyme of Streptomyces subtilisin inhibitor (SSI), from Streptomyces albogriseolus.DPH-A effectively forms chiral intermediates of 1,4-dihydropyridine calcium antagonists, and suggests the feasibility of developing DHP-A as a new commercial enzyme for use in the chiral drug industry [].
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

2 Contains

Id Name Short Name Type
IPR000209 Peptidase S8/S53 domain Peptidase_S8/S53_dom Domain
IPR022398 Peptidase S8, subtilisin, His-active site Peptidase_S8_His-AS Active_site

0 Found In

1 Parent Features

Id Name Short Name Type
IPR015500 Peptidase S8, subtilisin-related Peptidase_S8_subtilisin-rel Family

5 Publications

First Author Title Year Journal Volume Pages
Rawlings ND Evolutionary families of peptidases. 1993 Biochem J 290 ( Pt 1) 205-18
Rawlings ND Families of serine peptidases. 1994 Methods Enzymol 244 19-61
Bergeron F Subtilase-like pro-protein convertases: from molecular specificity to therapeutic applications. 2000 J Mol Endocrinol 24 1-22
Gensberg K Subtilisin-related serine proteases in the mammalian constitutive secretory pathway. 1998 Semin Cell Dev Biol 9 11-7
Arisawa A Streptomyces serine protease (DHP-A) as a new biocatalyst capable of forming chiral intermediates of 1,4-dihydropyridine calcium antagonists. 2002 Appl Environ Microbiol 68 2716-25



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)