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Carboxypeptidase D

January 01, 1970

Carboxypeptidase D can refer to one of several enzymes. A family of serine carboxypeptidases (i.e. enzymes that use an active site serine residue) includes (EC 3.4.16.6, cereal serine carboxypeptidase II, Saccharomyces cerevisiae KEX1 gene product, carboxypeptidase Kex1, gene KEX1 serine carboxypeptidase, KEX1 carboxypeptidase, KEX1 proteinase, KEX1DELTAp, CPDW-II, serine carboxypeptidase, Phaseolus proteinase) is an enzyme.[1][2][3][4] This enzyme has an optimal pH of 4.5-6.0, is inhibited by diisopropyl fluorophosphate, and catalyses the following chemical reaction

Carboxypeptidase D
Identifiers
EC no.3.4.16.6
CAS no.153967-26-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
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PubMedarticles
NCBIproteins
Preferential release of a C-terminal arginine or lysine residue

A completely distinct enzyme has also been named carboxypeptidase D (EC number 3.4.17.22). This second enzyme is a metallocarboxypeptidase (i.e. uses a zinc ion in the active site instead of a serine residue) and is broadly expressed in mammalian tissues.[5] Like the serine carboxypeptidase, the metallocarboxypeptidase D also removes C-terminal arginine or lysine residues from peptides, with an optimal pH range of 5 to 7. Metallocarboxypeptidase D is located in the trans Golgi network where it contributes to the biosynthesis of neuropeptides and peptide hormones (such as insulin) along with carboxypeptidase E. In addition to this role, metallocarboxypeptidase D contributes to the processing of proteins, following the action of furin (an endoprotease located in the trans Golgi network). The duck ortholog of metallocarboxypeptidase D was named gp180 and is a receptor for uptake of duck hepatitis B virus.[6] In fruit fly (Drosophila melanogaster), carboxypeptidase D is known as the silver mutation, with defects causing altered wing shape.[7] Metallocarboxypeptidase D is generally a membrane-bound protein, although in some organisms a soluble form is generated by either differential RNA splicing or by proteolytic activity.[8][9] In the scientific literature, most of the published articles using the name "Carboxypeptidase D" in the title refer to metallocarboxypeptidase D and not the serine carboxypeptidase.

References edit

  1. ^ Breddam, K. (1986). "Serine carboxypeptidases. A review". Carlsberg Res. Commun. 51 (2): 83–128. doi:10.1007/bf02907561.
  2. ^ Breddam, K.; Sørensen, S.B.; Svendsen, I. (1987). "Primary structure and enzymatic properties of carboxypeptidase II from wheat bran". Carlsberg Res. Commun. 52 (4): 297–311. doi:10.1007/bf02907172.
  3. ^ Dmochowska, A.; Dignard, D.; Henning, D.; Thomas, D.Y.; Bussey, H. (1987). "Yeast KEX1 gene encodes a putative protease with a carboxypeptidase B-like function involved in killer toxin and α-factor precursor processing". Cell. 50 (4): 573–584. doi:10.1016/0092-8674(87)90030-4. PMID 3301004. S2CID 22884209.
  4. ^ Liao, D.-I.; Breddam, K.; Sweet, R.M.; Bullock, T.; Remington, S.J. (1992). "Refined atomic model of wheat serine carboxypeptidase II at 2.2-Å resolution". Biochemistry. 31 (40): 9796–9812. doi:10.1021/bi00155a037. PMID 1390755.
  5. ^ Song L, Fricker LD (1995). "Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary". J. Biol. Chem. 270 (42): 25007–13. doi:10.1074/jbc.270.42.25007. PMID 7559630.
  6. ^ Eng FJ, Novikova EG, Kuroki K, Ganem D, Fricker LD (1998). "gp180, a protein that binds duck hepatitis B virus particles, has metallocarboxypeptidase D-like enzymatic activity". J. Biol. Chem. 273 (14): 8382–8. doi:10.1074/jbc.273.14.8382. PMID 9525948.
  7. ^ Settle SH, Green MM, Burtis KC (1995). "The silver gene of Drosophila melanogaster encodes multiple carboxypeptidases similar to mammalian prohormone-processing enzymes". Proc Natl Acad Sci U S A. 92 (21): 9470–4. Bibcode:1995PNAS...92.9470S. doi:10.1073/pnas.92.21.9470. PMC 40823. PMID 7568156.
  8. ^ Sidyelyeva G, Fricker LD (2002). "Characterization of Drosophila carboxypeptidase D". J. Biol. Chem. 277 (51): 49613–20. doi:10.1074/jbc.M209652200. PMID 12393882.
  9. ^ Song L, Fricker LD (1996). "Tissue distribution and characterization of soluble and membrane-bound forms of metallocarboxypeptidase D." J. Biol. Chem. 271 (46): 28884–9. doi:10.1074/jbc.271.46.28884. PMID 8910535.

External links edit

January 01, 1970
carboxypeptidase, refer, several, enzymes, family, serine, carboxypeptidases, enzymes, that, active, site, serine, residue, includes, cereal, serine, carboxypeptidase, saccharomyces, cerevisiae, kex1, gene, product, carboxypeptidase, kex1, gene, kex1, serine, . Carboxypeptidase D can refer to one of several enzymes A family of serine carboxypeptidases i e enzymes that use an active site serine residue includes EC 3 4 16 6 cereal serine carboxypeptidase II Saccharomyces cerevisiae KEX1 gene product carboxypeptidase Kex1 gene KEX1 serine carboxypeptidase KEX1 carboxypeptidase KEX1 proteinase KEX1DELTAp CPDW II serine carboxypeptidase Phaseolus proteinase is an enzyme 1 2 3 4 This enzyme has an optimal pH of 4 5 6 0 is inhibited by diisopropyl fluorophosphate and catalyses the following chemical reactionCarboxypeptidase DIdentifiersEC no 3 4 16 6CAS no 153967 26 1DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumSearchPMCarticlesPubMedarticlesNCBIproteins Preferential release of a C terminal arginine or lysine residue A completely distinct enzyme has also been named carboxypeptidase D EC number 3 4 17 22 This second enzyme is a metallocarboxypeptidase i e uses a zinc ion in the active site instead of a serine residue and is broadly expressed in mammalian tissues 5 Like the serine carboxypeptidase the metallocarboxypeptidase D also removes C terminal arginine or lysine residues from peptides with an optimal pH range of 5 to 7 Metallocarboxypeptidase D is located in the trans Golgi network where it contributes to the biosynthesis of neuropeptides and peptide hormones such as insulin along with carboxypeptidase E In addition to this role metallocarboxypeptidase D contributes to the processing of proteins following the action of furin an endoprotease located in the trans Golgi network The duck ortholog of metallocarboxypeptidase D was named gp180 and is a receptor for uptake of duck hepatitis B virus 6 In fruit fly Drosophila melanogaster carboxypeptidase D is known as the silver mutation with defects causing altered wing shape 7 Metallocarboxypeptidase D is generally a membrane bound protein although in some organisms a soluble form is generated by either differential RNA splicing or by proteolytic activity 8 9 In the scientific literature most of the published articles using the name Carboxypeptidase D in the title refer to metallocarboxypeptidase D and not the serine carboxypeptidase References edit Breddam K 1986 Serine carboxypeptidases A review Carlsberg Res Commun 51 2 83 128 doi 10 1007 bf02907561 Breddam K Sorensen S B Svendsen I 1987 Primary structure and enzymatic properties of carboxypeptidase II from wheat bran Carlsberg Res Commun 52 4 297 311 doi 10 1007 bf02907172 Dmochowska A Dignard D Henning D Thomas D Y Bussey H 1987 Yeast KEX1 gene encodes a putative protease with a carboxypeptidase B like function involved in killer toxin and a factor precursor processing Cell 50 4 573 584 doi 10 1016 0092 8674 87 90030 4 PMID 3301004 S2CID 22884209 Liao D I Breddam K Sweet R M Bullock T Remington S J 1992 Refined atomic model of wheat serine carboxypeptidase II at 2 2 A resolution Biochemistry 31 40 9796 9812 doi 10 1021 bi00155a037 PMID 1390755 Song L Fricker LD 1995 Purification and characterization of carboxypeptidase D a novel carboxypeptidase E like enzyme from bovine pituitary J Biol Chem 270 42 25007 13 doi 10 1074 jbc 270 42 25007 PMID 7559630 Eng FJ Novikova EG Kuroki K Ganem D Fricker LD 1998 gp180 a protein that binds duck hepatitis B virus particles has metallocarboxypeptidase D like enzymatic activity J Biol Chem 273 14 8382 8 doi 10 1074 jbc 273 14 8382 PMID 9525948 Settle SH Green MM Burtis KC 1995 The silver gene of Drosophila melanogaster encodes multiple carboxypeptidases similar to mammalian prohormone processing enzymes Proc Natl Acad Sci U S A 92 21 9470 4 Bibcode 1995PNAS 92 9470S doi 10 1073 pnas 92 21 9470 PMC 40823 PMID 7568156 Sidyelyeva G Fricker LD 2002 Characterization of Drosophila carboxypeptidase D J Biol Chem 277 51 49613 20 doi 10 1074 jbc M209652200 PMID 12393882 Song L Fricker LD 1996 Tissue distribution and characterization of soluble and membrane bound forms of metallocarboxypeptidase D J Biol Chem 271 46 28884 9 doi 10 1074 jbc 271 46 28884 PMID 8910535 External links editCarboxypeptidase D at the U S National Library of Medicine Medical Subject Headings MeSH Portal nbsp Biology Retrieved from https en wikipedia org w index php title Carboxypeptidase D amp oldid 1216238671, wikipedia, wiki, book, books, library,

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