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Plasma kallikrein

Plasma kallikrein
Identifiers
EC no.3.4.21.34
CAS no.410538-33-9
Alt. namesserum kallikrein, kininogenin, kallikrein I, kallikrein II, kininogenase, kallikrein, callicrein, glumorin, padreatin, padutin, kallidinogenase, bradykininogenase, panceatic kallikrein, onokrein P, dilminal D, depot-Padutin, urokallikrein, urinary kallikrein
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins
KLKB1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesKLKB1, KLK3, PPK, PKKD, PKK, kallikrein B1
External IDsOMIM: 229000; MGI: 102849; HomoloGene: 68097; GeneCards: KLKB1; OMA:KLKB1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

3818

16621

Ensembl

ENSG00000164344

ENSMUSG00000109764

UniProt

P03952

P26262

RefSeq (mRNA)

NM_000892
NM_001318394
NM_001318396

NM_008455

RefSeq (protein)

NP_000883
NP_001305323
NP_001305325

NP_032481

Location (UCSC)Chr 4: 186.21 – 186.26 MbChr 8: 45.72 – 45.75 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Plasma kallikrein (EC 3.4.21.34) is an enzyme[5][6][7][8][9] that catalyses the following chemical reaction:

Selective cleavage of some Arg- and Lys- bonds, including Lys-Arg and Arg-Ser in (human) kininogen to release bradykinin

Plasma kallikrein and its precursor are encoded by the KLKB1 gene.[10][11]

This enzyme is formed from prekallikrein (Fletcher factor) by factor XIIa.

Function

Plasma prekallikrein is a glycoprotein that participates in the surface-dependent activation of blood coagulation, fibrinolysis, kinin generation and inflammation. It is synthesized in the liver and secreted into the blood as a single polypeptide chain. Plasma prekallikrein is converted to plasma kallikrein by factor XIIa by the cleavage of an internal Arg-Ile bond. Plasma kallikrein therefore is composed of a heavy chain and a light chain held together by a disulfide bond. The heavy chain originates from the amino-terminal end of the zymogen and contains 4 tandem repeats of 90 or 91 amino acids. Each repeat harbors a novel structure called the apple domain. The heavy chain is required for the surface-dependent pro-coagulant activity of plasma kallikrein. The light chain contains the active site or catalytic domain of the enzyme and is homologous to the trypsin family of serine proteases. Plasma prekallikrein deficiency causes a prolonged activated partial thromboplastin time in patients.[12]

Interactions

Kallikrein and prekallikrein have been shown to interact with High-molecular-weight kininogen.[13][14][15][16]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000164344 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000109764 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Heimark RL, Davie EW (1981). "[14] Bovine and human plasma prekallikrein". Bovine and human plasma prekallikrein. Methods in Enzymology. Vol. 80 Pt C. pp. 157–72. doi:10.1016/s0076-6879(81)80016-x. ISBN 978-0-12-181980-4. PMID 6918767.
  6. ^ McRae BJ, Kurachi K, Heimark RL, Fujikawa K, Davie EW, Powers JC (December 1981). "Mapping the active sites of bovine thrombin, factor IXa, factor Xa, factor XIa, factor XIIa, plasma kallikrein, and trypsin with amino acid and peptide thioesters: development of new sensitive substrates". Biochemistry. 20 (25): 7196–206. doi:10.1021/bi00528a022. PMID 6976185.
  7. ^ Silverberg M, Kaplan AP (1988). "[8] Prekallikrein". Prekallikrein. Methods in Enzymology. Vol. 163. pp. 85–95. doi:10.1016/0076-6879(88)63010-2. ISBN 978-0-12-182064-0. PMID 3237096.
  8. ^ Seidah NG, Ladenheim R, Mbikay M, Hamelin J, Lutfalla G, Rougeon F, Lazure C, Chrétien M (October 1989). "The cDNA structure of rat plasma kallikrein". DNA. 8 (8): 563–74. doi:10.1089/dna.1989.8.563. PMID 2598771.
  9. ^ Tsuda Y, Teno N, Okada Y, Wanaka K, Bohgaki M, Hijikata-Okunomiya A, Okamoto U, Naito T, Okamoto S (November 1989). "Synthesis of tripeptide chloromethyl ketones and examination of their inhibitory effects on plasmin and plasma kallikrein". Chemical & Pharmaceutical Bulletin. 37 (11): 3108–11. doi:10.1248/cpb.37.3108. PMID 2534361.
  10. ^ Yu H, Bowden DW, Spray BJ, Rich SS, Freedman BI (April 1998). "Identification of human plasma kallikrein gene polymorphisms and evaluation of their role in end-stage renal disease". Hypertension. 31 (4): 906–11. doi:10.1161/01.hyp.31.4.906. PMID 9535413.
  11. ^ Chung DW, Fujikawa K, McMullen BA, Davie EW (August 1986). "Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats". Biochemistry. 25 (9): 2410–7. doi:10.1021/bi00357a017. PMID 3521732.
  12. ^ "Entrez Gene: KLKB1 kallikrein B, plasma (Fletcher factor) 1".
  13. ^ Thompson RE, Mandle R, Kaplan AP (October 1979). "Studies of binding of prekallikrein and Factor XI to high molecular weight kininogen and its light chain". Proc. Natl. Acad. Sci. U.S.A. 76 (10): 4862–6. Bibcode:1979PNAS...76.4862T. doi:10.1073/pnas.76.10.4862. PMC 413037. PMID 291905.
  14. ^ Page JD, You JL, Harris RB, Colman RW (October 1994). "Localization of the binding site on plasma kallikrein for high-molecular-weight kininogen to both apple 1 and apple 4 domains of the heavy chain". Arch. Biochem. Biophys. 314 (1): 159–64. doi:10.1006/abbi.1994.1424. PMID 7944388.
  15. ^ Herwald H, Jahnen-Dechent W, Alla SA, Hock J, Bouma BN, Müller-Esterl W (July 1993). "Mapping of the high molecular weight kininogen binding site of prekallikrein. Evidence for a discontinuous epitope formed by distinct segments of the prekallikrein heavy chain". J. Biol. Chem. 268 (19): 14527–35. doi:10.1016/S0021-9258(19)85270-5. PMID 7686159.
  16. ^ Renné T, Dedio J, Meijers JC, Chung D, Müller-Esterl W (September 1999). "Mapping of the discontinuous H-kininogen binding site of plasma prekallikrein. Evidence for a critical role of apple domain-2". J. Biol. Chem. 274 (36): 25777–84. doi:10.1074/jbc.274.36.25777. PMID 10464316.

Further reading

Quelle: https://en.wikipedia.org/wiki/Plasma_kallikrein