Plasma kallikrein

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Plasma kallikrein

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

Quick Facts Identifiers, EC no. ...
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
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Quick Facts KLKB1, Available structures ...
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
Ensembl
UniProt
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]
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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

Further reading

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