A Single Glycan at the 99-Loop of Human Kallikrein-related Peptidase 2 Regulates Activation and Enzymatic Activity

Human kallikrein-related peptidase 2 (KLK2) is a key serine protease in semen liquefaction and prostate cancer together with KLK3/prostate-specific antigen. In order to decipher the function of its potential N-glycosylation site, we produced pro-KLK2 in Leishmania tarentolae cells and compared it wi...

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Vydané v:	The Journal of biological chemistry Ročník 291; číslo 2; s. 593 - 604
Hlavní autori:	Guo, Shihui, Skala, Wolfgang, Magdolen, Viktor, Briza, Peter, Biniossek, Martin L, Schilling, Oliver, Kellermann, Josef, Brandstetter, Hans, Goettig, Peter
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	United States 08.01.2016
Predmet:	Amino Acid Sequence Autolysis Enzyme Activation Fibronectins - metabolism Glycosylation Humans Kinetics Models, Molecular Molecular Sequence Data Polysaccharides - metabolism Protein Structure, Secondary Proteolysis Recombinant Proteins - isolation & purification Structure-Activity Relationship Substrate Specificity Time Factors Tissue Kallikreins - chemistry Tissue Kallikreins - metabolism prostate cancer kallikrein zymogen activation substrate specificity N-linked glycosylation serine protease autolytic inactivation enzyme kinetics
ISSN:	1083-351X
On-line prístup:	Zistit podrobnosti o prístupe
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