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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Bibliographic Details
Published in:	The Journal of biological chemistry Vol. 291; no. 2; pp. 593 - 604
Main Authors:	Guo, Shihui, Skala, Wolfgang, Magdolen, Viktor, Briza, Peter, Biniossek, Martin L, Schilling, Oliver, Kellermann, Josef, Brandstetter, Hans, Goettig, Peter
Format:	Journal Article
Language:	English
Published:	United States 08.01.2016
Subjects:	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
Online Access:	Get more information
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