2008
DOI: 10.1007/s00018-008-7565-9
|View full text |Cite
|
Sign up to set email alerts
|

Serine peptidases: Classification, structure and function

Abstract: Serine peptidases play key roles in human health and disease and their biochemical properties shaped the molecular evolution of these processes. Of known proteolytic enzymes, the serine peptidase family is the major cornerstone of the vertebrate degradome. We describe the known diversity of serine peptidases with respect to structure and function. Particular emphasis is placed on the S1 peptidase family, the trypsins, which underwent the most predominant genetic expansion yielding the enzymes responsible for v… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

5
340
1
4

Year Published

2008
2008
2015
2015

Publication Types

Select...
5
4

Relationship

0
9

Authors

Journals

citations
Cited by 377 publications
(350 citation statements)
references
References 147 publications
5
340
1
4
Order By: Relevance
“…Monovalent cation coordination plays an influential role in many enzyme-catalysed reactions (Di Cera, 2006;Page & Di Cera, 2006). Due to limited electrostatic properties, Na + and K + are optimal reagents for stabilization of the active conformational state of an enzyme or for facilitating electrostatic interactions between enzyme and substrate (Page & Di Cera, 2008).…”
Section: Effect Of Peptidase Inhibitors and Reducing Agentsmentioning
confidence: 99%
“…Monovalent cation coordination plays an influential role in many enzyme-catalysed reactions (Di Cera, 2006;Page & Di Cera, 2006). Due to limited electrostatic properties, Na + and K + are optimal reagents for stabilization of the active conformational state of an enzyme or for facilitating electrostatic interactions between enzyme and substrate (Page & Di Cera, 2008).…”
Section: Effect Of Peptidase Inhibitors and Reducing Agentsmentioning
confidence: 99%
“…Proteases are common throughout tissues where they cleave polypeptides into fragments at specified sites (Page and Di Cera 2008) and represent the basis of natural protein degradation pathways (Goldberg 2003). Crystallins undergo a number of C-and N-terminal truncations which can have a major effect on their stability and solubility (Hains and Truscott 2007;Morris et al 2008;Treweek et al 2010).…”
Section: Truncationmentioning
confidence: 99%
“…The active configuration is produced via the combination of enzyme and cofactor, which usually includes an active site that the substrate can interact with [31]. Many enzymes are selective for just one substrate, and their activity is inhibited if the active site is blocked or the shape of the substrate is changed [32,33]. The change in structure of SIRT6 V2 due to the deleted 124-bp sequence ( Figure 5) might thus alter the interactions between substrate and enzyme, which are involved in the series of reactions associated with cell proliferation.…”
Section: Prediction Of Sirt6 V1 and V2 Protein Structuresmentioning
confidence: 99%