2007
DOI: 10.1007/s10142-007-0059-2
|View full text |Cite
|
Sign up to set email alerts
|

Serpins in plants and green algae

Abstract: Control of proteolysis is important for plant growth, development, responses to stress, and defence against insects and pathogens. Members of the serpin protein family are likely to play a critical role in this control through irreversible inhibition of endogenous and exogenous target proteinases. Serpins have been found in diverse species of the plant kingdom and represent a distinct clade among serpins in multicellular organisms. Serpins are also found in green algae, but the evolutionary relationship betwee… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

11
134
0
2

Year Published

2009
2009
2012
2012

Publication Types

Select...
4
1

Relationship

0
5

Authors

Journals

citations
Cited by 113 publications
(147 citation statements)
references
References 179 publications
11
134
0
2
Order By: Relevance
“…Serpins were not originally classified as PRs. For their probable defensive role, hypothesized on the basis of irreversible inhibition of exogenous proteinases that break down seed storage proteins 72,132,133 , cereal serpins have been considered as PRs 111 . Protein Z accounts for 2% of the total protein content of malt and up to 25% of the non-dialyzable beer protein estimated by the enzyme-linked immunosorbant assay (ELISA) 36,37 .…”
Section: Serpin (Protein Z)mentioning
confidence: 99%
“…Serpins were not originally classified as PRs. For their probable defensive role, hypothesized on the basis of irreversible inhibition of exogenous proteinases that break down seed storage proteins 72,132,133 , cereal serpins have been considered as PRs 111 . Protein Z accounts for 2% of the total protein content of malt and up to 25% of the non-dialyzable beer protein estimated by the enzyme-linked immunosorbant assay (ELISA) 36,37 .…”
Section: Serpin (Protein Z)mentioning
confidence: 99%
“…PIs can be divided into two classes, based on the protease inhibition mechanism: inhibitors employing standard mechanisms (Mm up to 22 kDa) and the serpins (serine proteinase inhibitors) (Mm ∼ 40 kDa) employing a so-called suicidal mechanism 281,282 . Standard inhibitors form a complex in which the reactive peptide bond is slowly hydrolyzed and the enzyme is liberated, but the rate of complex formation is much lower.…”
Section: Protease Inhibitors (Pis) (Pr-6)mentioning
confidence: 99%
“…The majority of serpins are metastable proteins, able to inhibit serine proteinases of the chymotrypsin family by employing a unique "suicide substrate" mechanism of inhibition, different from standard mechanisms such as those of the Bowman-Birk or Kunitz families 281 . Cleavage of the reactive bond, in the reactive center of the protein during inhibition, is followed by a drastic conformational change and the subsequent formation of an enzyme-inhibitor complex (Fig.…”
Section: Chymotrypsin/subtilisin Inhibitors (Ci-1 and Ci-2)mentioning
confidence: 99%
See 2 more Smart Citations