Difference between revisions of "Phospholipase A2 (FXIIIa)"
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| align="center" colspan="2" bgcolor="#ffffff" | [[Image:PLA2.JPG|200px|{{PAGENAME}}]] | | align="center" colspan="2" bgcolor="#ffffff" | [[Image:PLA2.JPG|200px|{{PAGENAME}}]] | ||
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| Notes | | Notes | ||
− | | Transglutaminase probably catalyze the formation of intramolecular isopeptide bonds and this enhances the noncovalent interaction of monomers | + | | Transglutaminase probably catalyze the formation of intramolecular isopeptide bonds |
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+ | and this enhances the noncovalent interaction of monomers. | ||
The crosslinking by transglutaminase enhances it's activity. | The crosslinking by transglutaminase enhances it's activity. | ||
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[[Category:FXIIIa|*]] | [[Category:FXIIIa|*]] |
Latest revision as of 11:13, 10 March 2015
Phospholipase A2 (FXIIIa) | |
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Substrate peptide name | Phospholipase A2 |
Synonyms | PLA2 |
Determination type | In vitro |
Source | Sus scrofa, Naja naja, Apis sp. |
Subcellular localization | Cytosol
Venom |
Swissprot ID | P00592 |
Reactive glutamines | Q4 |
Reactive lysines | K10 |
Substrate sequence | ALWQFRSMIKCAIPG |
Structure | 1A3D |
Surface accessibility | ASAView pdf
ASAView txt |
Disorder prediction | IUPred |
Reference | PMID:1976627 |
Notes | Transglutaminase probably catalyze the formation of intramolecular isopeptide bonds
and this enhances the noncovalent interaction of monomers. The crosslinking by transglutaminase enhances it's activity. |
Video | 4BZwJSIDhgCWVkY35|300}} |