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PMID:14550557

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Citation

Bahn, SC, Lee, HY, Kim, HJ, Ryu, SB and Shin, JS (2003) Characterization of Arabidopsis secretory phospholipase A2-gamma cDNA and its enzymatic properties. FEBS Lett. 553:113-8

Abstract

Plant secretory phospholipases A(2) (sPLA(2)s) probably play important roles in phospholipid signaling based on the data reported from other organisms, but their functions are poorly understood because of the lack of cloned sPLA(2) genes. In this study, we cloned and characterized an Arabidopsis secretory phospholipase A(2)-gamma (AtsPLA(2)-gamma) cDNA, and examined its enzymatic properties. The recombinant protein of AtsPLA(2)-gamma showed maximal enzyme activity at pH 8.0, and required Ca(2+) for activity. Moreover, AtsPLA(2)-gamma showed sn-2 position specificity but no prominent acyl preference, though it showed head group specificity to phosphatidylethanolamine rather than to phosphatidylcholine. AtsPLA(2)-gamma was found to predominate in the mature flower rather than in other tissues, and subcellular localization analysis confirmed that AtsPLA(2)-gamma is secreted into the intercellular space.

Links

PubMed

Keywords

Amino Acid Sequence; Arabidopsis/enzymology; Arabidopsis/genetics; Calcium/metabolism; Cloning, Molecular; Flowers/enzymology; Gene Expression Profiling; Group IV Phospholipases A2; Hydrogen-Ion Concentration; Molecular Sequence Data; Onions/cytology; Onions/enzymology; Phospholipases A/chemistry; Phospholipases A/genetics; Phospholipases A/metabolism; Phospholipases A2; Protein Transport; RNA, Messenger/genetics; RNA, Messenger/metabolism; Sequence Homology, Amino Acid; Substrate Specificity

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ARATH:PLA2C

enables

GO:0004623: phospholipase A2 activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete


See also

References

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