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PMID:15313216
Citation |
Shearer, HL, Turpin, DH and Dennis, DT (2004) Characterization of NADP-dependent malic enzyme from developing castor oil seed endosperm. Arch. Biochem. Biophys. 429:134-44 |
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Abstract |
Metabolic pathways sequestered within the leucoplast of developing oilseeds ensure a balanced supply of substrates and cofactors for fatty acid biosynthesis. NADP-dependent malic enzyme (NADP-ME) may be important in supplying both carbon and NADPH for fatty acid biosynthesis in the developing endosperm of the oilseed Ricinus communis. NADP-ME was purified 5160-fold to a specific activity of 18.2 U/mg protein. NADP-ME is a homotetramer with a native mass of 254 kDa and a subunit size of approximately 63 kDa. Effectors of castor NADP-ME are typical of the NADP-malic enzymes, with the exception of acetyl-CoA and its derivatives, which were found to act as activators. This is consistent with a regulatory role for these molecules during fatty acid biosynthesis in vivo. NADP-ME was found to have maximal activity at stage 7 of endosperm development, coincident with maximal lipid accumulation. |
Links |
PubMed Online version:10.1016/j.abb.2004.07.001 |
Keywords |
Blotting, Western; Castor Oil; Electrophoresis, Polyacrylamide Gel; Hydrogen-Ion Concentration; Isoenzymes/metabolism; Kinetics; Malate Dehydrogenase/metabolism; Molecular Weight; NADP/metabolism; Seeds/enzymology; Seeds/growth & development; Temperature |
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Significance
Annotations
Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
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GO:0004473: malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) activity |
ECO:0000314: |
F |
Protein was purified and assayed in vitro |
complete | ||||
See also
References
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