Title : Modification of an essential amino group of phosphoenolpyruvate carboxylase from maize leaves by pyridoxal phosphate and by pyridoxal phosphate-sensitized photooxidation.

Pub. Date : 1986 May 1

PMID : 3085590






4 Functional Relationships(s)
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Protein Name
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1 Modification of an essential amino group of phosphoenolpyruvate carboxylase from maize leaves by pyridoxal phosphate and by pyridoxal phosphate-sensitized photooxidation. Pyridoxal Phosphate MLO-like protein 4 Zea mays
2 Modification of an essential amino group of phosphoenolpyruvate carboxylase from maize leaves by pyridoxal phosphate and by pyridoxal phosphate-sensitized photooxidation. Pyridoxal Phosphate MLO-like protein 4 Zea mays
3 Phosphoenolpyruvate carboxylase from maize leaves was inactivated by pyridoxal 5"-phosphate in the dark and in the light. Pyridoxal Phosphate MLO-like protein 4 Zea mays
4 Spectral analysis of pyridoxal 5"-phosphate-modified phosphoenolpyruvate carboxylase showed absorption maxima at 432 and 327 nm, before and after reduction with NaBH4, respectively, suggesting that epsilon-amino groups of lysine residues are the reactive groups in the enzyme. Pyridoxal Phosphate MLO-like protein 4 Zea mays