Title : Conformational alteration in serum albumin as a carrier for pyridoxal phosphate: a distinction from pyridoxal phosphate-dependent glutamate decarboxylase.

Pub. Date : 1999 Apr 15

PMID : 10190974






3 Functional Relationships(s)
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Sentence
Compound Name
Protein Name
Organism
1 Conformational alteration in serum albumin as a carrier for pyridoxal phosphate: a distinction from pyridoxal phosphate-dependent glutamate decarboxylase. Pyridoxal Phosphate glutamate-ammonia ligase Homo sapiens
2 To help in understanding BSA as a carrier for pyridoxal-P, the results were compared with those for glutamate decarboxylase (GAD), a pyridoxal-P-dependent protein, which requires pyridoxal-P as the cofactor for activity. Pyridoxal Phosphate glutamate-ammonia ligase Homo sapiens
3 Although BSA and GAD exhibit comparable molecular weights (66430 versus 65300), numbers of amino acid residues (582 versus 585), and binding affinity (>10(6) M-1), distinct conformational alterations occur between the two proteins upon interacting with pyridoxal-P: a small conformational change for BSA versus a large conformational change for GAD. Pyridoxal Phosphate glutamate-ammonia ligase Homo sapiens