| Literature DB >> 175789 |
Abstract
The binding of NAD+ to glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) from Bacillus stearothermophilus has been studied by measurement of protein fluorescence quenching. Slight negative co-operativity was observed in the binding of the third and fourth coenzyme molecules to the tetrameric enzyme. The first two coenzyme molecules were tightly bound. In this respect the enzyme resembles that from sturgeon muscle rather than that from yeast.Entities:
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Year: 1975 PMID: 175789 PMCID: PMC1172424 DOI: 10.1042/bj1510747
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857