| First Author | Clarke JL | Year | 2003 |
| Journal | Arch Biochem Biophys | Volume | 415 |
| Issue | 2 | Pages | 229-34 |
| PubMed ID | 12831846 | Mgi Jnum | J:84549 |
| Mgi Id | MGI:2668276 | Doi | 10.1016/s0003-9861(03)00229-7 |
| Citation | Clarke JL, et al. (2003) Murine hexose-6-phosphate dehydrogenase: a bifunctional enzyme with broad substrate specificity and 6-phosphogluconolactonase activity. Arch Biochem Biophys 415(2):229-34 |
| abstractText | Murine hexose-6-phosphate dehydrogenase has been purified from liver microsomes by affinity chromatography on 2('),5(')-ADP-Sepharose. The purified enzyme has 6-phosphogluconolactonase activity and glucose-6-phosphate dehydrogenase activity and has a native molecular mass of 178 kDa and a subunit molecular mass of 89 kDa. Glucose 6-phosphate, galactose 6-phosphate, 2-deoxyglucose 6-phosphate, glucosamine 6-phosphate, and glucose 6-sulfate are substrates for murine hexose-6-phosphate dehydrogenase, with either NADP or deamino-NADP as coenzyme. This study confirms that hexose-6-phosphate dehydrogenase is a bifunctional enzyme which can catalyze the first two reactions of the pentose phosphate pathway. |
