Title : Role of the S128, H186, and N187 triad in substrate binding and decarboxylation in the sheep liver 6-phosphogluconate dehydrogenase reaction.

Pub. Date : 2006 Oct 24

PMID : 17042485






4 Functional Relationships(s)
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1 Crystal structures of 6-phosphogluconate dehydrogenase (6PGDH) from sheep liver indicate that S128 and N187 are within hydrogen-bonding distance of 6PG in the E:6PG binary complex and NADPH in the E:NADPH binary complex. NADP 6-phosphogluconate dehydrogenase, decarboxylating Ovis aries
2 Crystal structures of 6-phosphogluconate dehydrogenase (6PGDH) from sheep liver indicate that S128 and N187 are within hydrogen-bonding distance of 6PG in the E:6PG binary complex and NADPH in the E:NADPH binary complex. NADP 6-phosphogluconate dehydrogenase, decarboxylating Ovis aries
3 Crystal structures of 6-phosphogluconate dehydrogenase (6PGDH) from sheep liver indicate that S128 and N187 are within hydrogen-bonding distance of 6PG in the E:6PG binary complex and NADPH in the E:NADPH binary complex. NADP 6-phosphogluconate dehydrogenase, decarboxylating Ovis aries
4 Crystal structures of 6-phosphogluconate dehydrogenase (6PGDH) from sheep liver indicate that S128 and N187 are within hydrogen-bonding distance of 6PG in the E:6PG binary complex and NADPH in the E:NADPH binary complex. NADP 6-phosphogluconate dehydrogenase, decarboxylating Ovis aries