The tetrapyrrole-biosynthesis enzyme porphobilinogen deaminase has in two of its domains the same alpha/beta polypeptide-chain fold as the transferrins and the periplasmic binding proteins. These proteins have in common an active-site cleft located at the interface between two domains. The binding proteins and porphobilinogen deaminase are likely related by divergent evolution. The interdomain motions observed in the binding proteins are suggested also to have an important role in the mechanism of the reaction catalyzed by porphobilinogen deaminase.
机构:
MONTANA STATE UNIV, JOHNSON HALL LIFE SCI, DEPT PLANT PATHOL, BOZEMAN, MT 59717 USAMONTANA STATE UNIV, JOHNSON HALL LIFE SCI, DEPT PLANT PATHOL, BOZEMAN, MT 59717 USA
BELTRAN, JP
STROBEL, GA
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机构:
MONTANA STATE UNIV, JOHNSON HALL LIFE SCI, DEPT PLANT PATHOL, BOZEMAN, MT 59717 USAMONTANA STATE UNIV, JOHNSON HALL LIFE SCI, DEPT PLANT PATHOL, BOZEMAN, MT 59717 USA