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BRENDA support

Literature summary for 1.1.1.22 extracted from

  • Rajakannan, V.; Lee, H.S.; Chong, S.H.; Ryu, H.B.; Bae, J.Y.; Whang, E.Y.; Huh, J.W.; Cho, S.W.; Kang, L.W.; Choe, H.; Robinson, R.C.
    Structural basis of cooperativity in human UDP-glucose dehydrogenase (2011), PLoS ONE, 6, e25226.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
alternate crystal structure of human enzyme in complex with UDP-glucose at 2.8 A resolution. The substrate-bound protein complex consists of the open homohexamer. In all subunits of the open structure, residue Thr131 has translocated into the active site occupying the volume vacated by the absent active water and partially disordered NAD+ molecule. This conformation suggests a mechanism by which the enzyme may exchange NADH for NAD+ and repolarize the catalytic water molecule bound to Asp280 while protecting the reaction intermediates Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O60701
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