Literature summary for 1.1.1.30 extracted from

Machado, T.F.G.; Purg, M.; McMahon, S.A.; Read, B.J.; Oehler, V.; Aqvist, J.; Gloster, T.M.; da Silva, R.G.
Dissecting the mechanism of (R)-3-hydroxybutyrate dehydrogenase by kinetic isotope effects, protein crystallography, and computational chemistry (2020), ACS Catal., 10, 15019-15032 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of enzyme complexed to NAD+:acetoacetate and NAD+:3-oxovalerate	Psychrobacter arcticus
structures of enzyme complexed to NAD+:acetoacetate and NAD+:3-oxovalerate	Acinetobacter baumannii

Organism

Organism	UniProt	Comment	Textmining
Acinetobacter baumannii	A0A1E3M3N6	-	-
Psychrobacter arcticus	Q4FRT2	-	-
Psychrobacter arcticus DSM 17307	Q4FRT2	-	-

Synonyms

Synonyms	Comment	Organism
BdhA	-	Acinetobacter baumannii
HBDH	-	Psychrobacter arcticus
Psyc_1428	-	Psychrobacter arcticus

General Information

General Information	Comment	Organism
metabolism	steady-state ordered kinetic mechanism for acetoacetate reduction, where hydride transfer is not rate limiting. Hydride transfer becomes more rate limiting with non-native substrate 3-oxovalerate. Hydride and proton transfers occur in the same transition state. Transition states show concerted, albeit not synchronous, proton and hydride transfers to 3-oxovalerate	Psychrobacter arcticus
metabolism	steady-state ordered kinetic mechanism for acetoacetate reduction, where hydride transfer is not rate limiting. Hydride transfer becomes more rate limiting with non-native substrate 3-oxovalerate. Hydride and proton transfers occur in the same transition state. Transition states showconcerted, albeit not synchronous, proton and hydride transfers to 3-oxovalerate	Acinetobacter baumannii

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Release 2023.1 (January 2023)