TY - JOUR
T1 - The enantioselectivity of quinohaemoprotein alcohol dehydrogenases
T2 - Mechanistic and structural aspects
AU - Jongejan, Aldo
AU - Machado, Sonia S.
AU - Jongejan, Jaap A.
N1 - Funding Information: We gratefully acknowledge financial support from the Organization for the Advancement of Pure Research/NWO, Foundation for Chemical Research/SON, The Netherlands (A.J.), and the Conselho Nacional de Desenvolvimento Cientifico é Tecnologico/CNPq, Brasil (S.S.M.).
PY - 2000/1/12
Y1 - 2000/1/12
N2 - Quinohaemoprotein alcohol dehydrogenases, QH-ADHs, isolated from Acetobacter, Gluconobacter and Comamonas species show appreciable enantioselectivity in the oxidation of chiral primary and secondary alcohols. Current views of the structural and mechanistic factors of importance for the understanding of the enantioselective performance of these enzymes are reviewed. Structural properties of QH-ADH, Type I, from C. testosteroni, and QH-ADH, Type II, from A. pasteurianus have been deduced from homology modeling studies based on the X-ray crystallographic data available for PQQ-containing quinoprotein methanol dehydrogenases, MDHs. Mechanisms that have been proposed for quino(haemo)protein alcohol dehydrogenase-catalyzed substrate oxidation are discussed in relation to the constraints set by the observed enantioselectivity. Copyright (C) 2000 Elsevier Science B.V.
AB - Quinohaemoprotein alcohol dehydrogenases, QH-ADHs, isolated from Acetobacter, Gluconobacter and Comamonas species show appreciable enantioselectivity in the oxidation of chiral primary and secondary alcohols. Current views of the structural and mechanistic factors of importance for the understanding of the enantioselective performance of these enzymes are reviewed. Structural properties of QH-ADH, Type I, from C. testosteroni, and QH-ADH, Type II, from A. pasteurianus have been deduced from homology modeling studies based on the X-ray crystallographic data available for PQQ-containing quinoprotein methanol dehydrogenases, MDHs. Mechanisms that have been proposed for quino(haemo)protein alcohol dehydrogenase-catalyzed substrate oxidation are discussed in relation to the constraints set by the observed enantioselectivity. Copyright (C) 2000 Elsevier Science B.V.
KW - Alcohol dehydrogenase
KW - Chiral alcohols
KW - Enantioselective oxidation
KW - Kinetics
KW - Mechanism
KW - Molecular modeling
KW - Pyrroloquinoline quinone
KW - Quinohaemoprotein
KW - Review
KW - Structure
UR - http://www.scopus.com/inward/record.url?scp=0033962911&partnerID=8YFLogxK
U2 - https://doi.org/10.1016/S1381-1177(99)00063-6
DO - https://doi.org/10.1016/S1381-1177(99)00063-6
M3 - Article
SN - 1381-1177
VL - 8
SP - 121
EP - 163
JO - Journal of Molecular Catalysis - B Enzymatic
JF - Journal of Molecular Catalysis - B Enzymatic
IS - 1-3
ER -