J

JA Duine

37 records found

Treatment of the yeast Rhodotorula glutinis with AICI3 leads to adaptive acquirement of heritable aluminum resistance

Inhibition of nicotinoprotein (NAD(+)-containing) alcohol dehydrogenase by trans-4-(N,N-dimethylamino)-cinnamaldehyde binding to the active site

Involvement of a quinoprotein (PQQ-containing) alcohol dehydrogenase in the degradation of polypropylene glycols by the bacterium Stenotrophomonas maltophilia

Nicotinoprotein (NAD+ -containing) alcohol dehydrogenase: structural relationships and functional interpretatiions

Crystal structure of quinohemoprotein amine dehydrogenase from pseudomonas putida, Identification of a novel quinone cofactor encaged by multiple thioether cross-bridges

Cofactor diversity in biological oxidation; Implications and applications (niet eerder opgenomen)
Journal article (2001) - JA Duine (author)

The first step in polyethylene glycol degradation by sphingomonads proceeds via a flavoprotein alcohol dehydrogenase containing flavin adenine dinucleotide.

Ca2+ stabilizes the semiquinone radical of pyrroloquinone.

The covalent structure of the small subunit from Pseudomonas putida amine dehydrogenase reveals the presence of three novel types of internal cross-linkages, all involving cysteine in a thioether bond.

Crystallization of quinohaemoprotein alcohol dehydrogenase from Comamonas testosteroni: crystals with unique optical properties.

Enzymes involved in the glycidaldehyde (2,3-epoxy-propanal) oxidation step in the kinetic resolution of racemic glycidol (2,3-epoxy-1-propanol) by Acetobacter pasteurianus.

Thiols in formaldehyde dissimilation and detoxification.
Journal article (2000) - JA Duine (author)

Ca2+-assisted, direct hydride transfer, and rate-determining tautomerization of C5-reduced PQQ to PQQH(2), in the oxidation of beta-D-glucose by soluble, quinoprotein glucose dehydrogenase.
Journal article (2000) - A Dewanti (author), JA Duine (author)

Nicotinoprotein (NADH-containing) alcohol dehydrogenase from Thodococcus etythropolis DSM 1069: an efficient catalyst for coenzyme-independent oxidation of a broad spectrum of alcohols and the interconversion of alcohols and aldehydes.
Journal article (2000) - P Schenkels (author), JA Duine (author)

Metalloenzymes with a quinone cofactor
Book chapter (1999) - JA Duine (author)

The 1.7 angstrom crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat (vol 289, pg 319, 1999)

The temperature dependence of enzyme kinetic resolutions reveals the relative importance of enthalpy and entropy to enzyme enantioselectivity

The 1.7 angstrom crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat

Structure and mechanism of soluble quinoprotein glucose dehydrogenase

Entropic and enthalpic contributions to the enantioselectivity of quinohaemoprotein alcohol dehydrogenase of Acetobacter pasteurianus and Comamonas testosteroni in the oxidation of primary and secondary alcohols