Yeast supported gold nanoparticles: An efficient catalyst for the synthesis of commercially important aryl amines

Candida parapsilosis ATCC 7330 supported gold nanoparticles (CpGNP), prepared by a simple and green method can selectively reduce nitroarenes and substituted nitroarenes with different functional groups like halides (-F, -Cl,...

New insights into the stereospecific reduction by an (S) specific carbonyl reductase from Candida parapsilosis ATCC 7330: experimental and QM/MM studies

The quantum mechanics/molecular mechanics study of an (S) specific carbonyl reductase from C. parapsilosis ATCC 7330 showing a dual kinetic response for the reduction of ketones and α-ketoesters suggests different reaction mechanisms for the same.

Understanding (R) Specific Carbonyl Reductase from Candida parapsilosis ATCC 7330 [CpCR]: Substrate Scope, Kinetic Studies and the Role of Zinc

CpCR, an (R) specific carbonyl reductase, so named because it gave (R)-alcohols on asymmetric reduction of ketones and ketoesters, is a recombinantly expressed enzyme from Candida parapsilosis ATCC 7330. It turns out to be a better aldehyde reductase and catalyses cofactor (NADPH) specific reduction of aliphatic and aromatic aldehydes. Kinetics studies against benzaldehyde and 2,4-dichlorobenzaldehyde show that the enzyme affinity and rate of reaction change significantly upon substitution on the benzene ring of benzaldehyde. CpCR, an MDR (medium chain reductase/dehydrogenase) containing both structural and catalytic Zn atoms, exists as a dimer, unlike the (S) specific reductase (SRED) from the same yeast which can exist in both dimeric and tetrameric forms. Divalent metal salts inhibit the enzyme even at nanomolar concentrations. EDTA chelation decreases CpCR activity. However, chelation done after the enzyme is pre-incubated with the NADPH retains most of the activity implying that Zn removal is largely prevented by the formation of the enzyme-cofactor complex.

A carbonyl reductase from Candida parapsilosis ATCC 7330: substrate selectivity and enantiospecificity

A purified carbonyl reductase (SRED) asymmetrically reduces ketones and α-ketoesters to (S)-alcohols with a potential application in the synthesis of industrially important chiral molecules.