Understanding substrate specificity and enantioselectivity of carbonyl reductase from Candida parapsilosis ATCC 7330 (CpCR): Experimental and modeling studies

2018 ◽  
Vol 460 ◽  
pp. 40-45 ◽  
Author(s):  
Nidhi Aggarwal ◽  
Ragamanvitha Ananthathamula ◽  
Vinay Kumar Karanam ◽  
Mukesh Doble ◽  
Anju Chadha
Keyword(s):  
Substrate Specificity ◽  
Candida Parapsilosis ◽  
Carbonyl Reductase ◽  
Modeling Studies ◽  
Candida Parapsilosis Atcc 7330

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

2020 ◽  
Vol 10 (17) ◽  
pp. 5925-5934 ◽  
Author(s):  
Sneha Sudhakara ◽  
Chandrasekaran Ramakrishnan ◽  
M. Michael Gromiha ◽  
Anju Chadha
Keyword(s):  
Quantum Mechanics ◽  
Molecular Mechanics ◽  
Reaction Mechanisms ◽  
Candida Parapsilosis ◽  
Carbonyl Reductase ◽  
Stereospecific Reduction ◽  
Candida Parapsilosis Atcc 7330 ◽  
Reduction Of Ketones

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.

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

2017 ◽  
Vol 15 (19) ◽  
pp. 4165-4171 ◽  
Author(s):  
Sneha Sudhakara ◽  
Anju Chadha
Keyword(s):  
Potential Application ◽  
Candida Parapsilosis ◽  
Carbonyl Reductase ◽  
Substrate Selectivity ◽  
Chiral Molecules ◽  
Candida Parapsilosis Atcc 7330

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.

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

Catalysts ◽  
2019 ◽  
Vol 9 (9) ◽  
pp. 702 ◽  
Author(s):  
Karanam ◽  
Chaudhury ◽  
Chadha
Keyword(s):  
Candida Parapsilosis ◽  
Asymmetric Reduction ◽  
Kinetic Studies ◽  
Aromatic Aldehydes ◽  
Carbonyl Reductase ◽  
Rate Of Reaction ◽  
Reaction Change ◽  
Candida Parapsilosis Atcc 7330 ◽  
Reduction Of Ketones

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.

Who's Who? Allocation of Carbonyl Reductase Isoenzymes from Candida parapsilosis by Combining Bio- and Computational Chemistry

ChemBioChem ◽  
2012 ◽  
Vol 13 (6) ◽  
pp. 803-809 ◽  
Author(s):  
Andre Jakoblinnert ◽  
Marco Bocola ◽  
Monideepa Bhattacharjee ◽  
Sonja Steinsiek ◽  
Mara Bönitz-Dulat ◽  
...  
Keyword(s):  
Computational Chemistry ◽  
Candida Parapsilosis ◽  
Carbonyl Reductase
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