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Mario Klimacek
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Articles

The oxyanion hole of Pseudomonas fluorescens mannitol 2-dehydrogenase: a novel structural motif for electrostatic stabilization in alcohol dehydrogenase active sites

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Mario Klimacek, Bernd Nidetzky
Journal: Biochemical Journal
Biochem J (2010) 425 (2): 455–463.
https://doi.org/10.1042/BJ20091441
Published: 23 December 2009
View articletitled, The oxyanion hole of Pseudomonas fluorescens mannitol 2-dehydrogenase: a novel structural motif for electrostatic stabilization in alcohol dehydrogenase active sites
Open the PDF for The oxyanion hole of Pseudomonas fluorescens mannitol 2-dehydrogenase: a novel structural motif for electrostatic stabilization in alcohol dehydrogenase active sites in another window
Includes: Supplementary data
Articles

The catalytic mechanism of NADH-dependent reduction of 9,10-phenanthrenequinone by Candida tenuis xylose reductase reveals plasticity in an aldo-keto reductase active site

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Simone L. Pival, Mario Klimacek, Bernd Nidetzky
Journal: Biochemical Journal
Biochem J (2009) 421 (1): 43–49.
https://doi.org/10.1042/BJ20090128
Published: 12 June 2009
View articletitled, The catalytic mechanism of NADH-dependent reduction of 9,10-phenanthrenequinone by Candida tenuis xylose reductase reveals plasticity in an aldo-keto reductase active site
Open the PDF for The catalytic mechanism of NADH-dependent reduction of 9,10-phenanthrenequinone by Candida tenuis xylose reductase reveals plasticity in an aldo-keto reductase active site in another window
Includes: Supplementary data
Articles

Catalytic mechanism of Zn 2+ -dependent polyol dehydrogenases: kinetic comparison of sheep liver sorbitol dehydrogenase with wild-type and Glu 154 →Cys forms of yeast xylitol dehydrogenase

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Mario Klimacek, Heidemarie Hellmer, Bernd Nidetzky
Journal: Biochemical Journal
Biochem J (2007) 404 (3): 421–429.
https://doi.org/10.1042/BJ20061384
Published: 29 May 2007
View articletitled, Catalytic mechanism of Zn 2+ -dependent polyol dehydrogenases: kinetic comparison of sheep liver sorbitol dehydrogenase with wild-type and Glu 154 →Cys forms of yeast xylitol dehydrogenase
Open the PDF for Catalytic mechanism of Zn 2+ -dependent polyol dehydrogenases: kinetic comparison of sheep liver sorbitol dehydrogenase with wild-type and Glu 154 →Cys forms of yeast xylitol dehydrogenase in another window
Includes: Supplementary data
Articles

On the role of Brønsted catalysis in Pseudomonas fluorescens mannitol 2-dehydrogenase

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Mario KLIMACEK, Kathryn L. KAVANAGH, David K. WILSON, Bernd NIDETZKY
Journal: Biochemical Journal
Biochem J (2003) 375 (1): 141–149.
https://doi.org/10.1042/bj20030733
Published: 01 October 2003
View articletitled, On the role of Brønsted catalysis in Pseudomonas fluorescens mannitol 2-dehydrogenase
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Articles

Structure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases

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Kathryn L. KAVANAGH, Mario KLIMACEK, Bernd NIDETZKY, David K. WILSON
Journal: Biochemical Journal
Biochem J (2003) 373 (2): 319–326.
https://doi.org/10.1042/bj20030286
Published: 15 July 2003
View articletitled, Structure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases
Open the PDF for Structure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases in another window
Articles

A catalytic consensus motif for d-mannitol 2-dehydrogenase, a member of a polyol-specific long-chain dehydrogenase family, revealed by kinetic characterization of site-directed mutants of the enzyme from Pseudomonas fluorescens

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Mario KLIMACEK, Bernd NIDETZKY
Journal: Biochemical Journal
Biochem J (2002) 367 (1): 13–18.
https://doi.org/10.1042/bj20020932
Published: 01 October 2002
View articletitled, A catalytic consensus motif for d-mannitol 2-dehydrogenase, a member of a polyol-specific long-chain dehydrogenase family, revealed by kinetic characterization of site-directed mutants of the enzyme from Pseudomonas fluorescens
Open the PDF for A catalytic consensus motif for d-mannitol 2-dehydrogenase, a member of a polyol-specific long-chain dehydrogenase family, revealed by kinetic characterization of site-directed mutants of the enzyme from Pseudomonas fluorescens in another window