(Q43668041)

English

Exploring the active site of yeast xylose reductase by site-directed mutagenesis of sequence motifs characteristic of two dehydrogenase/reductase family types

scientific article published in July 2001

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

Exploring the active site of yeast xylose reductase by site-directed mutagenesis of sequence motifs characteristic of two dehydrogenase/reductase family types (English)

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

author name string

Klimacek M

1

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

Szekely M

2

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

Griessler R

3

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

Nidetzky B

4

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Europe PubMed Central

PubMed publication ID

25 November 2017

language of work or name

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publication date

1 July 2001

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Europe PubMed Central

PubMed publication ID

25 November 2017

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

500

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Europe PubMed Central

PubMed publication ID

25 November 2017

3

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

149-152

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

describes a project that uses

site-directed mutagenesis

1 reference

based on heuristic

inferred from title

A new nomenclature for the aldo-keto reductase superfamily.

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

Structural and functional properties of aldose xylose reductase from the D-xylose-metabolizing yeast Candida tenuis

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

The structure and function of yeast xylose (aldose) reductases.

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

Comparative anatomy of the aldo-keto reductase superfamily

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

Structural comparisons lead to the definition of a new superfamily of NAD(P)(H)-accepting oxidoreductases: the single-domain reductases/epimerases/dehydrogenases (the 'RED' family).

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

Three-dimensional structure of holo 3 alpha,20 beta-hydroxysteroid dehydrogenase: a member of a short-chain dehydrogenase family

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

Tyrosine-48 is the proton donor and histidine-110 directs substrate stereochemical selectivity in the reduction reaction of human aldose reductase: enzyme kinetics and crystal structure of the Y48H mutant enzyme

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

Mutagenesis of 3 alpha-hydroxysteroid dehydrogenase reveals a "push-pull" mechanism for proton transfer in aldo-keto reductases

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

Short-chain dehydrogenases/reductases (SDR)

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

Active site directed mutagenesis of 3 beta/17 beta-hydroxysteroid dehydrogenase establishes differential effects on short-chain dehydrogenase/reductase reactions

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

Mechanistic roles of tyrosine 149 and serine 124 in UDP-galactose 4-epimerase from Escherichia coli

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

Xylose utilisation: cloning and characterisation of the Xylose reductase from Candida tenuis

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

A simple method for site-directed mutagenesis using the polymerase chain reaction

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

NAD(P)H-dependent aldose reductase from the xylose-assimilating yeast Candida tenuis. Isolation, characterization and biochemical properties of the enzyme

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

The aldo-keto reductase (AKR) superfamily: an update

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

Steroid recognition and regulation of hormone action: crystal structure of testosterone and NADP+ bound to 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

The enhancement of enzymatic rate accelerations by Brønsted acid-base catalysis

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

D-Xylose metabolism by Candida intermedia: isolation and characterisation of two forms of aldose reductase with different coenzyme specificities

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

Retention of NADPH-linked quinone reductase activity in an aldo-keto reductase following mutation of the catalytic tyrosine

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2801%2902609-6

21 January 2018

Identifiers

10.1016/S0014-5793(01)02609-6

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

ResearchGate publication ID

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