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1ye6
From Proteopedia
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{{STRUCTURE_1ye6| PDB=1ye6 | SCENE= }} | {{STRUCTURE_1ye6| PDB=1ye6 | SCENE= }} | ||
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===Crystal structure of the Lys-274 to Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NADP+=== | ===Crystal structure of the Lys-274 to Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NADP+=== | ||
| + | {{ABSTRACT_PUBMED_15670843}} | ||
| - | + | ==Function== | |
| - | + | [[http://www.uniprot.org/uniprot/XYL1_CANTE XYL1_CANTE]] Reduces D-xylose into xylitol. Has a preference for NADPH, but can also utilize NADH as cosubstrate. | |
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==About this Structure== | ==About this Structure== | ||
| - | [[1ye6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[1ye6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10573 Atcc 10573]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YE6 OCA]. |
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:015670843</ref><references group="xtra"/> | + | <ref group="xtra">PMID:015670843</ref><references group="xtra"/><references/> |
| - | [[Category: | + | [[Category: Atcc 10573]] |
[[Category: Leitgeb, S.]] | [[Category: Leitgeb, S.]] | ||
[[Category: Nidetzky, B.]] | [[Category: Nidetzky, B.]] | ||
Revision as of 08:40, 23 April 2014
Contents |
Crystal structure of the Lys-274 to Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NADP+
Template:ABSTRACT PUBMED 15670843
Function
[XYL1_CANTE] Reduces D-xylose into xylitol. Has a preference for NADPH, but can also utilize NADH as cosubstrate.
About this Structure
1ye6 is a 4 chain structure with sequence from Atcc 10573. Full crystallographic information is available from OCA.
Reference
- Leitgeb S, Petschacher B, Wilson DK, Nidetzky B. Fine tuning of coenzyme specificity in family 2 aldo-keto reductases revealed by crystal structures of the Lys-274-->Arg mutant of Candida tenuis xylose reductase (AKR2B5) bound to NAD+ and NADP+. FEBS Lett. 2005 Jan 31;579(3):763-7. PMID:15670843 doi:10.1016/j.febslet.2004.12.063
