Sequence of XYL1_CANTE
EC Number:1.1.1.307
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
xylitol + NAD(P)+ = D-xylose + NAD(P)H + H+
Other sequences found for EC No. 1.1.1.307
General information:
Sequence
0 MSASIPDIKL SSGHLMPSIG FGCWKLANAT AGEQVYQAIK AGYRLFDGAE DYGNEKEVGD
60 GVKRAIDEGL VKREEIFLTS KLWNNYHDPK NVETALNKTL ADLKVDYVDL FLIHFPIAFK
120 FVPIEEKYPP GFYCGDGNNF VYEDVPILET WKALEKLVAA GKIKSIGVSN FPGALLLDLL
180 RGATIKPAVL QVEHHPYLQQ PKLIEFAQKA GVTITAYSSF GPQSFVEMNQ GRALNTPTLF
240 AHDTIKAIAA KYNKTPAEVL LRWAAQRGIA VIPKSNLPER LVQNRSFNTF DLTKEDFEEI
300 AKLDIGLRFN DPWDWDNIPI FV
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
118868
Hacker B.,Habenicht A.,Kiess M.,Mattes R.
Xylose utilisation: cloning and characterisation of the xylose reductase from Candida tenuis.
Biol. Chem.
380
1395-1403
1999
118869
Kavanagh K.L.,Klimacek M.,Nidetzky B.,Wilson D.K.
The structure of apo and holo forms of xylose reductase, a dimeric aldo-keto reductase from Candida tenuis.
Biochemistry
41
8785-8795
2002
118870
Kavanagh K.L.,Klimacek M.,Nidetzky B.,Wilson D.K.
Structure of xylose reductase bound to NAD+ and the basis for single and dual co-substrate specificity in family 2 aldo-keto reductases.
Biochem. J.
373
319-326
2003
118871
Petschacher B.,Leitgeb S.,Kavanagh K.L.,Wilson D.K.,Nidetzky B.
The coenzyme specificity of Candida tenuis xylose reductase (AKR2B5) explored by site-directed mutagenesis and X-ray crystallography.
Biochem. J.
385
75-83
2005
118872
Leitgeb S.,Petschacher B.,Wilson D.K.,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.
579
763-767
2005
118873
Kratzer R.,Leitgeb S.,Wilson D.K.,Nidetzky B.
Probing the substrate binding site of Candida tenuis xylose reductase (AKR2B5) with site-directed mutagenesis.
Biochem. J.
393
51-58
2006
