KEGG   ENZYME: 1.1.1.307
Entry
EC 1.1.1.307                Enzyme                                 
Name
D-xylose reductase [NAD(P)H];
XylR;
msXR;
dsXR;
dual specific xylose reductase;
NAD(P)H-dependent xylose reductase;
xylose reductase (ambiguous);
D-xylose reductase (ambiguous)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
Sysname
xylitol:NAD(P)+ oxidoreductase
Reaction(IUBMB)
xylitol + NAD(P)+ = D-xylose + NAD(P)H + H+ [RN:R01431 R09477]
Reaction(KEGG)
R01431 R09477
Substrate
xylitol [CPD:C00379];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006]
Product
D-xylose [CPD:C00181];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
Xylose reductases catalyse the reduction of xylose to xylitol, the initial reaction in the fungal D-xylose degradation pathway. Most of the enzymes exhibit a strict requirement for NADPH [cf. EC 1.1.1.431, D-xylose reductase (NADPH)]. However, a few D-xylose reductases, such as those from Neurospora crassa [5], Yamadazyma tenuis [2,3], Scheffersomyces stipitis [1], and the thermophilic fungus Chaetomium thermophilum [4,7], have dual coenzyme specificity, though they still prefer NADPH to NADH. Very rarely the enzyme prefers NADH [cf. EC 1.1.1.430, D-xylose reductase (NADH)].
History
EC 1.1.1.307 created 2010, modified 2022
Pathway
ec00040  Pentose and glucuronate interconversions
ec01100  Metabolic pathways
Orthology
K17743  D-xylose reductase
Genes
SASA100196319(xyl1)
QSU112005872 112027707
SCEYHR104W(GRE3)
SEUBDI49_2509
SPAOSPAR_H01460
AGOAGOS_ACL107C
ERCEcym_5508
KLAKLLA0_E21627g
KMXKLMA_10683(XYL1)
LTHKLTH0F16610g
ZROZYRO0A06336g
CGRCAGL0I01122g
NCSNCAS_0A06660(NCAS0A06660)
NDINDAI_0D01600(NDAI0D01600)
TPFTPHA_0E01860(TPHA0E01860)
TBLTBLA_0A00630(TBLA0A00630) TBLA_0F01720(TBLA0F01720)
TDLTDEL_0E02150(TDEL0E02150)
TGBHG536_0E00720
KAFKAFR_0C05320(KAFR0C05320)
KNGKNAG_0B03780(KNAG0B03780)
ZMKHG535_0C03920
PPAPAS_chr3_0744
DHADEHA2B00572g DEHA2F13068g
PICPICST_89614(XYL1)
PGUPGUG_00922 PGUG_02290
SPAASPAPADRAFT_61339(XYL1.2) SPAPADRAFT_61341(XYL1.1)
CALCAALFM_C502930CA(GRE3)
CTPCTRG_05978 CTRG_05993
COTCORT_0F01440
CDUCD36_52690(XYRA)
CTENCANTEDRAFT_95032
YLIYALI0D07634g
CLUCLUG_01135
CLUSA9F13_09g01958
CAURCJI97_000813
SLBAWJ20_3140(GRE3)
PKZC5L36_0B11990
BNNFOA43_003071(XYL1)
BBRXBRETT_005324(XYL1)
OPAHPODL_01370
SLUDSCDLUD_000181
NCRNCU08384(xr)
NTENEUTE1DRAFT133088(NEUTE1DRAFT_133088)
SMPSMAC_04649
PANPODANSg09635
TTTTHITE_2121064
MTMMYCTH_43671
CTHRCTHT_0056950
MGRMGG_01404 MGG_03648
PPEIPpBr36_00917 PpBr36_05674
TMNUCRPA7_3687 UCRPA7_6874
SSCKSPSK_06315
FGRFGSG_01523
FPUFPSE_05024
FVRFVEG_08194 FVEG_09602
FOXFOXG_01819 FOXG_11189
NHENECHADRAFT_102983 NECHADRAFT_38020
TRETRIREDRAFT_107776(xyl1)
TRRM419DRAFT_94809
MAJMAA_00542
PLJVFPFJ_08966
VALVDBG_00802 VDBG_03846 VDBG_06547
VDAVDAG_00411 VDAG_01073 VDAG_05087
CFJCFIO01_01300 CFIO01_01602
CHIGCH63R_03776 CH63R_05876
SAPOSAPIO_CDS7670 SAPIO_CDS9478
ELAUCREL1_14 UCREL1_6453
PFYPFICI_01687 PFICI_04525 PFICI_07157
SSLSS1G_05911
BFUBCIN_05g01550
MBEMBM_04242 MBM_09727
PSCOLY89DRAFT_599386 LY89DRAFT_657917
GLZGLAREA_03723
ANIAN0423.2
AFMAFUA_1G04820
ACTACLA_029850
NFINFIA_019940
AORAO090003000859
ANGANI_1_2444014(An01g03740)
AFVAFLA_000817
ALUCAKAW2_20539A(XYL1)
APUUAPUU_11638A(XYL1)
PCSPc16g09600
PDPPDIP_20350
TMFPMAA_054010 PMAA_100740
TRGTRUGW13939_00477
CIMCIMG_04915
CPWCPC735_069630
UREUREG_06636
ABEARB_06141
TVETRV_03808
PNOSNOG_12824
PTEPTT_08729
BZECOCCADRAFT_7101
BSCCOCSADRAFT_90781
BORCOCMIDRAFT_103379
AALTCC77DRAFT_925768
ZTRMYCGRDRAFT_56833
PFJMYCFIDRAFT_187110
FFUCLAFUR5_06085 CLAFUR5_06716
BCOMBAUCODRAFT_374705
NPAUCRNP2_5917
TMLGSTUM_00005097001
TVSTRAVEDRAFT_161569 TRAVEDRAFT_68124
DSQDICSQDRAFT_152560 DICSQDRAFT_95722
PCOPHACADRAFT_266555 PHACADRAFT_82194
SHSSTEHIDRAFT_117277 STEHIDRAFT_124813
HIRHETIRDRAFT_59016
PSQPUNSTDRAFT_95399
ADLAURDEDRAFT_181771
FMEFOMMEDRAFT_145959
GTRGLOTRDRAFT_113068 GLOTRDRAFT_71965
CCICC1G_12853
PCUBJR316_0009805
MPRMPER_01564
MRRMoror_16424
MOREE1B28_001457
SCMSCHCO_02610865(SCHCODRAFT_02610865)
CPUTCONPUDRAFT_96186
SLASERLADRAFT_455569
 » show all
Reference
1  [PMID:3921014]
  Authors
Verduyn C, Van Kleef R, Frank J, Schreuder H, Van Dijken JP, Scheffers WA
  Title
Properties of the NAD(P)H-dependent xylose reductase from the xylose-fermenting yeast Pichia stipitis.
  Journal
Biochem J 226:669-77 (1985)
DOI:10.1042/bj2260669
  Sequence
Reference
2  [PMID:9307017]
  Authors
Neuhauser W, Haltrich D, Kulbe KD, Nidetzky B
  Title
NAD(P)H-dependent aldose reductase from the xylose-assimilating yeast Candida tenuis. Isolation, characterization and biochemical properties of the enzyme.
  Journal
Biochem J 326 ( Pt 3):683-92 (1997)
DOI:10.1042/bj3260683
Reference
3  [PMID:10661866]
  Authors
Hacker B, Habenicht A, Kiess M, Mattes R.
  Title
Xylose utilisation: cloning and characterisation of the Xylose reductase from Candida tenuis.
  Journal
Biol Chem 380:1395-403 (1999)
DOI:10.1515/BC.1999.179
  Sequence
Reference
4  [PMID:12653995]
  Authors
Hakulinen N, Turunen O, Janis J, Leisola M, Rouvinen J.
  Title
Three-dimensional structures of thermophilic beta-1,4-xylanases from Chaetomium thermophilum and Nonomuraea flexuosa. Comparison of twelve xylanases in relation to their thermal stability.
  Journal
Eur J Biochem 270:1399-412 (2003)
DOI:10.1046/j.1432-1033.2003.03496.x
Reference
5  [PMID:15746370]
  Authors
Woodyer R, Simurdiak M, van der Donk WA, Zhao H
  Title
Heterologous expression, purification, and characterization of a highly active xylose reductase from Neurospora crassa.
  Journal
Appl Environ Microbiol 71:1642-7 (2005)
DOI:10.1128/AEM.71.3.1642-1647.2005
Reference
6  [PMID:20093741]
  Authors
Fernandes S, Tuohy MG, Murray PG
  Title
Xylose reductase from the thermophilic fungus Talaromyces emersonii: cloning and  heterologous expression of the native gene (Texr) and a double mutant (TexrK271R  + N273D) with altered coenzyme specificity.
  Journal
J Biosci 34:881-90 (2009)
DOI:10.1007/s12038-009-0102-7
Reference
7  [PMID:30621365]
  Authors
Quehenberger J, Reichenbach T, Baumann N, Rettenbacher L, Divne C, Spadiut O.
  Title
Kinetics and Predicted Structure of a Novel Xylose Reductase from Chaetomium thermophilum.
  Journal
Int J Mol Sci 20:E185 (2019)
DOI:10.3390/ijms20010185
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.307
IUBMB Enzyme Nomenclature: 1.1.1.307
ExPASy - ENZYME nomenclature database: 1.1.1.307
BRENDA, the Enzyme Database: 1.1.1.307

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