KEGG   ENZYME: 1.1.1.431
Entry
EC 1.1.1.431                Enzyme                                 
Name
D-xylose reductase (NADPH);
XYL1 (gene name, ambiguous);
xyl1 (gene name, ambiguous);
xyrA (gene name);
xyrB (gene name)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
Sysname
xylitol:NADP+ oxidoreductase
Reaction(IUBMB)
xylitol + NADP+ = D-xylose + NADPH + H+ [RN:R01431]
Reaction(KEGG)
R01431
Substrate
xylitol [CPD:C00379];
NADP+ [CPD:C00006]
Product
D-xylose [CPD:C00181];
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 (e.g. the enzymes from Saccharomyces cerevisiae, Aspergillus niger, Trichoderma reesei, Candida tropicalis, Saitozyma flava, and Candida intermedia). Some D-xylose reductases have dual cosubstrate specificity, though they still prefer NADPH to NADH (cf. EC 1.1.1.307, D-xylose reductase [NAD(P)H]). Very rarely the enzyme prefers NADH (cf. EC 1.1.1.430, D-xylose reductase (NADH)).
History
EC 1.1.1.431 created 2022
Orthology
K17743  D-xylose reductase
K26066  D-xylose/L-arabinose reductase (NADPH)
Genes
SASA100196319(xyl1)
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)
TGBHG536_0E00720
TDLTDEL_0E02150(TDEL0E02150)
KAFKAFR_0C05320(KAFR0C05320)
KNGKNAG_0B03780(KNAG0B03780)
ZMKHG535_0C03920
PPAPAS_chr3_0744
DHADEHA2B00572g DEHA2E24244g DEHA2F13068g
PICPICST_89614(XYL1)
PGUPGUG_00922 PGUG_02290 PGUG_05385
SPAASPAPADRAFT_61339(XYL1.2) SPAPADRAFT_61341(XYL1.1)
CALCAALFM_C502930CA(GRE3)
CTPCTRG_05978 CTRG_05993
COTCORT_0F01440
CDUCD36_52690(XYRA)
CTENCANTEDRAFT_102630 CANTEDRAFT_95032
YLIYALI0D07634g
CLUCLUG_01135
CLUSA9F13_09g01958
CAURCJI96_0001805 CJI96_0003286
SLBAWJ20_3140(GRE3)
PKZC5L36_0B11990
BNNFOA43_003071(XYL1)
BBRXBRETT_005324(XYL1)
OPAHPODL_00132 HPODL_01370
SLUDSCDLUD_000181
NCRNCU08384(xr)
NTENEUTE1DRAFT133088(NEUTE1DRAFT_133088)
SMPSMAC_04649
PANPODANSg09635
PBELQC761_103840(xyl1)
PPSDQC762_103840(xyl1)
PPSPQC763_103840(xyl1)
PPSAQC764_103840(xyl1)
TTTTHITE_2121064
MTMMYCTH_43671
CTHRCTHT_0056950
MGRMGG_01404 MGG_03648
PPEIPpBr36_00917 PpBr36_05674
PGRIPgNI_00350 PgNI_04112
TMNUCRPA7_3687 UCRPA7_6054 UCRPA7_6874
SSCKSPSK_06315 SPSK_10284
FGRFGSG_01523
FPUFPSE_05024
FPOAFPOAC1_001631(XYL1)
FVNFVRRES_01841
FVRFVEG_08194 FVEG_09602
FOXFOXG_01819 FOXG_11189
NHENECHADRAFT_102983 NECHADRAFT_37143 NECHADRAFT_38020 NECHADRAFT_42050
FFCNCS54_00032000 NCS54_00545600
FKRNCS57_00030100 NCS57_00469500 NCS57_00583800
FMUJ7337_000363(XYL1_1) J7337_002765(XYL1_2)
TRETRIREDRAFT_107776(xyl1)
TRRM419DRAFT_94809
MAJMAA_00542
PCHMVFPPC_01147 VFPPC_01327
CMTCCM_06357 CCM_08784
AMUSLMH87_002846 LMH87_007757
PLJVFPFJ_06456 VFPFJ_08966
PTKZJDV02_009626
VALVDBG_00802 VDBG_03846 VDBG_06547
VDAVDAG_00411 VDAG_01073 VDAG_05087
CFJCFIO01_01300 CFIO01_01602 CFIO01_09197 CFIO01_10020 CFIO01_11827
CLUPCLUP02_07368 CLUP02_13788 CLUP02_15584
CHIGCH63R_03776 CH63R_05876
SAPOSAPIO_CDS7670 SAPIO_CDS9478
ELAUCREL1_14 UCREL1_6453 UCREL1_8867
PFYPFICI_01687 PFICI_04525 PFICI_05410 PFICI_06515 PFICI_07157 PFICI_10486
SSLSS1G_05911
BFUBCIN_05g01550
MBEMBM_04242 MBM_09727
PSCOLY89DRAFT_599386 LY89DRAFT_656415 LY89DRAFT_657917
GLZGLAREA_03723
ANIANIA_00423 ANIA_03312
AFMAFUA_1G04820 AFUA_6G13830
ACTACLA_029850 ACLA_087030
NFINFIA_019940 NFIA_059700
AORAO090003000859 AO090103000359 AO090701000415
ANGAn01g03740(xyrA) An08g08480 An08g09360
AFVAFLA_000817 AFLA_004930 AFLA_013173
ALUCAKAW2_20539A(XYL1) AKAW2_51678S
ACHEACHE_10084A ACHE_50426S ACHE_50561S
APUUAPUU_10973S APUU_11638A(XYL1) APUU_60796S APUU_60916A
PCSN7525_006115 N7525_010651 N7525_010789
PDPPDIP_20350
POUPOX_e06956
TMFEYB26_006490 EYB26_008282
TRGTRUGW13939_00477 TRUGW13939_09110 TRUGW13939_09270
CIMCIMG_04915
CPWCPC735_069630
UREUREG_06636
ABEARB_06141
TVETRV_03808
PNOSNOG_12824
PTEPTT_08729
BZECOCCADRAFT_26499 COCCADRAFT_7101
BSCCOCSADRAFT_41505 COCSADRAFT_90781
BORCOCMIDRAFT_103379 COCMIDRAFT_31692
AALTCC77DRAFT_925768
ARABEKO05_0011455
ZTRMYCGRDRAFT_31902 MYCGRDRAFT_56833
PFJMYCFIDRAFT_187110 MYCFIDRAFT_209507
FFUCLAFUR5_06085 CLAFUR5_06716
CBETCB0940_00153 CB0940_08334
BCOMBAUCODRAFT_374705
NPAUCRNP2_5371 UCRNP2_5917
TMLGSTUM_00005097001
CCACCcaHIS019_0108390(xyl1)
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
RSXRhiXN_11579
CCICC1G_12853
PCUBJR316_0009805
MPRMPER_01564
MRRMoror_16424
MOREE1B28_001457
SCMSCHCO_02610865(SCHCODRAFT_02610865)
CPUTCONPUDRAFT_96186
SLASERLADRAFT_455569
 » show all
Reference
1  [PMID:18553673]
  Authors
Bolen PL, Detroy RW.
  Title
Induction of NADPH-linked D-xylose reductase and NAD-linked xylitol dehydrogenase activities in Pachysolen tannophilus by D-xylose, L-arabinose, or D-galactose.
  Journal
Biotechnol Bioeng 27:302-7 (1985)
DOI:10.1002/bit.260270314
Reference
2  [PMID:16232468]
  Authors
Suzuki T, Yokoyama S, Kinoshita Y, Yamada H, Hatsu M, Takamizawa K, Kawai K.
  Title
Expression of xyrA gene encoding for D-Xylose reductase of Candida tropicalis and production of xylitol in Escherichia coli.
  Journal
J Biosci Bioeng 87:280-4 (1999)
DOI:10.1016/s1389-1723(99)80032-2
  Sequence
Reference
3  [PMID:10548539]
  Authors
Nidetzky B, Mayr P, Hadwiger P, Stutz AE.
  Title
Binding energy and specificity in the catalytic mechanism of yeast aldose reductases.
  Journal
Biochem J 344 Pt 1:101-7 (1999)
Reference
4  [PMID:10681056]
  Authors
Mayr P, Bruggler K, Kulbe KD, Nidetzky B.
  Title
D-Xylose metabolism by Candida intermedia: isolation and characterisation of two forms of aldose reductase with different coenzyme specificities.
  Journal
J Chromatogr B Biomed Sci Appl 737:195-202 (2000)
DOI:10.1016/s0378-4347(99)00380-1
Reference
5  [PMID:11963895]
  Authors
Sene L, Felipe MG, Silva SS, Vitolo M.
  Title
Preliminary kinetic characterization of xylose reductase and xylitol dehydrogenase extracted from Candida guilliermondii FTI 20037 cultivated in sugarcane bagasse hydrolysate for xylitol production.
  Journal
Appl Biochem Biotechnol 91-93:671-80 (2001)
DOI:10.1385/abab:91-93:1-9:671
Reference
6  [PMID:11481678]
  Authors
Jeong EY, Sopher C, Kim IS, Lee H.
  Title
Mutational study of the role of tyrosine-49 in the Saccharomyces cerevisiae xylose reductase.
  Journal
Yeast 18:1081-9 (2001)
DOI:10.1002/yea.758
  Sequence
[sce:YHR104W]
Reference
7  [PMID:33666344]
  Authors
Chroumpi T, Peng M, Aguilar-Pontes MV, Muller A, Wang M, Yan J, Lipzen A, Ng V, Grigoriev IV, Makela MR, de Vries RP.
  Title
Revisiting a 'simple' fungal metabolic pathway reveals redundancy, complexity and diversity.
  Journal
Microb Biotechnol 14:2525-2537 (2021)
DOI:10.1111/1751-7915.13790
Reference
8  [PMID:33842213]
  Authors
Terebieniec A, Chroumpi T, Dilokpimol A, Aguilar-Pontes MV, Makela MR, de Vries RP.
  Title
Characterization of d-xylose reductase, XyrB, from Aspergillus niger.
  Journal
Biotechnol Rep (Amst) 30:e00610 (2021)
DOI:10.1016/j.btre.2021.e00610
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.431
IUBMB Enzyme Nomenclature: 1.1.1.431
ExPASy - ENZYME nomenclature database: 1.1.1.431
BRENDA, the Enzyme Database: 1.1.1.431

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