KEGG ENZYME: 1.1.1.307

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 cosubstrate 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

SASA:

100196319(xyl1)

SCE:	YHR104W(GRE3)

SEUB:

DI49_2509

SPAO:

SPAR_H01460

AGO:	AGOS_ACL107C

ERC:

Ecym_5508

KLA:	KLLA0_E21627g

KMX:	KLMA_10683(XYL1)

LTH:	KLTH0F16610g

ZRO:	ZYRO0A06336g

CGR:	CAGL0I01122g

NCS:	NCAS_0A06660(NCAS0A06660)

NDI:	NDAI_0D01600(NDAI0D01600)

TPF:	TPHA_0E01860(TPHA0E01860)

TBL:	TBLA_0A00630(TBLA0A00630) TBLA_0F01720(TBLA0F01720)

TGB:	HG536_0E00720

TDL:	TDEL_0E02150(TDEL0E02150)

KAF:	KAFR_0C05320(KAFR0C05320)

KNG:	KNAG_0B03780(KNAG0B03780)

ZMK:	HG535_0C03920

PPA:	PAS_chr3_0744

DHA:	DEHA2B00572g DEHA2F13068g

PIC:	PICST_89614(XYL1)

PGU:	PGUG_00922 PGUG_02290

SPAA:

SPAPADRAFT_61339(XYL1.2) SPAPADRAFT_61341(XYL1.1)

CAL:	CAALFM_C502930CA(GRE3)

CTP:	CTRG_05978 CTRG_05993

COT:	CORT_0F01440

CDU:	CD36_52690(XYRA)

CTEN:

CANTEDRAFT_95032

YLI:	YALI0D07634g

CLU:	CLUG_01135

CLUS:

A9F13_09g01958

CAUR:

CJI96_0003286

SLB:	AWJ20_3140(GRE3)

PKZ:	C5L36_0B11990

BNN:	FOA43_003071(XYL1)

BBRX:

BRETT_005324(XYL1)

OPA:	HPODL_01370

SLUD:

SCDLUD_000181

NCR:	NCU08384(xr)

NTE:	NEUTE1DRAFT133088(NEUTE1DRAFT_133088)

SMP:	SMAC_04649

PAN:	PODANSg09635

TTT:	THITE_2121064

MTM:	MYCTH_43671

CTHR:

CTHT_0056950

MGR:	MGG_01404 MGG_03648

PPEI:

PpBr36_00917 PpBr36_05674

PGRI:

PgNI_00350 PgNI_04112

TMN:	UCRPA7_3687 UCRPA7_6874

SSCK:

SPSK_06315

FGR:	FGSG_01523

FPU:	FPSE_05024

FPOA:

FPOAC1_001631(XYL1)

FVN:	FVRRES_01841

FVR:	FVEG_08194 FVEG_09602

FOX:	FOXG_01819 FOXG_11189

NHE:	NECHADRAFT_102983 NECHADRAFT_38020

FFC:	NCS54_00032000 NCS54_00545600

FMU:	J7337_000363(XYL1_1) J7337_002765(XYL1_2)

TRE:	TRIREDRAFT_107776(xyl1)

TRR:	M419DRAFT_94809

MAJ:

MAA_00542

PCHM:

VFPPC_01147

PLJ:	VFPFJ_08966

VAL:	VDBG_00802 VDBG_03846 VDBG_06547

VDA:	VDAG_00411 VDAG_01073 VDAG_05087

CFJ:	CFIO01_01300 CFIO01_01602

CLUP:

CLUP02_07368 CLUP02_13788

CHIG:

CH63R_03776 CH63R_05876

SAPO:

SAPIO_CDS7670 SAPIO_CDS9478

ELA:	UCREL1_14 UCREL1_6453

PFY:	PFICI_01687 PFICI_04525 PFICI_07157

SSL:	SS1G_05911

BFU:	BCIN_05g01550

MBE:	MBM_04242 MBM_09727

PSCO:

LY89DRAFT_599386 LY89DRAFT_657917

GLZ:	GLAREA_03723

ANI:

AN0423.2

AFM:	AFUA_1G04820

ACT:	ACLA_029850

NFI:	NFIA_019940

AOR:	AO090003000859

ANG:	An01g03740(xyrA)

AFV:	AFLA_000817

ALUC:

AKAW2_20539A(XYL1)

APUU:

APUU_11638A(XYL1)

PCS:	Pc16g09600

PDP:	PDIP_20350

POU:	POX_e06956

TMF:	EYB26_006490 EYB26_008282

TRG:	TRUGW13939_00477

CIM:	CIMG_04915

CPW:	CPC735_069630

URE:	UREG_06636

ABE:

ARB_06141

TVE:

TRV_03808

PNO:	SNOG_12824

PTE:

PTT_08729

BZE:	COCCADRAFT_7101

BSC:	COCSADRAFT_90781

BOR:	COCMIDRAFT_103379

AALT:

CC77DRAFT_925768

ARAB:

EKO05_0011455

ZTR:	MYCGRDRAFT_56833

PFJ:	MYCFIDRAFT_187110

FFU:	CLAFUR5_06085 CLAFUR5_06716

CBET:

CB0940_08334

BCOM:

BAUCODRAFT_374705

NPA:	UCRNP2_5917

TML:	GSTUM_00005097001

CCAC:

CcaHIS019_0108390(xyl1)

TVS:	TRAVEDRAFT_161569 TRAVEDRAFT_68124

DSQ:	DICSQDRAFT_152560 DICSQDRAFT_95722

PCO:	PHACADRAFT_266555 PHACADRAFT_82194

SHS:	STEHIDRAFT_117277 STEHIDRAFT_124813

HIR:	HETIRDRAFT_59016

PSQ:	PUNSTDRAFT_95399

ADL:	AURDEDRAFT_181771

FME:	FOMMEDRAFT_145959

GTR:	GLOTRDRAFT_113068 GLOTRDRAFT_71965

RSX:	RhiXN_11579

CCI:	CC1G_12853

PCUB:

JR316_0009805

MPR:	MPER_01564

MRR:	Moror_16424

E1B28_001457

SCM:	SCHCO_02610865(SCHCODRAFT_02610865)

CPUT:

CONPUDRAFT_96186

SLA:	SERLADRAFT_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

[pic:PICST_89614]

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

[ag:AAC25601]

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

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