KEGG ENZYME: 3.2.1.156

ENZYME: 3.2.1.156

Entry

EC 3.2.1.156                Enzyme

Name

oligosaccharide reducing-end xylanase;
Rex;
reducing end xylose-releasing exo-oligoxylanase

Class

Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

Sysname

beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranose reducing-end xylanase

Reaction(IUBMB)

Hydrolysis of (1->4)-beta-D-xylose residues from the reducing end of oligosaccharides

Comment

The enzyme, originally isolated from the bacterium Bacillus halodurans C-125, releases the xylose unit at the reducing end of oligosaccharides ending with the structure beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranose, leaving the new reducing end in the alpha configuration. It is specific for the beta anomers of xylooligosaccharides whose degree of polymerization is equal to or greater than 3.
The penultimate residue must be beta-D-xylopyranose, but replacing either of the flanking residues with glucose merely slows the rate greatly.

History

EC 3.2.1.156 created 2005

Orthology

K15531

oligosaccharide reducing-end xylanase

Genes

PSU:	Psesu_1642

PSUW:

WQ53_15240

PDD:	MNQ95_13805

VAS:	GT360_15735

PBW:	D172_007475 D172_007575

PEA:	PESP_a2206

PDV:	FFU37_07900

GAG:	Glaag_3338

PMES:

FX988_01654

PAT:

Patl_1069

LAL:	AT746_17515

AGZ:	M0C34_14060

AGQ:	LQZ07_17215

AGAR:

OAG1_13490

TTU:	TERTU_4506

MARQ:

MARGE09_P0229

TMJ:	P0M04_04365

NOR:	FA702_20220

SPAN:

AWL63_12905

SNOS:

K8P63_13375

POQ:	KZX46_13660

SCL:	sce3034(xynA1) sce3220(xynB1) sce5506(celY)

SCU:	SCE1572_01605 SCE1572_33355

BLH:	BaLi_c13740

BGY:

BGLY_2144

BCO:	Bcell_0537

BCIR:

C2I06_14670

BHA:

BH2105

AXL:

AXY_02640

RAX:	KO561_16435

GRC:	GI584_07915

GCS:	MUN88_20515

GSM:	MUN87_21045

NDT:	L1999_24425

BLEN:

NCTC4824_01188

CTHU:

HUR95_01350

PUK:	PU629_17345

PJD:	Pjdr2_1182

PMS:	KNP414_05090

PMQ:	PM3016_4494

PMW:

B2K_23280

PBD:	PBOR_13600

PGM:	PGRAT_23195

POD:	PODO_15035

PAEN:

P40081_13355

PAEF:

R50345_15165

PAEQ:

R50912_12865

PAEA:

R70723_17020

PAEH:

H70357_26020

PAEJ:

H70737_14560

PRI:

PRIO_5053

PSON:

JI735_32765

PXL:	BS614_18680

PYG:	AWM70_04450

PCX:	LPB68_10700

PLEN:

EIM92_02000

PLUT:

EI981_12140

PALB:

EJC50_08440

PPRT:

ET464_15535

PBAC:

HUB98_01525

PRZ:	GZH47_08690

PTRI:

KDC22_11965

PALO:

E6C60_0359

PCEL:

HUB94_09235

PTJ:	JRJ22_06130

PALR:

HGI30_05695

PUI:	PUW25_11625

PAMY:

P9222_22550

PMAE:

LMZ02_22435

PWN:	QNH46_02725

PPOG:

QPK24_02270

PPAB:

KET34_19105

PHEX:

L0M14_07460

PEZZ:

HW560_20120

TCO:	Theco_2781

CCHL:

FPL14_20820

CHEB:

HH215_32165

COHL:

J4772_14570

PLIG:

NAG76_03265

ACUR:

JZ785_24025

ALIC:

GI364_18535

LLK:

LLKF_1370

LLS:

lilo_1253

LLD:	P620_07390

LLX:	NCDO2118_1333

LLJ:

LG36_1096

LLM:

llmg_1166

LLC:

LACR_1432

LLN:	LLNZ_06010

LLI:	uc509_1320

LLW:

kw2_1262

WCF:	C6P13_00675

JEH:	EJN90_05505

JPO:	G7058_09330

CCB:	Clocel_1174

CLB:	Clo1100_0977 Clo1100_2907

CSR:	Cspa_c48550

CEU:	A7L45_08740

CNN:	CNEO_0645(rex)

CGEL:

psyc5s11_13970

HSC:

HVS_07865

CCE:	Ccel_1258 Ccel_1298

RHER:

EHE19_001765

RPAY:

P0092_05635 P0092_16715

RAL:	Rumal_0143

CAML:

H6X83_10020

CARL:

PXC00_10470

SVJ:	NQ490_05670

TMEL:

NOG13_05365

ALAC:

JYE50_03220

AHC:	JYE49_03950

CBAF:

JS518_05560

BPB:	bpr_I1513(xyn8A)

BFI:

CIY_10200

BHU:

bhn_I1756

RHO:	RHOM_05800

RIX:

RO1_26360

RIM:

ROI_37850

RRK:	H8S51_014625

BCOC:

BLCOC_19390(rex8A)

CPY:

Cphy_3207

LXA:	OW255_16265

HSD:

SD1D_1946

PXV:	FXF36_09920

ANR:	Ana3638_24525

ACEL:

acsn021_18590

ACHT:

bsdcttw_09280

SSUN:

H9Q77_06580

ERE:	EUBREC_1040

ERT:

EUR_20710

ERA:

ERE_20750

KIB:	RBB56_03280

CLE:	Clole_0527

CEW:	EKH84_05885

MAS:	Mahau_0199

HALS:

D7D81_17550

IFN:	GM661_14245

LXL:	KDY119_00669

XYL:	ET495_14880

BLL:

BLJ_1599

BLX:	GS08_08310

BAD:

BAD_0300

BADL:

BADO_0309

BADO:

BBMN23_0330

BKS:	BBKW_0330 BBKW_1070

BCAT:

BBCT_0289

BANG:

BBAG_0150

BPSC:

BBPC_0318 BBPC_0452

BGX:	ESN35_08235

BLEM:

BL8807_01490

BFJ:	B19861_02990

LEPT:

JVX88_31280

ATM:

ANT_28570

KBB:	ccbrp13_32240

PMET:

G4Y79_07185

DGE:

Dgeo_2684

OTE:	Oter_4314 Oter_4315

OBG:	Verru16b_00621

SLOM:

PXH66_18790

AAQW:

K1X11_013845

TPER:

IWA51_02565

SPER:

EW093_01550

SCD:	Spica_0597

GRW:	FTO74_03600

EPL:	P4G45_06845

ORP:	MOP44_11715

PFER:

IRI77_02195

FSU:	Fisuc_0207 Fisuc_0241 Fisuc_0471

FSC:	FSU_0613 FSU_0651 FSU_0889

BCEL:

BcellWH2_03025 BcellWH2_04306

BZG:	C4H11_06925

BHF:	C3V43_08980

BIS:	DXK01_005885 DXK01_010990

BEG:	INE88_02925

PPN:	Palpr_1660

PHER:

prwr041_12880

PRU:

PRU_1268

DORI:

FH5T_02230

DRC:	G0Q07_10265

ANF:

AQPE_2614

ASX:	CDL62_11475

NYN:	U0035_01075

ARK:	D6B99_10715

LACS:

H4075_10065

PEJ:	FYC62_01085

MGK:	FSB76_27380

MMAB:

HQ865_13530

MDJ:	LLH06_14900

SLI:

Slin_1409

SRHO:

HH216_13175

FAE:

FAES_2330

FIB:	A6C57_09615

HYJ:	FHG12_11460

HQI:	H9L05_06030

HTS:	HMJ29_19330

HMT:	MTP16_15095

HTB:	MTX78_24795

HSB:	MWH26_09000

HCF:	MUN80_21690

PONT:

C1N53_08450

RTI:	DC20_16660

FLM:

MY04_4897

FBT:	D770_14475

FJO:

Fjoh_3868

FJG:	BB050_03127

FCM:	BIW12_10340

FEN:	J0383_05000

FPB:	NLJ00_21465

FBI:	L0669_10660

FHU:	M0M44_20535

FPEC:

Q1W71_03745

SALT:

AO058_06980

AQD:	D1816_13825

» show all

Reference

1 [PMID:15491996]

Authors

Honda Y, Kitaoka M

Title

A family 8 glycoside hydrolase from Bacillus halodurans C-125 (BH2105) is a reducing end xylose-releasing exo-oligoxylanase.

Journal

J Biol Chem 279:55097-103 (2004)
DOI:10.1074/jbc.M409832200

Sequence

[bha:BH2105]

Reference

2 [PMID:15718242]

Authors

Fushinobu S, Hidaka M, Honda Y, Wakagi T, Shoun H, Kitaoka M.

Title

Structural basis for the specificity of the reducing end xylose-releasing exo-oligoxylanase from Bacillus halodurans C-125.

Journal

J Biol Chem 280:17180-6 (2005)
DOI:10.1074/jbc.M413693200

Sequence

[bha:BH2105]

Other DBs

ExplorEnz - The Enzyme Database:

3.2.1.156

IUBMB Enzyme Nomenclature:

3.2.1.156

ExPASy - ENZYME nomenclature database:

3.2.1.156

BRENDA, the Enzyme Database:

3.2.1.156

CAS:	879497-03-7

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   KEGG ORTHOLOGY (1)   
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Protein sequence (137)   
   UniProt (110)   
   SWISS-PROT (3)   
   PDBSTR (24)   
DNA sequence (47)   
   GenBank (24)   
   EMBL (23)   
3D Structure (15)   
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Protein domain (3)   
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