KEGG   ENZYME: 4.2.2.23
Entry
EC 4.2.2.23                 Enzyme                                 

Name
rhamnogalacturonan endolyase;
rhamnogalacturonase B;
alpha-L-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronide lyase;
Rgase B;
rhamnogalacturonan alpha-L-rhamnopyranosyl-(1,4)-alpha-D-galactopyranosyluronide lyase;
RG-lyase;
YesW;
RGL4;
Rgl11A;
Rgl11Y;
RhiE
Class
Lyases;
Carbon-oxygen lyases;
Acting on polysaccharides
Sysname
alpha-L-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronate endolyase
Reaction(IUBMB)
Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.
Comment
The enzyme is part of the degradation system for rhamnogalacturonan I in Bacillus subtilis strain 168 and Aspergillus aculeatus.
History
EC 4.2.2.23 created 2011
Orthology
K18195  rhamnogalacturonan endolyase
K18197  rhamnogalacturonan endolyase
Genes
DPA: 109532755 109533223 109538156 109538157 109538158
APLN: 108734492 108734509 108734566 108734567 108734573 108737019 108737022 108737035 108737036 108741360 112906427 112906656
ATH: AT1G09880 AT1G09890 AT1G09910 AT2G22620 AT4G24430 AT4G37950 AT4G38030
ALY: 9305022 9305028 9305791 9314693 9322893 9325839 9325840 9328595
CRB: 17877536 17877839 17879994 17888233 17895512 17897479 17898728 17900832
CSAT: 104702799 104713705 104716317 104717836 104719931 104720957 104722548 104729359 104729366 104733323 104739588 104739592 104739593 104751900 104755193 104755199 104768180 104768209 104768227 104773335 109132906
EUS: EUTSA_v10000697mg EUTSA_v100070381m EUTSA_v10007058mg EUTSA_v10007093mg EUTSA_v10024612mg EUTSA_v10024647mg EUTSA_v10027081mg
BRP: 103831399 103835061 103835062 103835070 103835071 103837873 103856050 103864654 103871766 103871768 103871769 117127273
BNA: 106346230 106346232 106346233 106346234 106355619 106359062 106359063 106359064 106359931 106359932 106362387 106368688 106385932 106391090 106394509 106397523 106400863 106401657 106410089 106415698 106420305 106428211 106429378 106441989 106453127 111204098 111212361
BOE: 106294701 106294702 106295821 106297743 106307171 106309817 106328544 106330948 106332195 106333160 106340776 106343536
LJA: Lj0g3v0234519.1(Lj0g3v0234519.1) Lj0g3v0234519.2(Lj0g3v0234519.2) Lj0g3v0286339.1(Lj0g3v0286339.1) Lj0g3v0307599.1(Lj0g3v0307599.1) Lj0g3v0307599.2(Lj0g3v0307599.2) Lj1g3v1601160.1(Lj1g3v1601160.1) Lj1g3v1601160.2(Lj1g3v1601160.2)
DOSA: Os08t0554100-01(Os08g0554100) Os08t0554300-00(Os08g0554300) Os11t0134100-00(Os11g0134100) Os12t0131900-00(Os12g0131900)
DCT: 110097712
PEQ: 110022118
NCR: NCU05598(asd-1)
NTE: NEUTE1DRAFT118112(NEUTE1DRAFT_118112)
MGR: MGG_06041
ANG: ANI_1_1554094(An11g00390) ANI_1_190124(An14g01130)
CNE: CNF04250
CNB: CNBF0610
ABP: AGABI1DRAFT120786(AGABI1DRAFT_120786)
ABV: AGABI2DRAFT72717(AGABI2DRAFT_72717)
ECA: ECA0804(rhiE)
PATR: EV46_03550
PATO: GZ59_07120(rhiE)
PCT: PC1_0682
PEC: W5S_0801
DDD: Dda3937_01465(rhiE)
XCP: XCR_3715
XCV: XCV3632
XAX: XACM_3402
XAC: XAC3505(rhgB)
XCI: XCAW_04203(rhgB)
XOM: XOO0978(XOO0978)
XOO: XOO1078(rhgB)
XOP: PXO_02430
XOR: XOC_3774
XAL: XALC_0866
XPH: XppCFBP6546_16655(XppCFBP6546P_16655)
PFS: PFLU_2268
CJA: CJA_3559(rgl11A)
SDE: Sde_1650(rgl11A)
SCL: sce3040
CSE: Cseg_2735
SSAN: NX02_27730
BSU: BSU07050(yesW)
BSR: I33_0796
BSL: A7A1_1749
BSH: BSU6051_07050(yesW)
BSUT: BSUB_00778(yesW)
BSUL: BSUA_00778(yesW)
BSUS: Q433_03970
BSO: BSNT_07086(yesW)
BSQ: B657_07050(yesW)
BSX: C663_0732(yesW)
BSS: BSUW23_03595(yesW)
BST: GYO_0965
BLI: BL03786(yesW)
BLD: BLi01376(yesW)
BLH: BaLi_c15180(yesW)
BSON: S101395_03472(yesW)
BMOJ: HC660_07520(rhgW)
BJS: MY9_0797
BACY: QF06_02430
BACL: BS34A_08040(yesW)
BALM: BsLM_0744
BEO: BEH_10495
BCL: ABC0393
PPY: PPE_00977
PPO: PPM_0906(M1_1103) PPM_0964(yesW)
PPOY: RE92_07105
MPS: MPTP_0357
CLT: CM240_2499(yesW)
CTH: Cthe_0246
HSC: HVS_15650(yesW)
CSD: Clst_0578
RCH: RUM_16320
ACEL: acsn021_37710(yesW)
SMAL: SMALA_5402
SFA: Sfla_5890
STRP: F750_0685
SAMB: SAM23877_6247(yesW)
SPRI: SPRI_1191
SLE: sle_12370(sle_12370)
SRN: A4G23_01860(yesW)
STRD: NI25_05685
CMS: CMS0960
MOO: BWL13_02659(yesX)
AAGI: NCTC2676_1_02228(yesW)
ACH: Achl_0488
JDE: Jden_0215
CFL: Cfla_3043
KFL: Kfla_5324
TFU: Tfu_2009
NDA: Ndas_0923
STRR: EKD16_15050(yesW)
NCX: Nocox_23295(yesW)
TBI: Tbis_2022
AMD: AMED_7411
AMN: RAM_38095
AMM: AMES_7300
AMZ: B737_7300
AMYY: YIM_20855(yesW1) YIM_32675(yesW2)
AORI: SD37_23545
AMI: Amir_1868
AHG: AHOG_11180(yesW1) AHOG_15410(yesW2)
MIL: ML5_3906
ASE: ACPL_4823
AMS: AMIS_4890
ACTN: L083_4250
AFS: AFR_19580
ACTS: ACWT_4692
HAU: Haur_3462
PIR: VN12_11290(yesW)
TTF: THTE_3601
AMUC: Pan181_16990(yesW_1) Pan181_17000(yesW_2) Pan181_24400(yesW_3)
PND: Pla175_31790(yesW_1) Pla175_31810(yesW_2)
PBU: L21SP3_00779(yesW_2)
PBP: STSP1_00184(yesW)
SUS: Acid_6872
FSC: FSU_2528
BOA: Bovatus_03112(yesX_1) Bovatus_03128(yesW_1) Bovatus_04416(yesW_2)
BCEL: BcellWH2_02089(yesW_1) BcellWH2_04225(yesW_2)
PSAC: PSM36_0916
PRU: PRU_1571
STHA: NCTC11429_02150(yesW)
FJO: Fjoh_4222
MRO: MROS_0087
 » show all
Reference
1  [PMID:8587995]
  Authors
Mutter M, Colquhoun IJ, Schols HA, Beldman G, Voragen AG
  Title
Rhamnogalacturonase B from Aspergillus aculeatus is a rhamnogalacturonan alpha-L-rhamnopyranosyl-(1-->4)-alpha-D-galactopyranosyluronide lyase.
  Journal
Plant Physiol 110:73-7 (1996)
DOI:10.1104/pp.110.1.73
  Sequence
Reference
2  [PMID:8720076]
  Authors
Azadi P, O'Neill MA, Bergmann C, Darvill AG, Albersheim P
  Title
The backbone of the pectic polysaccharide rhamnogalacturonan I is cleaved by an endohydrolase and an endolyase.
  Journal
Glycobiology 5:783-9 (1995)
DOI:10.1093/glycob/5.8.783
  Sequence
Reference
3  [PMID:9576783]
  Authors
Mutter M, Colquhoun IJ, Beldman G, Schols HA, Bakx EJ, Voragen AG
  Title
Characterization of recombinant rhamnogalacturonan alpha-L-rhamnopyranosyl-(1,4)-alpha-D-galactopyranosyluronide lyase from Aspergillus aculeatus. An enzyme that fragments rhamnogalacturonan I regions of pectin.
  Journal
Plant Physiol 117:141-52 (1998)
DOI:10.1104/pp.117.1.141
  Sequence
Reference
4  [PMID:12136151]
  Authors
Kadirvelraj R, Harris P, Poulsen JC, Kauppinen S, Larsen S
  Title
A stepwise optimization of crystals of rhamnogalacturonan lyase from Aspergillus aculeatus.
  Journal
Acta Crystallogr D Biol Crystallogr 58:1346-9 (2002)
DOI:10.1107/S0907444902009137
  Sequence
Reference
5  [PMID:12591882]
  Authors
Laatu M, Condemine G
  Title
Rhamnogalacturonate lyase RhiE is secreted by the out system in Erwinia chrysanthemi.
  Journal
J Bacteriol 185:1642-9 (2003)
DOI:10.1128/JB.185.5.1642-1649.2003
  Sequence
Reference
6  [PMID:12896991]
  Authors
Pages S, Valette O, Abdou L, Belaich A, Belaich JP
  Title
A rhamnogalacturonan lyase in the Clostridium cellulolyticum cellulosome.
  Journal
J Bacteriol 185:4727-33 (2003)
DOI:10.1128/JB.185.16.4727-4733.2003
Reference
7  [PMID:16682770]
  Authors
Ochiai A, Yamasaki M, Itoh T, Mikami B, Hashimoto W, Murata K
  Title
Crystallization and preliminary X-ray analysis of the rhamnogalacturonan lyase YesW from Bacillus subtilis strain 168, a member of polysaccharide lyase family 11.
  Journal
Acta Crystallogr Sect F Struct Biol Cryst Commun 62:438-40 (2006)
DOI:10.1107/S1744309106011894
  Sequence
[bsu:BSU07050]
Reference
8  [PMID:20851126]
  Authors
Jensen MH, Otten H, Christensen U, Borchert TV, Christensen LL, Larsen S, Leggio LL
  Title
Structural and biochemical studies elucidate the mechanism of rhamnogalacturonan lyase from Aspergillus aculeatus.
  Journal
J Mol Biol 404:100-11 (2010)
DOI:10.1016/j.jmb.2010.09.013
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 4.2.2.23
IUBMB Enzyme Nomenclature: 4.2.2.23
ExPASy - ENZYME nomenclature database: 4.2.2.23
BRENDA, the Enzyme Database: 4.2.2.23

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