KEGG   ENZYME: 4.2.2.23Help
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
BRITE hierarchy
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
ATH: AT1G09880 AT1G09890 AT1G09910 AT2G22620 AT4G24430 AT4G37950 AT4G38030
ALY: ARALYDRAFT_315485 ARALYDRAFT_334271 ARALYDRAFT_353036 ARALYDRAFT_354330 ARALYDRAFT_481121 ARALYDRAFT_678634 ARALYDRAFT_888241 ARALYDRAFT_912531
CRB: 17877536 17877839 17879994 17888233 17895512 17897479 17898728 17900832
CSAT: 104702799 104713705 104716317 104717836 104719931 104720957 104722548 104729359 104729366 104733323 104739588 104739592 104739593 104739595 104751900 104755193 104755199 104768180 104768209 104768227 104773335 109132906
EUS: EUTSA_v10000697mg EUTSA_v100070380m EUTSA_v100070381m EUTSA_v10007058mg EUTSA_v10007093mg EUTSA_v10024612mg EUTSA_v10024647mg EUTSA_v10027081mg
BRP: 103831399 103835061 103835062 103835070 103835071 103835552 103837873 103856050 103864654 103871766 103871768 103871769
BNA: 106346230 106346232 106346233 106346234 106355619 106359062 106359063 106359064 106359931 106359932 106362387 106362388 106368688 106385932 106388898 106391090 106394509 106397523 106400863 106401657 106410089 106415698 106415701 106420305 106428211 106429378 106441989 106453127 111204098 111206064 111212361
BOE: 106294701 106294702 106295821 106297743 106307171 106309817 106328544 106330948 106332195 106333160 106340776 106343536
THJ: 104807150 104816790 104816791 104824556 104824916 104824920
CPAP: 110807303 110807313 110808050 110809043 110818789 110825605 110825606
LJA: Lj0g3v0234519.1(Lj0g3v0234519.1) Lj0g3v0234519.2(Lj0g3v0234519.2) Lj0g3v0286339.1(Lj0g3v0286339.1) Lj0g3v0307599.1(Lj0g3v0307599.1) Lj0g3v0307599.2(Lj0g3v0307599.2) Lj1g3v0178870.1(Lj1g3v0178870.1) Lj1g3v0178890.1(Lj1g3v0178890.1) Lj1g3v1601160.1(Lj1g3v1601160.1) Lj1g3v1601160.2(Lj1g3v1601160.2) Lj1g3v1601160.3(Lj1g3v1601160.3)
DOSA: Os08t0554100-01(Os08g0554100) Os08t0554300-00(Os08g0554300) Os11t0134100-00(Os11g0134100) Os12t0131900-00(Os12g0131900)
ATS: 109768786(LOC109768786) 109773154(LOC109773154) 109773214(LOC109773214) 109773218(LOC109773218) 109781634(LOC109781634) 109781635(LOC109781635)
DCT: 110097712
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)
XOO: XOO1078(rhgB)
XOM: XOO0978(XOO0978)
XOP: PXO_02430
XOR: XOC_3774
XAL: XALC_0866
XPH: XppCFBP6546_16655(XppCFBP6546P_16655)
PFS: PFLU_2268
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
BSS: BSUW23_03595(yesW)
BST: GYO_0965
BSO: BSNT_07086(yesW)
BSQ: B657_07050(yesW)
BSX: C663_0732(yesW)
BLI: BL03786(yesW)
BLD: BLi01376(yesW)
BLH: BaLi_c15180(yesW)
BATR: TD68_00735
BJS: MY9_0797
BACY: QF06_02430
BACL: BS34A_08040(yesW)
BALM: BsLM_0744
PPO: PPM_0906(M1_1103)
PPOL: X809_04520
PPOY: RE92_07105
MPS: MPTP_0357
CLT: CM240_2499(yesW)
HSC: HVS_15650(yesW)
CCE: Ccel_0739
CSD: Clst_0578
ACTI: UA75_11940
ACAD: UA74_11855
AHG: AHOG_11180(yesW1)
AMS: AMIS_4890
ASE: ACPL_4823
ACTS: ACWT_4692
OTE: Oter_2208
PIR: VN12_11290(yesW)
TTF: THTE_3601
FSC: FSU_2528
BOA: Bovatus_03112(yesX_1) Bovatus_03128(yesW_1)
BCEL: BcellWH2_02089(yesW_1) BcellWH2_04225(yesW_2)
MRO: MROS_0087
 » show all
Taxonomy
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)
  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)
  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)
  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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