KEGG   ENZYME: 4.2.2.2Help
Entry
EC 4.2.2.2                  Enzyme                                 

Name pectate lyase;
polygalacturonic transeliminase;
pectic acid transeliminase;
polygalacturonate lyase;
endopectin methyltranseliminase;
pectate transeliminase;
endogalacturonate transeliminase;
pectic acid lyase;
pectic lyase;
alpha-1,4-D-endopolygalacturonic acid lyase;
PGA lyase;
PPase-N;
endo-alpha-1,4-polygalacturonic acid lyase;
polygalacturonic acid lyase;
pectin trans-eliminase;
Polygalacturonic acid trans-eliminase
Class Lyases;
Carbon-oxygen lyases;
Acting on polysaccharides
BRITE hierarchy
Sysname (1->4)-alpha-D-galacturonan lyase
Reaction(IUBMB) Eliminative cleavage of (1->4)-alpha-D-galacturonan to give
oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at
their non-reducing ends [RN:R08694]
Reaction(KEGG) R08694 > R02361 R06240(G)
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Comment Favours pectate, the anion, over pectin, the methyl ester (which is
the preferred substrate of EC 4.2.2.10, pectin lyase).
Pathway PATH: ec00040  Pentose and glucuronate interconversions
Orthology KO: K01728  pectate lyase
Genes ATH: AT1G30350 AT3G09540 AT3G24670 AT3G27400 AT3G55140 AT4G13710
     AT5G09280 AT5G55720
OSA: 4326883(Os01g0546800) 4335013(Os04g0137100)
MGR: MGG_04348
AFM: AFUA_1G01120 AFUA_2G00760 AFUA_7G06400 AFUA_8G05910
ANG: An10g00870(plyA)
YPE: YPO3994(pelY)
YPK: y3834
YPM: YP_3357(pelY)
YPA: YPA_3822
YPN: YPN_3644
YPG: YpAngola_A4065
YPS: YPTB3834(pelY)
YPI: YpsIP31758_4066
YPY: YPK_0096
YPB: YPTS_4050
YEN: YE4069(pelY)
ECA: ECA2135 ECA4067(pelA) ECA4068(pelB) ECA4069(pelC) ECA4070(pelZ)
PCT: PC1_2170 PC1_3860
PWA: Pecwa_2511
ENT: Ent638_0482
DDA: Dd703_0352 Dd703_0353 Dd703_2763 Dd703_2764
DZE: Dd1591_0270 Dd1591_0271 Dd1591_1090 Dd1591_1091
XCC: XCC0644(pel) XCC0645(pel) XCC2815(pelB)
XCB: XC_1298 XC_3590 XC_3591
XCA: xccb100_3710(pel2) xccb100_3711(pel3)
XCV: XCV2278 XCV2569 XCV3132(pel1) XCV3687(pel2)
XAC: XAC2373(pel) XAC2986(pelB) XAC3562(pel)
XOO: XOO0821(pel) XOO2265
XOM: XOO_0747
CJA: CJA_1277(pelC)
MMW: Mmwyl1_0132 Mmwyl1_2362
AAV: Aave_3434
SME: SM_b21239
SMD: Smed_6139
BSU: BSU07560(pel)
BHA: BH0698
BLI: BL03760(pel)
BLD: BLi01404(pel)
BCL: ABC0063(pelB) ABC1141
BAY: RBAM_007720(pel)
BPU: BPUM_3515(pelB)
LCI: LCK_00931(pel)
SCO: SCO1880(SCI39.27c)
TFU: Tfu_0153
RBA: RB3417 RB5312(pel) RB5316
TMA: TM0433
Taxonomy
Structures PDB: 1AIR  1BN8  1EE6  1GXM  1GXN  1GXO  1JRG  1JTA  1O88  1O8D  
     1O8E  1O8F  1O8G  1O8H  1O8I  1O8J  1O8K  1O8L  1O8M  1OOC  
     1PCL  1PE9  1PLU  1R76  1RU4  1VBL  2BSP  2EWE  2NZM  2O04  
     2O0V  2O0W  2O17  2O1D  2PEC  2QX3  2V8I  2V8J  2V8K  3B4N  
     3B8Y  3B90  
Reference
  Authors
  Title

  Journal
  Organism
1  [PMID:13860094]
ALBERSHEIM P, KILLIAS U.
Studies relating to the purification and properties of pectin
transeliminase.
Arch. Biochem. Biophys. 97 (1962) 107-15.
Pisum sativum
Reference
  Authors
  Title

  Journal
  Organism
2  [PMID:14235514]
EDSTROM RD, PHAFF HJ.
PURIFICATION AND CERTAIN PROPERTIES OF PECTIN TRANS-ELIMINASE FROM
ASPERGILLUS FONSECAEUS.
J. Biol. Chem. 239 (1964) 2403-8.
Aspergillus fonsecaeus
Reference
  Authors
  Title

  Journal
  Organism
3  [PMID:14235515]
EDSTROM RD, PHAFF HJ.
ELIMINATIVE CLEAVAGE OF PECTIN AND OF OLIGOGALACTURONIDE METHYL
ESTERS BY PECTIN TRANS-ELIMINASE.
J. Biol. Chem. 239 (1964) 2409-15.
Aspergillus fonsecaeus
Reference
  Authors
  Title

  Journal
  Organism
4  [PMID:13727438]
NAGEL CW, VAUGHN RH.
The degradation of oligogalacturonides by the polygalacturonase of
Bacillus polymyxa.
Arch. Biochem. Biophys. 94 (1961) 328-32.
Bacillus polymyxa
Reference
  Authors
  Title
  Journal
  Organism
5  [PMID:6035509]
Nasuno S, Starr MP.
Polygalacturonic acid trans-eliminase of Xanthomonas campestris.
Biochem. J. 104 (1967) 178-85.
Xanthomonas campestris
Reference
  Authors

  Title


  Journal
  Organism
6  [PMID:9195887]
Mayans O, Scott M, Connerton I, Gravesen T, Benen J, Visser J,
Pickersgill R, Jenkins J.
Two crystal structures of pectin lyase A from Aspergillus reveal a
pH driven conformational change and striking divergence in the
substrate-binding clefts of pectin and pectate lyases.
Structure. 5 (1997) 677-89.
Aspergillus niger [GN:ang]
Other DBs ExplorEnz - The Enzyme Database: 4.2.2.2
IUBMB Enzyme Nomenclature: 4.2.2.2
ExPASy - ENZYME nomenclature database: 4.2.2.2
BRENDA, the Enzyme Database: 4.2.2.2
CAS: 9015-75-2

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