KEGG   ENZYME: 3.2.1.82
Entry
EC 3.2.1.82                 Enzyme                                 
Name
exo-poly-alpha-digalacturonosidase;
pehX (gene name);
poly(1,4-alpha-D-galactosiduronate) digalacturonohydrolase;
exopolygalacturonosidase (misleading);
poly[(1->4)-alpha-D-galactosiduronate] digalacturonohydrolase;
exo-poly-alpha-galacturonosidase
Class
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
Sysname
poly[(1->4)-alpha-D-galactosiduronate] non-reducing-end-digalacturonohydrolase
Reaction(IUBMB)
[(1->4)-alpha-D-galacturonosyl]n + H2O = alpha-D-galacturonosyl-(1->4)-D-galacturonate + [(1->4)-alpha-D-galacturonosyl]n-2 [RN:R02360 R06239]
Reaction(KEGG)
R02360 R06239(G)
Substrate
[(1->4)-alpha-D-galacturonosyl]n [CPD:C00470];
H2O [CPD:C00001]
Product
alpha-D-galacturonosyl-(1->4)-D-galacturonate [CPD:C02273];
[(1->4)-alpha-D-galacturonosyl]n-2
Comment
The enzyme, characterized from bacteria, hydrolyses the second alpha-1,4-glycosidic bond from the non-reducing end of polygalacturonate, releasing digalacturonate.
History
EC 3.2.1.82 created 1972, modified 2019
Orthology
K18650  exo-poly-alpha-galacturonosidase
Genes
KOXKOX_13235
KOEA225_1464
KOYJ415_24315
KOMHR38_11985
KOKKONIH1_07185
KOCAB185_28860
KLLBJF97_07630
KGRJJJ10_20875
KPASLUW96_14020
KLCK7H21_20890
KLMBWI76_07155
KIENCTC12125_00461(pehX_1)
KASKATP_14600(pehX)
KLUK7B04_21690
KCYRIN60_07560
SYMK6K13_14425
YENYE0164(pehX)
YEPYE105_C0167
YEYY11_33621
YELLC20_08995
YEWCH47_3321(pehX)
YETCH48_1856(pehX)
YEFFORC2_3934
YEEYE5303_41081(pehX)
YSIBF17_08810
YINCH53_1967(pehX)
YROCH64_2753(pehX)
YAKACZ76_10035
YMADA391_22030
YHID5F51_00875
YCAF0T03_00845
YMOHRD69_04365
YASN0H69_21105
YEGPL78_07565
SFGAV650_16660
SFOZ042_11045 Z042_19390
PRODPCO85_21680
SERASer39006_003785
SERQCWC46_03785
ECAECA3111(pehX)
PATREV46_15395
PATOGZ59_31190(pehX)
PCTPC1_2862
PCCPCC21_029350
PCVBCS7_14740
PWAPecwa_1410
PPARA8F97_11825
PECW5S_1293
PWSA7983_01380
PPOABJK05_09555
PBRAB5S52_07160
PARII2D83_07120
PAQUDMB82_0007000
PVZOA04_31120(pehX)
PPAVLOZ86_14440
PQUIG609_006165
PPOOLW347_14610
PCACOI450_06250
PACBM9782_16940
DDDDda3937_00261(pehX) Dda3937_00262(pehW) Dda3937_00263(pehV)
DZEDd1591_0152 Dd1591_0153
DDCDd586_3904
DZCW909_19025
DSOA4U42_07660 A4U42_07670 A4U42_07675
CEDLH89_13825
DFNCVE23_21045
DDQDDI_4012 DDI_4013
DAQDAQ1742_04251(pehX)
DICDpoa569_000250
DLCO1Q98_12795
DDADd703_0200
BGJAWC36_19995
BRBEH207_12225
BNGEH206_01265
BIZHC231_01250
LBQCKQ53_04220
LPOPI6N93_00885
PPFPput_1884
PPBPPUBIRD1_1854
PPIYSA_08947
PPXT1E_2073(pehX)
PPUTL483_21750
PFVPsefu_3160
PFSPFLU_2286(pehX)
PTVAA957_24405
PMUDNCTC8068_02353(pehX)
PSESPSCI_0280
PPSHG5J76_17945
PXAKSS93_18540
PTZHU718_011220
PASGKSS96_12180
PTAENCTC10697_02681(pehX)
PGFJ0G10_11745
PKMPZ739_14175
PTAIICN73_23245
PKKQQ992_18090
GSNYC6258_03209
RSORSc1756(pehB)
RSEF504_1633
RPUCDC45_09050
RNCGO999_08415
RSCRCFBP_11765(pehB)
RSLRPSI07_0327(pehB)
RSNRSPO_c01791(pehB)
RSMCMR15_11765(pehB)
RSYRSUY_19490(pehX)
RSGJK151_03080
NNVQNH39_20875
PMSKNP414_02001
PMQPM3016_2299
PMWB2K_11610
PBDPBOR_08815
PAEAR70723_08115
PAEER70331_08155
PKBB4V02_22345
NTRB0W44_12550
LHBD1010_14310
EGAAL523_00840
EIEENLAB_09950
CACCA_C3684
CAESMB_G3725(pehX)
CAYCEA_G3691
CLJCLJU_c29360
CSRCspa_c52840
CSBCLSA_c18950(pehX)
CAHCAETHG_0930
CRWCROST_001180(pehX_1) CROST_001190(pehX_2) CROST_002390(pehX_3)
CFBCLFE_000630(pehX_1) CLFE_001810(pehX_2) CLFE_001820(pehX_3) CLFE_040580
CAUNCLAUR_021790 CLAUR_027690(pehX_1) CLAUR_028900(pehX_2) CLAUR_028910(pehX_3)
CGELpsyc5s11_19170(pehX)
BPBbpr_I2854(pgl28B)
BHUbhn_I2679
SRISELR_01400
PUFUFO1_0808
PFTJBW_03716
LXLKDY119_03537(pehX)
ARZAUT26_18105
ARXARZXY2_4273
PUEFV140_19810
PNVJMY29_18500
PRVG7070_02070
ACTQOG417_33020
BLEMBL8807_11500
BEUBE0216_11810
BNKKIM372_05040
FGGFSB75_10870
FLNFLA_0076
LACSH4075_11225
MMABHQ865_23305
SBXCA265_05770
 » show all
Reference
1  [PMID:5661621]
  Authors
Hasegawa S, Nagel CW.
  Title
Isolation of an oligogalacturonate hydrolase from a Bacillus specie.
  Journal
Arch Biochem Biophys 124:513-20 (1968)
DOI:10.1016/0003-9861(68)90360-3
Reference
2
  Authors
Hatanaka, C. and Ozawa, J.
  Title
Enzymic degradation of pectic acid. XIII. New exopolygalacturonase producing digalacturonic acid from pectic acid.
  Journal
J Agric Chem Soc Jpn 43:764-772 (1968)
Reference
3
  Authors
Hatanaka, C. and Ozawa, J.
  Title
Ber des O'Hara Inst 15:47 (1971)
Reference
4  [PMID:2168372]
  Authors
He SY, Collmer A
  Title
Molecular cloning, nucleotide sequence, and marker exchange mutagenesis of the exo-poly-alpha-D-galacturonosidase-encoding pehX gene of Erwinia chrysanthemi EC16.
  Journal
J Bacteriol 172:4988-95 (1990)
DOI:10.1128/JB.172.9.4988-4995.1990
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 3.2.1.82
IUBMB Enzyme Nomenclature: 3.2.1.82
ExPASy - ENZYME nomenclature database: 3.2.1.82
BRENDA, the Enzyme Database: 3.2.1.82
CAS: 37288-58-7

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