KEGG   ENZYME: 4.2.2.26
Entry
EC 4.2.2.26                 Enzyme                                 
Name
oligo-alginate lyase;
aly (gene name) (ambiguous);
oalS17 (gene name);
oligoalginate lyase;
exo-oligoalginate lyase
Class
Lyases;
Carbon-oxygen lyases;
Acting on polysaccharides
Sysname
alginate oligosaccharide 4-deoxy-alpha-L-erythro-hex-4-enopyranuronate-(1->4)-hexananopyranuronate lyase
Reaction(IUBMB)
Cleavage of poly(4-deoxy-alpha-L-erythro-hexopyranuronoside) oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their non-reducing ends into 4-deoxy-alpha-L-erythro-hex-4-enopyranuronate monosaccharides.
Comment
The enzyme degrades unsaturated oligosaccharides produced by the action of alginate lyases (EC 4.2.2.3 and EC 4.2.2.11) on alginate, by repeatedly removing the unsaturated residue from the non-reducing end until only unsaturated monosaccharides are left. The enzyme catalyses a beta-elimination reaction, generating a new unsaturated non-reducing end after removal of the pre-existing one.
History
EC 4.2.2.26 created 2015
Orthology
K20525  oligo-alginate lyase
Genes
KGOCEW81_15485
KLUK7B04_14075
KCYRIN60_14365
SFOZ042_21520
RAHRahaq_2074
RACEJHW33_06460
RAQRahaq2_2212
RAAQ7S_10515
RVCJ9880_19105
RIUI2123_12390
EAMEGXP68_10025
XARXB05_00680
XHYFZ025_04470
XEUXSP_001205
XAGHEP73_03146
XASHEP74_02963
SMLSmlt2602
SMTSmal_2067
SRHBAY15_0476
SLMBIZ42_10915
STEMCLM74_16325
STESMG068_10895
SINCDAIF1_32030
SPAQSTNY_R22840
STEQICJ04_13255
SGENRKE57_11200
PSUWWQ53_03470
VAGN646_4459 N646_4460
VHRAL538_15535 AL538_15540
VOWA9237_02440 A9237_02445
VSPVS_1246 VS_1247
VEUIXK98_14685 IXK98_14690
VBRA6E01_15020 A6E01_15025
VAFD1115_05485 D1115_05490
VNLD3H41_17415 D3H41_17420
VCCFAZ90_06435 FAZ90_06440
VASGT360_15085 GT360_15090
VSLLTQ54_15605 LTQ54_15610
VPGLZI70_17695 LZI70_17700
VCRAIS519_00695 IS519_00700
VLEISX51_07850 ISX51_07855
VSYK08M4_12390 K08M4_12400
AWDAWOD_II_1150 AWOD_II_1151
PGBH744_1c1644 H744_1c1645
AVNAvin_46500
AVLAvCA_46500
AVDAvCA6_46500
ACXAchr_5040
SFRSfri_3104
SJASJ2017_1079
SLJEGC82_17620
SMAIEXU30_09955 EXU30_09960
SPOLFH971_04070
SINVK8B83_13145 K8B83_13150 K8B83_19175
COLWA3Q33_13235
COLADBO93_13855 DBO93_13910
COVEKO29_05460
CBERB5D82_13235 B5D82_13295
THTE2K93_04470
THAPFNC98_00220
PHAPSHAa1748(alyll)
PIAPI2015_1887
PBWD172_011660
PEAPESP_a2549
PARTPARC_a2609
PAGAPAGA_a1383
PCARPC2016_1119
PMAACPA52_10500
PDVFFU37_09495
AMACMASE_04140
AMBAMBAS45_04405
ALTambt_05125
AALEP13_15685
ASPAOR13_1043
ASQAVL57_13410
AAWAVL56_12520
ALEAV939_12325
ALZAV940_12085
SALMD0Y50_18865
GAGGlaag_3645
PMESFX988_03261
PATPatl_3651
CATEC2869_02775
AGZM0C34_09010 M0C34_09015
AGQLQZ07_11285 LQZ07_11290
CATTOLW01_17880
PMAWMACH26_09680
CEBB0D95_02120
SDESde_3284(alg17A)
SAGAM5M_10445
GILNHM04_04305
MTHDA3224_00425
MAGAMag101_00420
MBRGPVT68_15520
HALCEY643_05725
MMAIsS8_3472
GAIIMCC3135_30035
HAFC8233_00690 C8233_00695
CMAIBFX80_07160 BFX80_07165
MARSA8C75_02220 A8C75_02225
MRZKDW95_14115 KDW95_14120
CFHC1707_09410
BSBBresu_2896
BDMEQG53_08455
BNDKWG56_16500
MMRMmar10_0256
HBAHbal_2771
NREBES08_00050
NOVTQ38_023940
SPHKSKP52_04175
SPHPLH20_00370
STERAOA14_11265
SPHQBWQ93_09895
SPHXE5675_06715
SPHUSPPYR_0943
SKRBRX40_02300
SPHCCVN68_20060
SPAPH3Z74_06340
SARIH5J25_12810
SSUAFPZ54_03250
SCABLZK98_13080
SDONM9980_09000
SPHYCHN51_02465
SPHLLPB140_00300
PARPHFP51_00430
PHAOHF685_13560
AMXAM2010_1736
PMASNCF86_09620
ADOA6F68_01721
TFVIDJ81_07185
CNAAB433_04690
ERYCP97_03810
ERFFIU90_09070
TMKQGN29_05695
GYMGYMC10_3686
PSABPSAB_17950
PBJVN24_16145
POWIJ21_37920
PDHB9T62_12600
PVOPVOR_18484
PLWD5F53_11790
PCHIPC41400_19575
ASOCCB4_00526
CPYCphy_0489
CSHClosa_0105
VPYHZI73_21220
CSCCsac_2721
SALAESZ53_09770
PSEYGU243_13585
BCVBcav_3334 Bcav_3344
OBTOPIT5_15555 OPIT5_17440 OPIT5_18925 OPIT5_27565
AAGGETAA8_58750
PNDPla175_23860(hepC)
STQSpith_1748
SUSAcid_4041
IPOIlyop_2136
GBAJ421_1193
BOABovatus_00025 Bovatus_03848
BCELBcellWH2_03161 BcellWH2_04826
BISDXK01_006440 DXK01_008725
BUNBun01g_02180
BEGINE88_01839
BFCBacF7301_04405
BDOEL88_16420
BDHGV66_00670
PMUCING2E5A_0343
PSACPSM36_2063
TTZFHG85_04010
MBASALGA_3305
NKONiako_5223
NSONIASO_03465 NIASO_04790
NIAA8C56_19530
FGGFSB75_07860
PSEGD3H65_19220
PGOFSB84_21275
PHEPhep_0331
PEPAQ505_11715
PCMAY601_1649
PSTYBFS30_00305
PEJFYC62_00980
PGJQG516_25180
PSNPedsa_1196
MMABHQ865_17725
ESTDN752_00830 DN752_22945
SPIKEXU85_21470
SPIBG8759_17385
ALSDJ013_05545 DJ013_09505
RUPDTQ70_08520
FPFDCC35_17600
FLMMY04_2549
FLLEI427_11105
FYAKMW28_03450
FKAKM029_18335
CLITOQ292_34430
REKN6H18_03930
RCGN7E81_12945
PPSVPEPS_32150 PEPS_32240
GFOGFO_1151
FFAFFWV33_03540
FKIFK004_07155
FCRHYN56_19355
FNKE1750_01145
CATCA2559_11508
MARMYQ22_05100
MARTBTR34_05385
MAREEJ994_16720
CAOCelal_4221
CLYCelly_0295
CLHIX49_01145
CBALM667_17460
CBATM666_17460
COMNPBN93_01460
KDIKrodi_0315
DOKMED134_10670
DDOI597_0903
DODDCS32_10570
LANLacal_1748
LVNBWR22_11825
ZGAZOBELLIA_2624(alyA3) ZOBELLIA_3452
NDODDD_0330(alyll)
NULR1T42_07200
POMMED152_09820
POBLPB03_09610
PRNBW723_07355
POLABXQ17_10045
PHALH9I45_00595
PPECH9W90_14125
PUNNQP51_08945
SZEAW14_12520
AHZAPS56_06060 APS56_15085
TJETJEJU_2494(alyA3)
WFUAXE80_11225
FOPFNB79_00985
OLLCW732_00355
OAQDZC78_07845
FEKC1H87_08185
TAJC1A40_05220
KANIMCC3317_38130
MARFCJ739_3056
AQBD1818_06345
AQAD1815_01040
AQDD1816_00480
PSYNE9099_09530
PPONMUN68_012555
MGELG5B37_00450
ASAGFGM00_07275
FLGLV716_03090
MAQILDL77_02525
FBEFF125_19655
ALUTO5O44_07265
LUYQZH61_02195
EAOBD94_3097
EMNM876_12940
EENBBD30_10785
ELBVO54_03461
EGOBBD34_05300
EGMAYC65_01410
ELZFCS00_15310
CSALNBC122_01621
CHRCQGN23_13830
KFAQ73A0000_08505
OHOOweho_2211
RMRRmar_1166
RLOGQ464_011560
RBARAWN76_018385
MROMROS_1366
 » show all
Reference
1  [PMID:10913091]
  Authors
Hashimoto W, Miyake O, Momma K, Kawai S, Murata K
  Title
Molecular identification of oligoalginate lyase of Sphingomonas sp. strain A1 as  one of the enzymes required for complete depolymerization of alginate.
  Journal
J Bacteriol 182:4572-7 (2000)
DOI:10.1128/JB.182.16.4572-4577.2000
Reference
2  [PMID:22281843]
  Authors
Kim HT, Chung JH, Wang D, Lee J, Woo HC, Choi IG, Kim KH
  Title
Depolymerization of alginate into a monomeric sugar acid using Alg17C, an exo-oligoalginate lyase cloned from Saccharophagus degradans 2-40.
  Journal
Appl Microbiol Biotechnol 93:2233-9 (2012)
DOI:10.1007/s00253-012-3882-x
  Sequence
[sde:Sde_3284]
Reference
3  [PMID:24795372]
  Authors
Jagtap SS, Hehemann JH, Polz MF, Lee JK, Zhao H
  Title
Comparative biochemical characterization of three exolytic oligoalginate lyases from Vibrio splendidus reveals complementary substrate scope, temperature, and pH adaptations.
  Journal
Appl Environ Microbiol 80:4207-14 (2014)
DOI:10.1128/AEM.01285-14
Reference
4  [PMID:25335746]
  Authors
Wang L, Li S, Yu W, Gong Q
  Title
Cloning, overexpression and characterization of a new oligoalginate lyase from a  marine bacterium, Shewanella sp.
  Journal
Biotechnol Lett 37:665-71 (2015)
DOI:10.1007/s10529-014-1706-z
Other DBs
ExplorEnz - The Enzyme Database: 4.2.2.26
IUBMB Enzyme Nomenclature: 4.2.2.26
ExPASy - ENZYME nomenclature database: 4.2.2.26
BRENDA, the Enzyme Database: 4.2.2.26

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