KEGG   ENZYME: 4.2.2.26Help
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
BRITE hierarchy
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
KGO: CEW81_15485
SFO: Z042_21520
RAH: Rahaq_2074
RAQ: Rahaq2_2212
RAA: Q7S_10515
SML: Smlt2602
SMT: Smal_2067
SRH: BAY15_0476
SLM: BIZ42_10915
STEM: CLM74_16325
PSUW: WQ53_03470
VSP: VS_1247
ACX: Achr_5040
SFR: Sfri_3104
PHA: PSHAa1748(alyll)
PAT: Patl_3651
PART: PARC_a2609
AMAC: MASE_04140
SDE: Sde_3284(alg17A)
SAGA: M5M_10445
HBA: Hbal_2771
SPHP: LH20_00370
SPHU: SPPYR_0943
GBA: J421_1193
MBAS: ALGA_3305
RMR: Rmar_1166
FLM: MY04_2549
GFO: GFO_1151
MARM: YQ22_05100
CBAL: M667_17460
CBAT: M666_17460
DDO: I597_0903
ZGA: ZOBELLIA_2624(alyA3)
NDO: DDD_0330(alyll)
TJE: TJEJU_2494(alyA3)
MARF: CJ739_3056
MRO: MROS_1366
 » show all
Taxonomy
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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