KEGG   ENZYME: 3.2.1.81Help
Entry
EC 3.2.1.81                 Enzyme                                 

Name
beta-agarase;
agarase (ambiguous);
AgaA;
AgaB;
endo-beta-agarase;
agarose 3-glycanohydrolase (incorrect)
Class
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
BRITE hierarchy
Sysname
agarose 4-glycanohydrolase
Reaction(IUBMB)
Hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, giving the tetramer as the predominant product
Comment
Also acts on porphyran, but more slowly [1]. This enzyme cleaves the beta-(1->4) linkages of agarose in a random manner with retention of the anomeric-bond configuration, producing beta-anomers that give rise progressively to alpha-anomers when mutarotation takes place [6]. The end products of hydrolysis are neoagarotetraose and neoagarohexaose in the case of AgaA from the marine bacterium Zobellia galactanivorans, and neoagarotetraose and neoagarobiose in the case of AgaB [6].
History
EC 3.2.1.81 created 1972, modified 2006
Orthology
K01219  
agarase
Genes
PAT: 
SDE: 
Sde_1175(aga16B) Sde_1176(aga50A) Sde_2644(aga50B) Sde_2650(aga86C) Sde_2655(aga86E)
GAG: 
RPB: 
RPD: 
RPE: 
SCO: 
SCO3471(dagA)
CAA: 
RBA: 
RB3421(agrA)
Taxonomy
Reference
1  [PMID:5386190]
  Authors
Duckworth M, Turvey JR.
  Title
The action of a bacterial agarase on agarose, porphyran and alkali-treated porphyran.
  Journal
Biochem. J. 113 (1969) 687-92.
  Organism
Cytophaga sp.
Reference
2  [PMID:12970344]
  Authors
Allouch J, Jam M, Helbert W, Barbeyron T, Kloareg B, Henrissat B, Czjzek M.
  Title
The three-dimensional structures of two beta-agarases.
  Journal
J. Biol. Chem. 278 (2003) 47171-80.
  Organism
Zobellia galactanivorans
  Sequence
Reference
3  [PMID:15170112]
  Authors
Ohta Y, Nogi Y, Miyazaki M, Li Z, Hatada Y, Ito S, Horikoshi K.
  Title
Enzymatic properties and nucleotide and amino acid sequences of a thermostable beta-agarase from the novel marine isolate, JAMB-A94.
  Journal
Biosci. Biotechnol. Biochem. 68 (2004) 1073-81.
  Organism
Microbulbifer salipaludis
Reference
4  [PMID:15088129]
  Authors
Ohta Y, Hatada Y, Nogi Y, Miyazaki M, Li Z, Akita M, Hidaka Y, Goda S, Ito S, Horikoshi K.
  Title
Enzymatic properties and nucleotide and amino acid sequences of a thermostable beta-agarase from a novel species of deep-sea Microbulbifer.
  Journal
Appl. Microbiol. Biotechnol. 64 (2004) 505-14.
  Organism
Microbulbifer elongataus, Microbulbifer salipaludis, Microbulbifer elongataus, Microbulbifer hydrolyticus
Reference
5  [PMID:8517750]
  Authors
Sugano Y, Terada I, Arita M, Noma M, Matsumoto T.
  Title
Purification and characterization of a new agarase from a marine bacterium, Vibrio sp. strain JT0107.
  Journal
Appl. Environ. Microbiol. 59 (1993) 1549-54.
  Organism
Undaria pinnatiJida, Laminaria sp., Vibrio sp.
Reference
6  [PMID:15456406]
  Authors
Jam M, Flament D, Allouch J, Potin P, Thion L, Kloareg B, Czjzek M, Helbert W, Michel G, Barbeyron T.
  Title
The endo-beta-agarases AgaA and AgaB from the marine bacterium Zobellia galactanivorans: two paralogue enzymes with different molecular organizations and catalytic behaviours.
  Journal
Biochem. J. 385 (2005) 703-13.
  Organism
Zobellia galactanivorans
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
37288-57-6

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