KEGG   ENZYME: 3.2.1.81
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
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  beta-agarase
Genes
VASGT360_06905
SJASJ2017_2075
PBWD172_008050
PAGAPAGA_a1786
ASPAOR13_1359
ASQAVL57_11855
AAWAVL56_11045
ALEAV939_10915
ALZAV940_10685
GAGGlaag_1821 Glaag_2339
CATEC2869_02075 C2869_07230
CEKD0B88_11585 D0B88_11590
CEGD0C16_02330 D0C16_02335 D0C16_02385
SDESde_1175(aga16B)
SAGAM5M_16890
MTHDA3224_10290 A3224_13515
MAGAMag101_05925
SCOSCO3471(dagA)
CAACaka_0054 Caka_0364 Caka_0553
VBSEGM51_00030
PHMPSMK_13810 PSMK_31770
BUNBun01g_38580(dagA_1)
ESTDN752_04920
FLMMY04_5423 MY04_5483
FLLEI427_25440
FYAKMW28_21570
FKAKM029_21095
RCGN7E81_10840 N7E81_17460
FFAFFWV33_00015 FFWV33_00795
MARMYQ22_01755
CAOCelal_2463 Celal_3665 Celal_3979
CLYCelly_0445 Celly_2860
CLHIX49_01925
CBALM667_09675 M667_09860
CBATM666_09600 M666_09850
COMNPBN93_02100 PBN93_02245 PBN93_14305
ZGAZOBELLIA_3573(agaB) ZOBELLIA_4203(agaA) ZOBELLIA_4243(agaD)
ZLAQ5W13_00285
PRNBW723_05770 BW723_07545
TJETJEJU_1794(agaQ) TJEJU_2943(agaZ)
WFUAXE80_09700
TAJC1A40_08665 C1A40_12485 C1A40_12565
AQAD1815_13830
AQDD1816_23605
AQENBT05_08985
 » show all
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 113:687-92 (1969)
DOI:10.1042/bj1130687
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 278:47171-80 (2003)
DOI:10.1074/jbc.M308313200
  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 68:1073-81 (2004)
DOI:10.1271/bbb.68.1073
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 64:505-14 (2004)
DOI:10.1007/s00253-004-1573-y
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 59:1549-54 (1993)
DOI:10.1128/AEM.59.5.1549-1554.1993
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 385:703-13 (2005)
DOI:10.1042/BJ20041044
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 3.2.1.81
IUBMB Enzyme Nomenclature: 3.2.1.81
ExPASy - ENZYME nomenclature database: 3.2.1.81
BRENDA, the Enzyme Database: 3.2.1.81
CAS: 37288-57-6

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