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Information on EC 3.2.1.158 - alpha-agarase and Organism(s) Thalassotalea agarivorans and UniProt Accession A1IGV8

for references in articles please use BRENDA:EC3.2.1.158
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EC Tree
IUBMB Comments
Requires Ca2+. The enzyme from Thalassomonas sp. can use agarose, agarohexaose and neoagarohexaose as substrate. The products of agarohexaose hydrolysis are dimers and tetramers, with agarotetraose being the predominant product, whereas hydrolysis of neoagarohexaose gives rise to two types of trimer. While the enzyme can also hydrolyse the highly sulfated agarose porphyran very efficiently, it cannot hydrolyse the related compounds kappa-carrageenan (see EC 3.2.1.83) and iota-carrageenan (see EC 3.2.1.157) . See also EC 3.2.1.81, beta-agarase.
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Thalassotalea agarivorans
UNIPROT: A1IGV8
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The taxonomic range for the selected organisms is: Thalassotalea agarivorans
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
alpha-agarase, agaa33, agarasea33, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
agarose 3-glycanohydrolase
Requires Ca2+. The enzyme from Thalassomonas sp. can use agarose, agarohexaose and neoagarohexaose as substrate. The products of agarohexaose hydrolysis are dimers and tetramers, with agarotetraose being the predominant product, whereas hydrolysis of neoagarohexaose gives rise to two types of trimer. While the enzyme can also hydrolyse the highly sulfated agarose porphyran very efficiently, it cannot hydrolyse the related compounds kappa-carrageenan (see EC 3.2.1.83) and iota-carrageenan (see EC 3.2.1.157) [2]. See also EC 3.2.1.81, beta-agarase.
CAS REGISTRY NUMBER
COMMENTARY hide
63952-00-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
agarose + H2O
agarotetraose + ?
show the reaction diagram
agarose + H2O
agarotetraose + agarobiose + agarohexaose
show the reaction diagram
-
agarotetraose is the main product
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
agarose + H2O
agarotetraose + ?
show the reaction diagram
-
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
0.1 U/mL alpha-agarase used for enzymatic cleavage of alpha-1,3 linkages in porphyran at a concentration of 2.0% in 50 mM Tris/HCl buffer for 3 h, specific activity of 44.7 U/mg comparable between recombinant protein and native enzyme purified from Thalassomonas sp.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
porphyran cleavage assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 9.5
recombinant protein
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
porphyran cleavage assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AAGAR_THASX
1463
0
158250
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
86780
deduced from amino acid sequence
87000
recombinant enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 11
native enzyme
705484
6.5 - 10.5
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
stable up to 40°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hydroxyapatite chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Bacillus subtilis
expressed in Escherichia coli HB101, open reading frame of 1463 amino acid residues of the agaA33 gene determined, for extracellular production of recombinant alpha-agarase AgaA33 the Bacillus subtilis strain ISW1214 serves as host and plasmid pEXBS as expression vector
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hatada, Y.; Ohta, Y.; Horikoshi, K.
Hyperproduction and application of alpha-agarase to enzymatic enhancement of antioxidant activity of porphyran
J. Agric. Food Chem.
54
9895-9900
2006
Thalassotalea agarivorans (A1IGV8), Thalassotalea agarivorans JAMB-A33 (A1IGV8)
Manually annotated by BRENDA team
Fu, X.T.; Kim, S.M.
Agarase: review of major sources, categories, purification method, enzyme characteristics and applications
Mar. drugs
8
200-218
2010
Alteromonas agarilytica (Q9LAP7), Alteromonas agarilytica GJ1B (Q9LAP7), Thalassotalea agarivorans (A1IGV8), Thalassotalea agarivorans JAMB-A33 (A1IGV8)
Manually annotated by BRENDA team