Information on EC 3.2.1.158 - alpha-agarase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.2.1.158
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RECOMMENDED NAME
GeneOntology No.
alpha-agarase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of (1->3)-alpha-L-galactosidic linkages in agarose, yielding agarotetraose as the major product
show the reaction diagram
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain JAMB-A33
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Manually annotated by BRENDA team
strain JAMB-A33
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
agar + H2O
?
show the reaction diagram
agarohexaose + H2O
?
show the reaction diagram
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?
agarohexaose + H2O
agarotetraose + agarobiose
show the reaction diagram
agarose + H2O
agarotetraose
show the reaction diagram
agarose + H2O
agarotetraose + agarobiose + agarohexaose
show the reaction diagram
agarose + H2O
agarotetraose + agarohexaose
show the reaction diagram
neoagarohexaose + H2O
?
show the reaction diagram
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-
-
?
neoagarohexaose + H2O
agarotetraose
show the reaction diagram
porphyran + H2O
?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
agar + H2O
?
show the reaction diagram
agarose + H2O
agarotetraose
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40.7
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; pH 8.5, 45°C
6423
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pH 7.2, 42°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
porphyran cleavage assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
cultivation of Eschericha coli cells harbouring the agaA gene, agarose lysis observed after one week on Zd agar broth
40
porphyran cleavage assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75000
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x * 75000, SDS-PAGE
86780
deduced from amino acid sequence
87000
recombinant enzyme
154000
deduced from amino acid sequence of pre-protein of 1429 residues
180000
360000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
additional information
includes the peptides A and B, signal peptide of 26 residues, cleaved between A26 and E27
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 11
6.5 - 10.5
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+ stabilizes enzyme
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; isolated from the sediment of Noma point, Japan, at a depth of 230m, purified by DEAE-Toyopearl 650M column, ultracentrifugation and gel filtration
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hydroxyapatite chromatography and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
agaA gene isolated from a genomic library of Alteromonas agarilytica, alpha-agarase precursor of 1429 amino acid residues, expressed in Escherichia coli, novel catalytic domain defines a new GH family
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
expressed in Saccharomyces cerevisiae strains SEY2102 and FY833 and in Pichia pastoris strain GS115
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