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Information on EC 3.2.1.158 - alpha-agarase and Organism(s) Alteromonas agarilytica and UniProt Accession Q9LAP7

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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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Alteromonas agarilytica
UNIPROT: Q9LAP7
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Word Map
The taxonomic range for the selected organisms is: Alteromonas agarilytica
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 + ?
show the reaction diagram
-
-
-
-
?
agarose + H2O
agarotetraose + agarohexaose
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
no substrate: neoagarobiose, neoagarotetraose
-
-
?
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
-
-
-
?
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
6423
-
pH 7.2, 42°C
additional information
degradation of agarose observed after cultivation of transformed Escherichia coli cells harbouring the agaA gene of Alteromonas agarilytica on Zd agar broth at 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3
-
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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_ALTAG
1429
0
154671
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
154000
deduced from amino acid sequence of pre-protein of 1429 residues
180000
2 * 180000, SDS-PAGE
360000
gel filtration
180000
-
2 * 180000, SDS-PAGE
360000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
2 * 180000, SDS-PAGE
dimer
-
2 * 180000, SDS-PAGE
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
6.5
stable at pH values greater 6.5
705484
6.5
-
prolonged treatment below, inactivation
664808
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
stable up to 45°C
45
-
inactivation above
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Young, K.S.; Bhattacharjee, S.S.; Yaphe, W.
Enzymic cleavage of the alpha-linkages in agarose, to yield agaro-oligosaccharides
Carbohydr. Res.
66
207-212
1978
Alteromonas agarilytica, Alteromonas agarilytica GJ1B
-
Manually annotated by BRENDA team
Potin, P.; Richard, C.; Rochas, C.; Kloareg, B.
Purification and characterization of the alpha-agarase from Alteromonas agarlyticus (Cataldi) comb. nov., strain GJ1B
Eur. J. Biochem.
214
599-607
1993
Alteromonas agarilytica, Alteromonas agarilytica GJ1B
Manually annotated by BRENDA team
Flament, D.; Barbeyron, T.; Jam, M.; Potin, P.; Czjzek, M.; Kloareg, B.; Michel, G.
Alpha-agarases define a new family of glycoside hydrolases, distinct from beta-agarase families
Appl. Environ. Microbiol.
73
4691-4694
2007
Alteromonas agarilytica (Q9LAP7)
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