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Literature summary for 3.2.1.B1 extracted from

  • Ma, C.; Lu, X.; Shi, C.; Li, J.; Gu, Y.; Ma, Y.; Chu, Y.; Han, F.; Gong, Q.; Yu, W.
    Molecular cloning and characterization of a novel beta-agarase, AgaB, from marine Pseudoalteromonas sp. CY24 (2007), J. Biol. Chem., 282, 3747-3754.
    View publication on PubMed
Search for more literature for 3.2.1.B1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pseudoalteromonas sp.

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ slight inhibition Pseudoalteromonas sp.
EDTA slight inhibition Pseudoalteromonas sp.
Hg2+ complete inhibition Pseudoalteromonas sp.
Mn2+ slight inhibition Pseudoalteromonas sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
8.36
-
 neoagarotetradecaose 25°C, pH 6.0 Pseudoalteromonas sp.
12.4
-
 neoagarododecaose 25°C, pH 6.0 Pseudoalteromonas sp.
12.8
-
 neoagarodecaose 25°C, pH 6.0 Pseudoalteromonas sp.

Metals/Ions

Metals/Ions Comment Organism Structure
Ba2+ slight activation Pseudoalteromonas sp.
Ca2+ slight activation Pseudoalteromonas sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
47200
-
 x * 47200, calculated, x * 50400, SDS-PAGE Pseudoalteromonas sp.
50400
-
 x * 47200, calculated, x * 50400, SDS-PAGE Pseudoalteromonas sp.

Organism

Organism UniProt Comment Textmining
Pseudoalteromonas sp. A1A3Y9
-
-

Reaction

Reaction Comment Organism Reaction ID
hydrolysis of 1,3-beta-D-galactosidic linkages in agarose, giving the octamer as the predominant product enzyme has a large substrate binding cleft that accomodates 12 sugar units, with 8 sugar units toward the reducing end spanning subsites +1 to +8 and 4 sugar units toward the non-reducing end spanning subsites -4 to -1. Enzyme hydrolyzes the glycosidic bond with inversion of anomeric configuration Pseudoalteromonas sp.
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
agarose + H2O
-
 Pseudoalteromonas sp. neoagarooctaose + neoagarodecaose main end products, plus small amounts of neoagarotetraose and neoagarohexaose ?
additional information enzyme has a large substrate binding cleft that accomodates 12 sugar units, with 8 sugar units toward the reducing end spanning subsites +1 to +8 and 4 sugar units toward the non-reducing end spanning subsites -4 to -1. No substrates are kappa-carrageenan, iota-carrageenan, lambda-carrageenan, alginate, and chitosan and oligosaccharides with a degree of polymerization below 10 Pseudoalteromonas sp. ?
-
 ?
neoagarodecaose + H2O
-
 Pseudoalteromonas sp. ?
-
 ?
neoagarododecaose + H2O
-
 Pseudoalteromonas sp. ?
-
 ?
neoagarotetradecaose + H2O
-
 Pseudoalteromonas sp. ?
-
 ?

Subunits

Subunits Comment Organism
? x * 47200, calculated, x * 50400, SDS-PAGE Pseudoalteromonas sp.

Synonyms

Synonyms Comment Organism
AgaB
-
 Pseudoalteromonas sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
 Pseudoalteromonas sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
35
-
 stable up to Pseudoalteromonas sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.19
-
 neoagarodecaose 25°C, pH 6.0 Pseudoalteromonas sp.
3.3
-
 neoagarotetradecaose 25°C, pH 6.0 Pseudoalteromonas sp.
4.77
-
 neoagarododecaose 25°C, pH 6.0 Pseudoalteromonas sp.
5.16
-
 neoagarotetradecaose 25°C, pH 6.0 Pseudoalteromonas sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Pseudoalteromonas sp.

pH Range

pH Minimum pH Maximum Comment Organism
5.7 10.6 more than 95% of maximum acitivity Pseudoalteromonas sp.

pI Value

Organism Comment pI Value Maximum pI Value
Pseudoalteromonas sp. calculated
-
 4.8