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Literature summary for 3.2.1.81 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

Cloned(Commentary)

Cloned (Comment) Organism
ligated into pBluescript II KS(+), and transferred into Escherichia coli DH5alpha, forming a genomic DNA library. Cloned into the pET-24a(+) vector and transformed into Escherichia coli BL21 (DE3) competent cells Pseudoalteromonas sp. CY24

Inhibitors

Inhibitors Comment Organism Structure
Cu2+ slightly inhibits Pseudoalteromonas sp. CY24
EDTA slightly inhibits Pseudoalteromonas sp. CY24
Hg2+ completely inhibits Pseudoalteromonas sp. CY24
Mn2+ slightly inhibits Pseudoalteromonas sp. CY24

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
8.36
-
neoagarotetradecaose
-
Pseudoalteromonas sp. CY24
12.39
-
neoagarododecaose
-
Pseudoalteromonas sp. CY24
12.81
-
neoagarodecaose
-
Pseudoalteromonas sp. CY24

Metals/Ions

Metals/Ions Comment Organism Structure
Ba2+ slightly increases activity Pseudoalteromonas sp. CY24
Ca2+ slightly increases activity Pseudoalteromonas sp. CY24

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50400
-
1 * 50400, SDS-PAGE Pseudoalteromonas sp. CY24
50900
-
sequence analysis Pseudoalteromonas sp. CY24

Organism

Organism UniProt Comment Textmining
Pseudoalteromonas sp. CY24 A1A3Y9
-
-

Purification (Commentary)

Purification (Comment) Organism
476fold and with a final yield of 21.2%, by ammonium sulfate precipitation, weak anion-exchange chromatography, hydrophobic interaction chromatography, and gel filtration Pseudoalteromonas sp. CY24

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5000
-
recombinant AgaB 476fold purified Pseudoalteromonas sp. CY24

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
agarose + H2O
-
Pseudoalteromonas sp. CY24 neoagarooctaose + neoagarodecaose
-
?
additional information the agarase AgaB appears to have a large substrate binding cleft that accommodates 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, and enzymatic cleavage taking place between subsites -1 and +1. The enzyme hydrolyzes the glycosidic bond with inversion of anomeric configuration. AgaB does not hydrolyze neoagarooctaose, kappa-carrageenan, lota-carrageenan, lambda-carrageenan, alginate, and chitosan Pseudoalteromonas sp. CY24 ?
-
?
neoagarodecaose + H2O is a very poor substrate Pseudoalteromonas sp. CY24 ?
-
?
neoagarododecaose + H2O
-
Pseudoalteromonas sp. CY24 ?
-
?
neoagarotetradecaose + H2O
-
Pseudoalteromonas sp. CY24 ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 50400, SDS-PAGE Pseudoalteromonas sp. CY24

Synonyms

Synonyms Comment Organism
AgaB
-
Pseudoalteromonas sp. CY24
beta-agarase
-
Pseudoalteromonas sp. CY24

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
Pseudoalteromonas sp. CY24

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
35
-
retains more than 90% activity until 35°C Pseudoalteromonas sp. CY24

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.19
-
neoagarodecaose
-
Pseudoalteromonas sp. CY24
4.77
-
neoagarododecaose
-
Pseudoalteromonas sp. CY24
5.16
-
neoagarotetradecaose
-
Pseudoalteromonas sp. CY24

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
Pseudoalteromonas sp. CY24

pH Stability

pH Stability pH Stability Maximum Comment Organism
5.7 10.6 retains more than 95% activity Pseudoalteromonas sp. CY24