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Literature summary extracted from

  • Chi, W.J.; Park, d.a..Y.; Seo, Y.B.; Chang, Y.K.; Lee, S.Y.; Hong, S.K.
    Cloning, expression, and biochemical characterization of a novel GH16 beta-agarase AgaG1 from Alteromonas sp. GNUM-1 (2014), Appl. Microbiol. Biotechnol., 98, 4545-4555.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.B1 expressed in Escherichia coli BL21 (DE3) pLysS cells Alteromonas sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.B1 Ca2+ complete inhibition at 5 mM Alteromonas sp.
3.2.1.B1 Mg2+ 78% residual activity at 1 and 5 mM Alteromonas sp.
3.2.1.B1 Mn2+ complete inhibition at 5 mM Alteromonas sp.
3.2.1.B1 additional information not inhibited by EDTA Alteromonas sp.
3.2.1.B1 Zn2+ % residual activity at 47 mM Alteromonas sp.

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.B1 extracellular
-
 Alteromonas sp.
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.B1 Co2+ 125% activity at 1 mM Alteromonas sp.
3.2.1.B1 additional information not influenced by K+ and Na+ Alteromonas sp.
3.2.1.B1 additional information the enzyme does not require metal ions for its activity Alteromonas sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.B1 58700
-
 x * 58700, calculated from amino acid sequence Alteromonas sp.
3.2.1.B1 59000
-
 gel filtration Alteromonas sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.B1 agarose + H2O Alteromonas sp.
-
 neoagarotetraose + neoagarohexaose + ? main products ?
3.2.1.B1 agarose + H2O Alteromonas sp. GNUM-1
-
 neoagarotetraose + neoagarohexaose + ? main products ?
3.2.1.B1 neoagarotetraose + H2O Alteromonas sp.
-
 neoagarobiose
-
 ?
3.2.1.B1 neoagarotetraose + H2O Alteromonas sp. GNUM-1
-
 neoagarobiose
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.B1 Alteromonas sp. U3PAU3 KCTC23886
-
3.2.1.B1 Alteromonas sp. GNUM-1 U3PAU3 KCTC23886
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.B1 glutathione Sepharose column chromatography, and gel filtration Alteromonas sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.B1 4-nitrophenyl beta-D-galactopyranoside + H2O
-
 Alteromonas sp. 4-nitrophenol + beta-D-galactopyranose
-
 ?
3.2.1.B1 4-nitrophenyl beta-D-galactopyranoside + H2O
-
 Alteromonas sp. GNUM-1 4-nitrophenol + beta-D-galactopyranose
-
 ?
3.2.1.B1 agarose + H2O
-
 Alteromonas sp. neoagarotetraose + neoagarohexaose + ? main products ?
3.2.1.B1 agarose + H2O
-
 Alteromonas sp. GNUM-1 neoagarotetraose + neoagarohexaose + ? main products ?
3.2.1.B1 additional information the enzyme does not hydrolyze 4-nitrophenyl alpha-D-galactopyranoside Alteromonas sp. ?
-
 ?
3.2.1.B1 additional information the enzyme does not hydrolyze 4-nitrophenyl alpha-D-galactopyranoside Alteromonas sp. GNUM-1 ?
-
 ?
3.2.1.B1 neoagarotetraose + H2O
-
 Alteromonas sp. neoagarobiose
-
 ?
3.2.1.B1 neoagarotetraose + H2O
-
 Alteromonas sp. GNUM-1 neoagarobiose
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.B1 ? x * 59000, SDS-PAGE Alteromonas sp.
3.2.1.B1 ? x * 58700, calculated from amino acid sequence Alteromonas sp.

Synonyms

EC Number Synonyms Comment Organism
3.2.1.B1 AgaG1
-
 Alteromonas sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.B1 40
-
-
 Alteromonas sp.

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.B1 25 55 the enzyme exhibits high activity at temperatures ranging between 25 and 45°C. The enzyme can sustain its enzymatic activity up to 90% of its peak activity at 45°C, while the relative activities rapidly decline to 20 and 3% at 50 and 55°C, respectively Alteromonas sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.B1 40 45 the enzyme is stable up to 40°C (100%), and retains more than 70% of its initial activity at 45°C after heat treatment for 30 min. The enzyme stability dramatically declines at 50°C to 19% Alteromonas sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.B1 7
-
-
 Alteromonas sp.

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.B1 6 9 the enzyme retains more than 42% of its activity at pH 8.0. The enzyme exhibits low activity at both acidic (pH 6.0) and basic (pH 9.0) conditions Alteromonas sp.