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Literature summary for 3.2.1.B1 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)

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

Inhibitors

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

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Alteromonas sp.
-
-

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Alteromonas sp. U3PAU3 KCTC23886
-
Alteromonas sp. GNUM-1 U3PAU3 KCTC23886
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
AgaG1
-
Alteromonas sp.

Temperature Optimum [°C]

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

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
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]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
Alteromonas sp.

pH Range

pH Minimum pH Maximum Comment Organism
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.