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Literature summary for 3.2.1.162 extracted from

  • Li, J.; Hu, Q.; Seswita-Zilda, D.
    Purification and characterization of a thermostable delta-carrageenase from a hot spring bacterium, Bacillus sp (2014), Biotechnol. Lett., 36, 1669-1674.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Cd2+
-
Bacillus sp. (in: Bacteria)
Cu2+
-
Bacillus sp. (in: Bacteria)
EDTA
-
Bacillus sp. (in: Bacteria)
Fe2+
-
Bacillus sp. (in: Bacteria)
Mg2+
-
Bacillus sp. (in: Bacteria)
Mn2+
-
Bacillus sp. (in: Bacteria)
Sr2+
-
Bacillus sp. (in: Bacteria)

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Bacillus sp. (in: Bacteria)
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates Bacillus sp. (in: Bacteria)
Co2+ activates Bacillus sp. (in: Bacteria)
K+ activates Bacillus sp. (in: Bacteria)
Na+ activates Bacillus sp. (in: Bacteria)

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37000
-
x * 37000, SDS-PAGE Bacillus sp. (in: Bacteria)

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
delta-carrageenan + H2O Bacillus sp. (in: Bacteria) Cga-L50 is an endo-type delta-carrageenase that hydrolyzes beta-1,4-linkages of kappa-carrageenan, yielding neo-delta-carrabiose as the main product neo-delta-carrabiose + ?
-
?
delta-carrageenan + H2O Bacillus sp. (in: Bacteria) Lc50-1 Cga-L50 is an endo-type delta-carrageenase that hydrolyzes beta-1,4-linkages of kappa-carrageenan, yielding neo-delta-carrabiose as the main product neo-delta-carrabiose + ?
-
?

Organism

Organism UniProt Comment Textmining
Bacillus sp. (in: Bacteria)
-
a thermophilic strain isolated from a hot spring in Indonesia
-
Bacillus sp. (in: Bacteria) Lc50-1
-
a thermophilic strain isolated from a hot spring in Indonesia
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 37.8fold from culture supernatant, by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration Bacillus sp. (in: Bacteria)

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
105.9
-
purified native enzyme, pH 7.5, 75°C Bacillus sp. (in: Bacteria)

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
delta-carrageenan + H2O Cga-L50 is an endo-type delta-carrageenase that hydrolyzes beta-1,4-linkages of kappa-carrageenan, yielding neo-delta-carrabiose as the main product Bacillus sp. (in: Bacteria) neo-delta-carrabiose + ?
-
?
delta-carrageenan + H2O Cga-L50 is an endo-type delta-carrageenase that hydrolyzes beta-1,4-linkages of kappa-carrageenan, yielding neo-delta-carrabiose as the main product Bacillus sp. (in: Bacteria) Lc50-1 neo-delta-carrabiose + ?
-
?

Subunits

Subunits Comment Organism
? x * 37000, SDS-PAGE Bacillus sp. (in: Bacteria)

Synonyms

Synonyms Comment Organism
Cga-L50
-
Bacillus sp. (in: Bacteria)
delta-carrageenase
-
Bacillus sp. (in: Bacteria)
endo-type delta-carrageenase
-
Bacillus sp. (in: Bacteria)

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
75
-
-
Bacillus sp. (in: Bacteria)

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
85
-
purified native enzyme, 10 min, over 50% activity remaining Bacillus sp. (in: Bacteria)

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
Bacillus sp. (in: Bacteria)

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 9 purified native enzyme, stable at Bacillus sp. (in: Bacteria)