Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Lee, J.E.; Kim, I.H.; Jung, J.H.; Seo, D.H.; Kang, S.G.; Holden, J.F.; Cha, J.; Park, C.S.
    Molecular cloning and enzymatic characterization of cyclomaltodextrinase from hyperthermophilic archaeon Thermococcus sp. CL1 (2013), J. Microbiol. Biotechnol., 23, 1060-1069.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.2.1.54 food industry the extremely thermostable enzyme might be of potential value in the production of isomaltooligosaccharides in the food industry Thermococcus sp.

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.54 gene CL1_0884, DNA and amino acid sequence determination and analysis, sequence comparisons and genetic structure, phylogenetic analysis, expression of His6-tagged enzyme in Escherichia coli strain BL21-CodonPlus(DE3)-RP Thermococcus sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.54 Al3+ 82% inhibition at 5 mM Thermococcus sp.
3.2.1.54 Ba2+ 50% inhibition at 5 mM Thermococcus sp.
3.2.1.54 Ca2+ inhibits slightly at 5 mM Thermococcus sp.
3.2.1.54 Cd2+ 97% inhibition at 5 mM Thermococcus sp.
3.2.1.54 Co2+ 29% inhibition at 5 mM Thermococcus sp.
3.2.1.54 Cu2+ complete inhibition at 5 mM Thermococcus sp.
3.2.1.54 DMSO 61%inhibition at 10% Thermococcus sp.
3.2.1.54 ethanol complete inhibition at 10% Thermococcus sp.
3.2.1.54 Fe2+ complete inhibition at 5 mM Thermococcus sp.
3.2.1.54 Fe3+ complete inhibition at 5 mM Thermococcus sp.
3.2.1.54 methanol 99% inhibition at 10% Thermococcus sp.
3.2.1.54 Mg2+ 21% inhibition at 5 mM Thermococcus sp.
3.2.1.54 Ni2+ 61% inhibition at 5 mM Thermococcus sp.
3.2.1.54 Zn2+ complete inhibition at 5 mM Thermococcus sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.54 K+ activates lsightly at 5 mM Thermococcus sp.
3.2.1.54 Na+ activates lsightly at 5 mM Thermococcus sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.54 65000
-
 about, gel filtration Thermococcus sp.
3.2.1.54 75956
-
 1 * 65000, recombinant His6-tagged enzyme, SDS-PAGE and gel filtration, 1 * 75956, sequence calculation Thermococcus sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.54 alpha-cyclodextrin + H2O Thermococcus sp.
-
 isomaltooligosaccharides
-
 ?
3.2.1.54 alpha-cyclodextrin + H2O Thermococcus sp. CL1
-
 isomaltooligosaccharides
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.54 Thermococcus sp. I3ZTQ5 isolated from a Paralvinella sp. polychaete worm collected from an active deep-sea hydrothermal vent sulfide chimney, gene CL1_0884 or tccd
-
3.2.1.54 Thermococcus sp. CL1 I3ZTQ5 isolated from a Paralvinella sp. polychaete worm collected from an active deep-sea hydrothermal vent sulfide chimney, gene CL1_0884 or tccd
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.54 recombinant His6-tagged enzyme from Escherichia coli strain BL21-CodonPlus(DE3)-RP by nickel affinity chromatography and dialysis Thermococcus sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.54 4-nitrophenyl-alpha-D-maltohexaoside + H2O
-
 Thermococcus sp. 4-nitrophenol + maltohexaose
-
 ?
3.2.1.54 4-nitrophenyl-alpha-D-maltohexaoside + H2O
-
 Thermococcus sp. CL1 4-nitrophenol + maltohexaose
-
 ?
3.2.1.54 6-O-alpha-D-glucosyl-alpha-cyclodextrin + H2O branched cyclodextrin Thermococcus sp. isomaltooligosaccharides
-
 ?
3.2.1.54 6-O-alpha-D-glucosyl-beta-cyclodextrin + H2O branched cyclodextrin Thermococcus sp. isomaltooligosaccharides
-
 ?
3.2.1.54 6-O-alpha-D-maltosyl-beta-cyclodextrin + H2O branched cyclodextrin Thermococcus sp. isomaltooligosaccharides
-
 ?
3.2.1.54 acarbose + H2O
-
 Thermococcus sp. D-glucose + maltose + ?
-
 ?
3.2.1.54 alpha-cyclodextrin + H2O
-
 Thermococcus sp. isomaltooligosaccharides
-
 ?
3.2.1.54 alpha-cyclodextrin + H2O
-
 Thermococcus sp. isomaltooligosaccharides mainly D-glucose and maltose ?
3.2.1.54 alpha-cyclodextrin + H2O
-
 Thermococcus sp. CL1 isomaltooligosaccharides
-
 ?
3.2.1.54 alpha-cyclodextrin + H2O
-
 Thermococcus sp. CL1 isomaltooligosaccharides mainly D-glucose and maltose ?
3.2.1.54 maltotriose + H2O
-
 Thermococcus sp. maltose + D-glucose
-
 ?
3.2.1.54 maltotriose + H2O
-
 Thermococcus sp. CL1 maltose + D-glucose
-
 ?
3.2.1.54 additional information substrate specificity, overview. The enzyme preferentially hydrolyzes alpha-cyclodextrin, and at the initial stage catalyzes a ring-opening reaction by cleaving one alpha-1,4-glycosidic linkage of the cyclodextrin ring to produce the corresponding single maltooligosaccharide. A long substrate is preferred over smaller substrates. The enzyme can hydrolyze branched cyclodextrins to yield significant amounts of isomaltooligosaccharides (panose and 6-alpha-maltosylmaltose) in addition to glucose and maltose. No activity with pullulan and maltose, poor activity with soluble starch, amylopactin, and amylose, product analysis by thin layer chromatography, overview Thermococcus sp. ?
-
 ?
3.2.1.54 additional information substrate specificity, overview. The enzyme preferentially hydrolyzes alpha-cyclodextrin, and at the initial stage catalyzes a ring-opening reaction by cleaving one alpha-1,4-glycosidic linkage of the cyclodextrin ring to produce the corresponding single maltooligosaccharide. A long substrate is preferred over smaller substrates. The enzyme can hydrolyze branched cyclodextrins to yield significant amounts of isomaltooligosaccharides (panose and 6-alpha-maltosylmaltose) in addition to glucose and maltose. No activity with pullulan and maltose, poor activity with soluble starch, amylopactin, and amylose, product analysis by thin layer chromatography, overview Thermococcus sp. CL1 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.54 monomer 1 * 65000, recombinant His6-tagged enzyme, SDS-PAGE and gel filtration, 1 * 75956, sequence calculation Thermococcus sp.

Synonyms

EC Number Synonyms Comment Organism
3.2.1.54 CDase
-
 Thermococcus sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.54 85
-
-
 Thermococcus sp.

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.54 50 95 activity range, profile overview Thermococcus sp.

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.54 93
-
 purified enzyme, melting temperature, differential scanning calorimetry and differential scanning fluorimetry analysis Thermococcus sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.54 5
-
-
 Thermococcus sp.

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.54 4.5 7.5 activity range, profile overview Thermococcus sp.

General Information

EC Number General Information Comment Organism
3.2.1.54 evolution cyclomaltodextrinase is a member of the glycoside hydrolase family 13, GH13. The N-terminal extra domain of these enzymes is known to be composed of all of the substrate-binding components in a monomeric unit, which is generally provided by the dimeric N-domain position in bacterial enzymes Thermococcus sp.