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Literature summary for 3.2.1.54 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
Search for more literature for 3.2.1.54

Application

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

Cloned(Commentary)

Cloned (Comment) Organism
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

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

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
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
-
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)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl-alpha-D-maltohexaoside + H2O
-
 Thermococcus sp. 4-nitrophenol + maltohexaose
-
 ?
4-nitrophenyl-alpha-D-maltohexaoside + H2O
-
 Thermococcus sp. CL1 4-nitrophenol + maltohexaose
-
 ?
6-O-alpha-D-glucosyl-alpha-cyclodextrin + H2O branched cyclodextrin Thermococcus sp. isomaltooligosaccharides
-
 ?
6-O-alpha-D-glucosyl-beta-cyclodextrin + H2O branched cyclodextrin Thermococcus sp. isomaltooligosaccharides
-
 ?
6-O-alpha-D-maltosyl-beta-cyclodextrin + H2O branched cyclodextrin Thermococcus sp. isomaltooligosaccharides
-
 ?
acarbose + H2O
-
 Thermococcus sp. D-glucose + maltose + ?
-
 ?
alpha-cyclodextrin + H2O
-
 Thermococcus sp. isomaltooligosaccharides
-
 ?
alpha-cyclodextrin + H2O
-
 Thermococcus sp. isomaltooligosaccharides mainly D-glucose and maltose ?
alpha-cyclodextrin + H2O
-
 Thermococcus sp. CL1 isomaltooligosaccharides
-
 ?
alpha-cyclodextrin + H2O
-
 Thermococcus sp. CL1 isomaltooligosaccharides mainly D-glucose and maltose ?
maltotriose + H2O
-
 Thermococcus sp. maltose + D-glucose
-
 ?
maltotriose + H2O
-
 Thermococcus sp. CL1 maltose + D-glucose
-
 ?
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. ?
-
 ?
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

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

Synonyms

Synonyms Comment Organism
CDase
-
 Thermococcus sp.

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
 Thermococcus sp.

pH Range

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

General Information

General Information Comment Organism
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.