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

BRENDA support

Literature summary extracted from

  • Kelly, R.M.; Dijkhuizen, L.; Leemhuis, H.
    The evolution of cyclodextrin glucanotransferase product specificity (2009), Appl. Microbiol. Biotechnol., 84, 119-133.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.19 phylogenetic analysis Klebsiella pneumoniae
2.4.1.19 phylogenetic analysis Thermoanaerobacter sp.
2.4.1.19 phylogenetic analysis Bacillus sp. (in: Bacteria)
2.4.1.19 phylogenetic analysis, expression in Bacillus subtilis strain DB104A Thermoanaerobacterium thermosulfurigenes
2.4.1.19 phylogenetic analysis, expression in Bacillus subtilis strain NA-1 Geobacillus stearothermophilus
2.4.1.19 phylogenetic analysis, expression in Escherichia coli strain BL21(DE3) Thermococcus sp.
2.4.1.19 phylogenetic analysis, expression in Escherichia coli strain BL21(DE3) Anaerobranca gottschalkii
2.4.1.19 phylogenetic analysis, expression of the enzyme from strain BC8 in Escherichia coli strain JM103, and of the enzyme from strain BC251 in Bacillus subtilis strain DB104A Niallia circulans

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.19 additional information
-
 additional information reaction kinetics Klebsiella pneumoniae
2.4.1.19 additional information
-
 additional information reaction kinetics Niallia circulans
2.4.1.19 additional information
-
 additional information reaction kinetics Thermoanaerobacterium thermosulfurigenes
2.4.1.19 additional information
-
 additional information reaction kinetics Thermococcus sp.
2.4.1.19 additional information
-
 additional information reaction kinetics Thermoanaerobacter sp.
2.4.1.19 additional information
-
 additional information reaction kinetics Geobacillus stearothermophilus
2.4.1.19 additional information
-
 additional information reaction kinetics Anaerobranca gottschalkii
2.4.1.19 additional information
-
 additional information reaction kinetics Bacillus sp. (in: Bacteria)

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.19 Ca2+ raise the unfolding temperature of CGTase Niallia circulans
2.4.1.19 Ca2+ raise the unfolding temperature of CGTase Thermoanaerobacterium thermosulfurigenes
2.4.1.19 Ca2+ raise the unfolding temperature of CGTase Bacillus sp. (in: Bacteria)

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.19 additional information Klebsiella pneumoniae CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview ?
-
 ?
2.4.1.19 additional information Niallia circulans CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview ?
-
 ?
2.4.1.19 additional information Thermoanaerobacterium thermosulfurigenes CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview ?
-
 ?
2.4.1.19 additional information Thermococcus sp. CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview ?
-
 ?
2.4.1.19 additional information Thermoanaerobacter sp. CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview ?
-
 ?
2.4.1.19 additional information Geobacillus stearothermophilus CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview ?
-
 ?
2.4.1.19 additional information Anaerobranca gottschalkii CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview ?
-
 ?
2.4.1.19 additional information Bacillus sp. (in: Bacteria) CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview ?
-
 ?
2.4.1.19 additional information Thermococcus sp. B1001 CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview ?
-
 ?
2.4.1.19 additional information Geobacillus stearothermophilus NO2 CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview ?
-
 ?
2.4.1.19 additional information Thermoanaerobacterium thermosulfurigenes EM1 CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview ?
-
 ?
2.4.1.19 additional information Klebsiella pneumoniae M5a1 CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.19 Anaerobranca gottschalkii
-
-
-
2.4.1.19 Bacillus sp. (in: Bacteria) P05618 alkalophilic, strain A2-5a
-
2.4.1.19 Geobacillus stearothermophilus P31797
-
-
2.4.1.19 Geobacillus stearothermophilus NO2 P31797
-
-
2.4.1.19 Klebsiella pneumoniae
-
-
-
2.4.1.19 Klebsiella pneumoniae M5a1
-
-
-
2.4.1.19 Niallia circulans
-
 strains BC8 and BC251
-
2.4.1.19 Thermoanaerobacter sp.
-
 strain ATCC 53627
-
2.4.1.19 Thermoanaerobacterium thermosulfurigenes
-
-
-
2.4.1.19 Thermoanaerobacterium thermosulfurigenes EM1
-
-
-
2.4.1.19 Thermococcus sp.
-
-
-
2.4.1.19 Thermococcus sp. B1001
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.19 recombinant enzyme from Escherichia coli strain BL21(DE3) inclusion bodies Thermococcus sp.

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.4.1.19 recombinant CGTase from inclusion bodies by solubilization in 6 M urea, refolded by dialysis and heated to 80°C for 20 min Thermococcus sp.

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.19 commercial preparation
-
 Klebsiella pneumoniae
-
2.4.1.19 commercial preparation
-
 Bacillus sp. (in: Bacteria)
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.19 0.5
-
 beta-cyclization Klebsiella pneumoniae
2.4.1.19 23
-
 beta-cyclization Thermococcus sp.
2.4.1.19 28
-
 beta-cyclization Anaerobranca gottschalkii
2.4.1.19 52
-
 beta-cyclization by strain BC8 enzyme Niallia circulans
2.4.1.19 94
-
 beta-cyclization, commercial preparation Bacillus sp. (in: Bacteria)
2.4.1.19 127
-
 beta-cyclization Thermoanaerobacter sp.
2.4.1.19 255
-
 beta-cyclization Thermoanaerobacterium thermosulfurigenes
2.4.1.19 255
-
 beta-cyclization Geobacillus stearothermophilus
2.4.1.19 265
-
 beta-cyclization by strain BC251 enzyme Niallia circulans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.19 additional information CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview Klebsiella pneumoniae ?
-
 ?
2.4.1.19 additional information CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview Niallia circulans ?
-
 ?
2.4.1.19 additional information CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview Thermoanaerobacterium thermosulfurigenes ?
-
 ?
2.4.1.19 additional information CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview Thermococcus sp. ?
-
 ?
2.4.1.19 additional information CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview Thermoanaerobacter sp. ?
-
 ?
2.4.1.19 additional information CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview Geobacillus stearothermophilus ?
-
 ?
2.4.1.19 additional information CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview Anaerobranca gottschalkii ?
-
 ?
2.4.1.19 additional information CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview Bacillus sp. (in: Bacteria) ?
-
 ?
2.4.1.19 additional information reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview Klebsiella pneumoniae ?
-
 ?
2.4.1.19 additional information reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview Bacillus sp. (in: Bacteria) ?
-
 ?
2.4.1.19 additional information reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows high also shows hydrolytic activity on potato starch Thermoanaerobacter sp. ?
-
 ?
2.4.1.19 additional information reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows high hydrolytic activity on potato starch Thermoanaerobacterium thermosulfurigenes ?
-
 ?
2.4.1.19 additional information reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows hydrolytic activity on potato starch Thermococcus sp. ?
-
 ?
2.4.1.19 additional information reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows hydrolytic activity on potato starch Geobacillus stearothermophilus ?
-
 ?
2.4.1.19 additional information reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows hydrolytic activity on potato starch Anaerobranca gottschalkii ?
-
 ?
2.4.1.19 additional information reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme from strain BC251 also shows hydrolytic activity on potato starch. Substrate binding structure of the strain BC251 enzyme, overview Niallia circulans ?
-
 ?
2.4.1.19 additional information CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview Thermococcus sp. B1001 ?
-
 ?
2.4.1.19 additional information reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows hydrolytic activity on potato starch Thermococcus sp. B1001 ?
-
 ?
2.4.1.19 additional information CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview Geobacillus stearothermophilus NO2 ?
-
 ?
2.4.1.19 additional information reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows hydrolytic activity on potato starch Geobacillus stearothermophilus NO2 ?
-
 ?
2.4.1.19 additional information CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview Thermoanaerobacterium thermosulfurigenes EM1 ?
-
 ?
2.4.1.19 additional information reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview. The enzyme also shows high hydrolytic activity on potato starch Thermoanaerobacterium thermosulfurigenes EM1 ?
-
 ?
2.4.1.19 additional information CGTases produce a mixture of cyclodextrins from starch consisting of 6 alpha, 7 beta, or 8 gamma glucose units, specificity, overview Klebsiella pneumoniae M5a1 ?
-
 ?
2.4.1.19 additional information reaction mechanism, a linear glucan chain binds to the substrate binding subsites of CGTase followed by bond cleavage to yield a covalent glycosyl-enzyme intermediate. The nature of the acceptor molecule in the second step of the reaction, to which the covalently bound oligosaccharide is transferred, determines the enzyme reaction specificity, schematic overview Klebsiella pneumoniae M5a1 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.19 CGTase
-
 Klebsiella pneumoniae
2.4.1.19 CGTase
-
 Niallia circulans
2.4.1.19 CGTase
-
 Thermoanaerobacterium thermosulfurigenes
2.4.1.19 CGTase
-
 Thermococcus sp.
2.4.1.19 CGTase
-
 Thermoanaerobacter sp.
2.4.1.19 CGTase
-
 Geobacillus stearothermophilus
2.4.1.19 CGTase
-
 Anaerobranca gottschalkii
2.4.1.19 CGTase
-
 Bacillus sp. (in: Bacteria)
2.4.1.19 cyclodextrin glucanotransferase
-
 Klebsiella pneumoniae
2.4.1.19 cyclodextrin glucanotransferase
-
 Niallia circulans
2.4.1.19 cyclodextrin glucanotransferase
-
 Thermoanaerobacterium thermosulfurigenes
2.4.1.19 cyclodextrin glucanotransferase
-
 Thermococcus sp.
2.4.1.19 cyclodextrin glucanotransferase
-
 Thermoanaerobacter sp.
2.4.1.19 cyclodextrin glucanotransferase
-
 Geobacillus stearothermophilus
2.4.1.19 cyclodextrin glucanotransferase
-
 Anaerobranca gottschalkii
2.4.1.19 cyclodextrin glucanotransferase
-
 Bacillus sp. (in: Bacteria)

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.19 30
-
-
 Klebsiella pneumoniae
2.4.1.19 30
-
-
 Thermococcus sp.
2.4.1.19 30
-
 assay at Anaerobranca gottschalkii
2.4.1.19 30
-
 assay at Bacillus sp. (in: Bacteria)
2.4.1.19 30
-
 strain BC8 enzyme Niallia circulans
2.4.1.19 50
-
 strain BC251 enzyme Niallia circulans
2.4.1.19 60
-
-
 Thermoanaerobacterium thermosulfurigenes
2.4.1.19 60
-
-
 Thermoanaerobacter sp.
2.4.1.19 65
-
-
 Geobacillus stearothermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.19 5.5
-
-
 Thermococcus sp.
2.4.1.19 5.5
-
 assay at Bacillus sp. (in: Bacteria)
2.4.1.19 6
-
-
 Thermoanaerobacterium thermosulfurigenes
2.4.1.19 6
-
-
 Thermoanaerobacter sp.
2.4.1.19 6
-
-
 Geobacillus stearothermophilus
2.4.1.19 6
-
 strain BC251 enzyme Niallia circulans
2.4.1.19 6.8
-
-
 Klebsiella pneumoniae
2.4.1.19 6.8
-
 strain BC8 enzyme Niallia circulans
2.4.1.19 8.5
-
 assay at Anaerobranca gottschalkii