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Literature summary for 2.4.1.19 extracted from

  • Kelly, R.M.; Leemhuis, H.; Gaetjen, L.; Dijkhuizen, L.
    Evolution toward small molecule inhibitor resistance affects native enzyme function and stability, generating acarbose-insensitive cyclodextrin glucanotransferase variants (2008), J. Biol. Chem., 283, 10727-10734.
    View publication on PubMed
Search for more literature for 2.4.1.19

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Bacillus subtilis strain DB104A Niallia circulans

Protein Variants

Protein Variants Comment Organism
A230V the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme Niallia circulans
F283L the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme Niallia circulans
H140Q the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme Niallia circulans
K232E the mutation confers increased resistance to inhibition by acarbose, the mutant shows highly increased IC50 compared to the wild-type enzyme Niallia circulans
additional information error-prone PCR mutagenesis for searching the sequence space of CGTase for acarbose-insensitive variants, overview Niallia circulans

Inhibitors

Inhibitors Comment Organism Structure
acarbose the acceptor substrate binding site near the active site of the enzyme is involved in inhibition by acarbose, mutants K232E, F283L, and A230V show increased resistance, overview Niallia circulans

Organism

Organism UniProt Comment Textmining
Niallia circulans P30920
-
-
Niallia circulans 251 P30920
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information beta-cyclodextrin-forming activity from partially hydrolyzed potato starch with an average degree of polymerization of 50. Disproportionation activity is determined using 4-nitrophenyl-beta-D-maltoheptaoside-4-6-O-ethylidene, i.e. pNPG7, as substrate Niallia circulans ?
-
 ?
additional information beta-cyclodextrin-forming activity from partially hydrolyzed potato starch with an average degree of polymerization of 50. Disproportionation activity is determined using 4-nitrophenyl-beta-D-maltoheptaoside-4-6-O-ethylidene, i.e. pNPG7, as substrate Niallia circulans 251 ?
-
 ?
starch
-
 Niallia circulans beta-cyclodextrin + gamma-cyclodextrin
-
 ?
starch
-
 Niallia circulans 251 beta-cyclodextrin + gamma-cyclodextrin
-
 ?

Synonyms

Synonyms Comment Organism
CGTase
-
 Niallia circulans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 assay at Niallia circulans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
9
-
 starch pH 6.0, 60°C, beta-cyclization activity, mutant A230V Niallia circulans
26
-
 starch pH 6.0, 60°C, beta-cyclization activity, mutant K232E Niallia circulans
35
-
 starch pH 6.0, 60°C, beta-cyclization activity, mutant F283L Niallia circulans
48
-
 starch pH 6.0, 60°C, beta-cyclization activity, mutant A230V/H140Q Niallia circulans
79
-
 starch pH 6.0, 60°C, beta-cyclization activity, mutant H140Q Niallia circulans
329
-
 starch pH 6.0, 60°C, beta-cyclization activity, wild-type enzyme Niallia circulans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 assay at Niallia circulans

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0011
-
 pH 6.0, 60°C, wild-type enzyme Niallia circulans acarbose
1.807
-
 pH 6.0, 60°C, mutant H140Q Niallia circulans acarbose
1.845
-
 pH 6.0, 60°C, mutant A230V/H140Q Niallia circulans acarbose
3.93
-
 pH 6.0, 60°C, mutant K232E Niallia circulans acarbose
4.197
-
 pH 6.0, 60°C, mutant F283L Niallia circulans acarbose
7.37
-
 pH 6.0, 60°C, mutant A230V Niallia circulans acarbose