Literature summary for 3.2.1.54 extracted from

Nakagawa, Y.; Saburi, W.; Takada, M.; Hatada, Y.; Horikoshi, K.
Gene cloning and enzymatic characteristics of a novel gamma-cyclodextrin-specific cyclodextrinase from alkalophilic Bacillus clarkii 7364 (2008), Biochim. Biophys. Acta, 1784, 2004-2011.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli BL21 (DE3)	Evansella clarkii

General Stability

General Stability	Organism
more than 90% of the enzyme activity remains in the pH range of 8.0-10.0 and at 4°C in the absence of CaCl2 after pH and temperature treatments, respectively. Cda is efficiently stabilized by CaCl2. In the presence of CaCl2. Cda is stable in the pH range of 7.0-10.5 and at temperatures below 30°C.	Evansella clarkii

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.008	-	gamma-cyclodextrin	-	Evansella clarkii
0.067	-	maltooctaose	-	Evansella clarkii

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
77800	-	calculated	Evansella clarkii
979000	-	gel filtration chromatography	Evansella clarkii

Organism

Organism	UniProt	Comment	Textmining
Evansella clarkii	B9A1J7	7364	-
Evansella clarkii 7364	B9A1J7	7364	-

Purification (Commentary)

Purification (Comment)	Organism
Ni-chelating chromatography	Evansella clarkii

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	Cda rapidly hydrolyzes only gamma-cyclodextrinase, whereas it slowly hydrolyzes alpha- and beta-cyclodextrinase, maltooctaose, amylose, amylopectin and soluble starch. The hydrolysis activities toward these substrates are less than 4% of that toward gamma-cyclodextrinase. Pullulan and glycogen are hardly hydrolyzed. Cda is a CDase that has high specificity for only gamma-cyclodextrinase	Evansella clarkii

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
gamma-cyclodextrin + H2O	cyclodextrinase rapidly hydrolyzes only gamma-cyclodextrinase, whereas it slowly hydrolyzes alpha- and beta-cyclodextrinase, maltooctaose, amylose, amylopectin and soluble starch. The hydrolysis activities toward these substrates are less than 4% of that toward gamma-cyclodextrinase. Pullulan and glycogen are hardly hydrolyzed. Cyclodextrinase is a CDase that has high specificity for only gamma-cyclodextrinase	Evansella clarkii	maltooctaose + ?	-	?
gamma-cyclodextrin + H2O	cyclodextrinase rapidly hydrolyzes only gamma-cyclodextrinase, whereas it slowly hydrolyzes alpha- and beta-cyclodextrinase, maltooctaose, amylose, amylopectin and soluble starch. The hydrolysis activities toward these substrates are less than 4% of that toward gamma-cyclodextrinase. Pullulan and glycogen are hardly hydrolyzed. Cyclodextrinase is a CDase that has high specificity for only gamma-cyclodextrinase	Evansella clarkii 7364	maltooctaose + ?	-	?
maltooctaose + H2O	-	Evansella clarkii	maltohexaose + maltose	small amounts of maltotriose, maltotetraose and maltopentaose are also observed	?
maltooctaose + H2O	-	Evansella clarkii 7364	maltohexaose + maltose	small amounts of maltotriose, maltotetraose and maltopentaose are also observed	?

Subunits

Subunits	Comment	Organism
dodecamer	12 * 77800	Evansella clarkii

Synonyms

Synonyms	Comment	Organism
CDA	-	Evansella clarkii
CDase	-	Evansella clarkii
cyclodextrinase	-	Evansella clarkii

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	-	Evansella clarkii

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.03	-	maltooctaose	-	Evansella clarkii
3100	-	gamma-cyclodextrin	-	Evansella clarkii

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8.5	-	-	Evansella clarkii

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Release 2023.1 (January 2023)