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Literature summary for 3.2.1.2 extracted from

  • Jeon, E.J.; Jung, J.H.; Seo, D.H.; Jung, D.H.; Holden, J.F.; Park, C.S.
    Bioinformatic and biochemical analysis of a novel maltose-forming alpha-amylase of the GH57 family in the hyperthermophilic archaeon Thermococcus sp. CL1 (2014), Enzyme Microb. Technol., 60, 9-15.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed the gene in Escherichia coli Thermococcus sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.25
-
maltotriose pH 5.0, 85°C Thermococcus sp.
16.2
-
maltopentaose pH 5.0, 85°C Thermococcus sp.
18.2
-
maltotetraose pH 5.0, 85°C Thermococcus sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
intracellular
-
Thermococcus sp. 5622
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
67120
-
-
Thermococcus sp.
70000
-
1 * 70000, SDS-PAGE Thermococcus sp.

Organism

Organism UniProt Comment Textmining
Thermococcus sp. I3ZTN9
-
-
Thermococcus sp. CL1 I3ZTN9
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amylopectin + H2O the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan Thermococcus sp. maltose + ?
-
?
amylopectin + H2O the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan Thermococcus sp. CL1 maltose + ?
-
?
glycogen + H2O the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan Thermococcus sp. maltose + ?
-
?
glycogen + H2O the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan Thermococcus sp. CL1 maltose + ?
-
?
maltopentaose + H2O the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible Thermococcus sp. 2 maltose + D-glucose
-
?
maltopentaose + H2O the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible Thermococcus sp. CL1 2 maltose + D-glucose
-
?
maltotetraose + H2O the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible Thermococcus sp. 2 maltose
-
?
maltotetraose + H2O the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible Thermococcus sp. CL1 2 maltose
-
?
maltotriose + H2O the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible Thermococcus sp. maltose + D-glucose
-
?
maltotriose + H2O the enzyme displays dual hydrolysis activity toward alpha-1,4- and alpha-1,6-glycosidic linkages, the catalytic efficiency of 6-O-maltosyl-beta-cyclodextrin is 16fold higher than that of maltotriose. Compared to the kcat/Km value toward maltotriose, the values for longer substrates such as maltotetraose and maltopentaose are negligible Thermococcus sp. CL1 maltose + D-glucose
-
?
soluble starch + H2O the enzyme only releases maltose from polymers such as soluble starch, amylopectin, and glycogen, while maltose is rarely detected from reaction with amylose and pullulan Thermococcus sp. maltose + ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 70000, SDS-PAGE Thermococcus sp.

Synonyms

Synonyms Comment Organism
TCMA
-
Thermococcus sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
85
-
alpha-1,4-glycosidic linkage hydrolysis Thermococcus sp.
98
-
alpha-1,6-glycosidic linkage hydrolysis Thermococcus sp.

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
60 95 60°C; about 50% of maximal activity, 60°C: about 60% of maximal activity, alpha-1,4-glycosidic linkage hydrolysis of maltotriose Thermococcus sp.
80 98 activity at 80°C is about 50% compared to the activity at 98°C, alpha-1,6-glycosidic linkage hydrolysis of 6-O-maltotetraosyl-beta-cyclodextrin Thermococcus sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
67
-
melting temperature at pH 4.0 Thermococcus sp.
85
-
the half-life is 69 min, 225 min, and 255 min at pH 5.0, pH 6.0, and pH 7.0 Thermococcus sp.
91
-
melting temperature at pH 5.0 Thermococcus sp.
105
-
melting temperature at pH 6.0 Thermococcus sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.85
-
maltopentaose pH 5.0, 85°C Thermococcus sp.
3.95
-
maltotetraose pH 5.0, 85°C Thermococcus sp.
11.45
-
maltotriose pH 5.0, 85°C Thermococcus sp.

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
alpha-1,4-glycosidic linkage hydrolysis Thermococcus sp.
6
-
alpha-1,6-glycosidic linkage hydrolysis Thermococcus sp.

pH Range

pH Minimum pH Maximum Comment Organism
4 6 pH 4.0: about 85% of maximal activity, pH 6.0: about 60% of maximal activity, alpha-1,4-glycosidic linkage hydrolysis of maltotriose Thermococcus sp.
4 8 pH 4.0: about 50% of maximal activity, pH 8.0: about 70% of maximal activity, alpha-1,6-glycosidic linkage hydrolysis of 6-O-maltotetraosyl-beta-cyclodextrin Thermococcus sp.

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.22
-
maltotetraose pH 5.0, 85°C Thermococcus sp.
0.24
-
maltopentaose pH 5.0, 85°C Thermococcus sp.
2.7
-
maltotriose pH 5.0, 85°C Thermococcus sp.