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Literature summary for 3.2.1.B36 extracted from

  • Jung, J.H.; Seo, D.H.; Holden, J.F.; Park, C.S.
    Maltose-forming alpha-amylase from the hyperthermophilic archaeon Pyrococcus sp. ST04 (2014), Appl. Microbiol. Biotechnol., 98, 2121-2131.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Pyrococcus sp.

Inhibitors

Inhibitors Comment Organism Structure
Cd2+
-
Pyrococcus sp.
Cu2+
-
Pyrococcus sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.3
-
6-O-maltotetraosyl-beta-cyclodextrin pH 5.0, 90°C Pyrococcus sp.
8.4
-
maltotriose pH 5.0, 90°C Pyrococcus sp.
18.8
-
maltotetraose pH 5.0, 90°C Pyrococcus sp.
21.2
-
maltopentaose pH 5.0, 90°C Pyrococcus sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
4 * 70000, SDS-PAGE Pyrococcus sp.
260000
-
gel filtration Pyrococcus sp.

Organism

Organism UniProt Comment Textmining
Pyrococcus sp. I3RE04
-
-
Pyrococcus sp. ST04 I3RE04
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pyrococcus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl alpha-D-maltohexaoside + H2O at an early stage of the reaction only maltose and 4-nitrophenol alpha-D-maltotetraoside, but not maltotetraose are observed. Even as the reaction proceeded, maltotetraose does not appear at all Pyrococcus sp. 4-nitrophenyl alpha-D-maltotetraoside + maltose
-
?
6-O-maltosyl-beta-cyclodextrin + H2O
-
Pyrococcus sp. maltose + beta-cyclodextrin
-
?
6-O-maltotetraosyl-beta-cyclodextrin + H2O no formation of matotetraose Pyrococcus sp. 2 maltose + beta-cyclodextrin
-
?
maltopentaose + H2O
-
Pyrococcus sp. 2 maltose + D-glucose
-
?
maltotetraose + H2O
-
Pyrococcus sp. 2 maltose
-
?
maltotriose + H2O
-
Pyrococcus sp. maltose + D-glucose
-
?
additional information exo-type maltose-forming alpha-amylase acting on the non-reducing end of the substrates and requires at least a maltose unit at its working sites of substrates. When the length of the branch is longer than G2 in the substrate, the enzyme primarily attacks alpha-1,4-glycosidic linkages in the long branch and cleaves off maltose unit until it reaches the final G2, and then it performs a debranching reaction by acting on alpha-1,6-glycosidic bonds at branching points. 6-O-glucosyl-beta-cyclodextrin and beta-cyclodextrin are resistant to hydrolysis Pyrococcus sp. ?
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 70000, SDS-PAGE Pyrococcus sp.

Synonyms

Synonyms Comment Organism
PSMA
-
Pyrococcus sp.
Py04_0872 locus name Pyrococcus sp.

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
90
-
assay at Pyrococcus sp.
90 95
-
Pyrococcus sp.

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
70
-
about 55% of maximal activity Pyrococcus sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
75
-
half-life: 254 min Pyrococcus sp.
85
-
half-life: 72 min Pyrococcus sp.

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0017
-
maltopentaose pH 5.0, 90°C Pyrococcus sp.
0.0033
-
maltotetraose pH 5.0, 90°C Pyrococcus sp.
6.35
-
maltotriose pH 5.0, 90°C Pyrococcus sp.
25.75
-
6-O-maltotetraosyl-beta-cyclodextrin pH 5.0, 90°C Pyrococcus sp.

pH Optimum

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

pH Range

pH Minimum pH Maximum Comment Organism
4 6 pH 4.0: less than 10% of maximal activity, pH 6.0: about 40% of maximal activity Pyrococcus sp.

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.000078
-
maltopentaose pH 5.0, 90°C Pyrococcus sp.
0.00018
-
maltotetraose pH 5.0, 90°C Pyrococcus sp.
0.76
-
maltotriose pH 5.0, 90°C Pyrococcus sp.
85.8
-
6-O-maltotetraosyl-beta-cyclodextrin pH 5.0, 90°C Pyrococcus sp.