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Literature summary for 3.2.1.98 extracted from

  • Tran, P.L.; Lee, J.S.; Park, K.H.
    Experimental evidence for a 9-binding subsite of Bacillus licheniformis thermostable alpha-amylase (2014), FEBS Lett., 588, 620-624.
    View publication on PubMed
Search for more literature for 3.2.1.98

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain MC1061 Bacillus licheniformis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.36
-
 maltononaose pH and temperature not specified in the publication Bacillus licheniformis

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis
-
-
-
Bacillus licheniformis ATCC 27811
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA resin column chromatography Bacillus licheniformis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
maltononaose + H2O preferred substrate Bacillus licheniformis maltohexaose + maltotriose major products ?
maltononaose + H2O preferred substrate Bacillus licheniformis ATCC 27811 maltohexaose + maltotriose major products ?

Synonyms

Synonyms Comment Organism
thermostable alpha-amylase
-
 Bacillus licheniformis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
12.86
-
 maltononaose pH and temperature not specified in the publication Bacillus licheniformis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
35.72
-
 maltononaose pH and temperature not specified in the publication Bacillus licheniformis