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Literature summary for 2.4.1.18 extracted from

  • Kuriki, T.; Stewart, D.C.; Preiss, J.
    Construction of chimeric enzymes out of maize endosperm branching enzymes I and II: activity and properties (1997), J. Biol. Chem., 272, 28999-29004.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli, chimeric enzymes consisting of part mBE I and mBE II Zea mays

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.059
-
amylose amylose AS-320, pH 7.0, 30°C, enzyme forms BE I and BE II Zea mays
0.083
-
amylose amylose AS-320, pH 7.0, 30°C, chimeric enzyme form BE II-I BspHI Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Purification (Commentary)

Purification (Comment) Organism
chimeric enzymes expressed in E. coli Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
endosperm
-
Zea mays
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
amylose
-
Zea mays amylose containing alpha-1,6-glucosidic linkages
-
?
additional information the catalytic center is exclusively located in the central position of the enzyme Zea mays ?
-
?