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Literature summary for 2.4.1.18 extracted from

  • Libessart, N.; Preiss, J.
    Arginine residue 384 at the catalytic center is important for branching enzyme II from maize endosperm (1998), Arch. Biochem. Biophys., 360, 135-141.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
wild-type and mutant enzymes R384A, R384S, R384Q, E384E and R384K Zea mays

Protein Variants

Protein Variants Comment Organism
R384A mutation causes almost complete inactivation Zea mays
R384E mutation causes almost complete inactivation Zea mays
R384K residual activity of the mutant enzyme is 5% of the wild-type enzyme Zea mays
R384Q mutation causes almost complete inactivation Zea mays
R384S mutation causes almost complete inactivation Zea mays

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0068
-
amylose pH 7.5, 30°C, reduced amylose AS-320, wild-type enzyme Zea mays
0.0113
-
amylose pH 7.5, 30°C, reduced amylose AS-320, mutant enzyme R384K Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzymes R384A, R384S, R384Q, E384E and R384K 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 conserved Arg residue 384 plays an important role in the catalytic function but may not be directly involved in substrate binding Zea mays ?
-
?