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Literature summary 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)

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

Protein Variants

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.18 0.0068
-
 amylose pH 7.5, 30°C, reduced amylose AS-320, wild-type enzyme Zea mays
2.4.1.18 0.0113
-
 amylose pH 7.5, 30°C, reduced amylose AS-320, mutant enzyme R384K Zea mays

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.18 Zea mays
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.18 wild-type and mutant enzymes R384A, R384S, R384Q, E384E and R384K Zea mays

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.18 endosperm
-
 Zea mays
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.18 amylose
-
 Zea mays amylose containing alpha-1,6-glucosidic linkages
-
 ?
2.4.1.18 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 ?
-
 ?