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Literature summary extracted from

  • Inatomi, K.; Slaughter, J.C.
    Glutamate decarboxylase from barley embryos and roots (1975), Biochem. J., 147, 479-484.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.15 2-mercaptoethanol enzyme form I and II from embryos Hordeum vulgare
4.1.1.15 Cys enzyme from embryos Hordeum vulgare
4.1.1.15 dithiothreitol enzyme from embryos Hordeum vulgare
4.1.1.15 reduced glutathione enzyme from embryos Hordeum vulgare

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.15 22
-
L-Glu
-
Hordeum vulgare

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.15 120000
-
enzyme form II from embryo, sucrose density gradient centrifugation Hordeum vulgare
4.1.1.15 256000
-
enzyme form I from embryo, sucrose density gradient centrifugation Hordeum vulgare
4.1.1.15 310000
-
root enzyme Hordeum vulgare

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.15 Hordeum vulgare
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.1.1.15 embryo 2 enzyme form: I and II Hordeum vulgare
-
4.1.1.15 root 1 enzyme form Hordeum vulgare
-

Storage Stability

EC Number Storage Stability Organism
4.1.1.15 0°C, slight decrease in activity after 2 days Hordeum vulgare

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.15 L-Glu
-
Hordeum vulgare 4-Aminobutanoate + CO2
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.15 pyridoxal 5'-phosphate activates up to 3.5times Hordeum vulgare