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Literature summary for 4.1.1.15 extracted from

  • Tong, J.C.; Mackay, I.R.; Chin, J.; Law, R.H.; Fayad, K.; Rowley, M.J.
    Enzymatic characterization of a recombinant isoform hybrid of glutamic acid decarboxylase (rGAD67/65) expressed in yeast (2002), J. Biotechnol., 97, 183-190.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
a hybrid cDNA is created by fusing a cDNA for amino acids 1-101 of GAD67 to a human cDNA for amino acids 96-585 of GAD65. The recombinant rGAD67/65 protein is expressed in yeast and has equivalent immunoreactivity to mammalian brain GAD with diabetes sera Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information a hybrid cDNA is created by fusing a cDNA for amino acids 1-101 of GAD67 to a human cDNA for amino acids 96-585 of GAD65. The recombinant rGAD67/65 protein is expressed in yeast and has equivalent immunoreactivity to mammalian brain GAD with diabetes sera. rGAD67/65 has enzymatic properties similar to that of the mixed isoforms of GAD preparations from mammalian brain Homo sapiens

General Stability

General Stability Organism
stability is optimal over 3 months, in lyophilized form at 20°C Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3
-
L-Glu
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.37
-
-
Homo sapiens

Storage Stability

Storage Stability Organism
-80°C, 3 months. rGAD67/65 is stable Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Glu
-
Homo sapiens 4-Aminobutanoate + CO2
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate efficient non-covalent binding to the cofactor Homo sapiens