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Literature summary for 4.1.1.15 extracted from

  • Fenalti, G.; Law, R.H.; Buckle, A.M.; Langendorf, C.; Tuck, K.; Rosado, C.J.; Faux, N.G.; Mahmood, K.; Hampe, C.S.; Banga, J.P.; Wilce, M.; Schmidberger, J.; Rossjohn, J.; El-Kabbani, O.; Pike, R.N.; Smith, A.I.; Mackay, I.R.; Rowley, M.J.; Whisstock, J.C.
    GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop (2007), Nat. Struct. Mol. Biol., 14, 280-286.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Sacchaormyces cerevisiae, His-tag Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
N-terminally truncated mutants of both isoform GAD65 and GAD67. GAD67 shows a thethered loop covering the active site, providing a catalytic environment that sustains 4-aminobutanoate production. In isoform GAD65, the same catalytic loop is inherently mobile promoting a side reaction that results in cofactor release and enzyme autoinactivation Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information crystallization data of N-terminally truncated isoform GAD67, expressing amino acids 90-594, catalytically active, and of N-terminally truncated isoform GAD65 expressing amino acids 84-585 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information isoform GAD65 undergoes a side reaction yielding pyridoxamine 5’-phosphate, succinic semialdehyde and inactive apo enzyme Homo sapiens ?
-
 ?

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Homo sapiens