BRENDA - Enzyme Database

Isocitrate lyase from Pinus pinea. Characterization of its true substrate and the action of magnesium ions

Giachetti, E.; Pinzauti, G.; Bonaccorsi, R.; Vanni, P.; Eur. J. Biochem. 172, 85-91 (1988)

Data extracted from this reference:

Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
4.1.3.1
Mg2+
reactivation after thermal inactivation, Mg2+-isocitrate complex is true substrate, 2 Mg2+-binding sites: catalytic and activator site
Pinus pinea
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.1.3.1
Pinus pinea
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.1.3.1
isocitrate
Mg-isocitrate is the true substrate
33122
Pinus pinea
succinate + glyoxylate
-
33122
Pinus pinea
r
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
4.1.3.1
Mg2+
reactivation after thermal inactivation, Mg2+-isocitrate complex is true substrate, 2 Mg2+-binding sites: catalytic and activator site
Pinus pinea
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.1.3.1
isocitrate
Mg-isocitrate is the true substrate
33122
Pinus pinea
succinate + glyoxylate
-
33122
Pinus pinea
r