Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.4.4.2 extracted from

  • Hiraga, K.; Kikuchi, G.
    The mitochondrial glycine cleavage system. Purification and properties of glycine decarboxylase from chicken liver mitochondria (1980), J. Biol. Chem., 255, 11664-11670.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
40
-
glycine
-
Gallus gallus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Gallus gallus 5739
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
100000
-
alpha2, 2 * 100000, SDS-PAGE Gallus gallus
208000
-
sucrose density gradient centrifugation Gallus gallus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glycine + lipoylprotein Gallus gallus reaction is stimulated by lipoic acid which is a functional group of the H-protein S-aminomethyldihydrolipoylprotein + CO2
-
?
glycine + lipoylprotein Gallus gallus glycine decarboxylation catalyzed by P-protein alone is extremely low S-aminomethyldihydrolipoylprotein + CO2
-
?
glycine + lipoylprotein Gallus gallus lipoyl protein: H-protein, lipoamide can also act as acceptor S-aminomethyldihydrolipoylprotein + CO2
-
?

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Gallus gallus

Reaction

Reaction Comment Organism Reaction ID
glycine + [glycine-cleavage complex H protein]-N6-lipoyl-L-lysine = [glycine-cleavage complex H protein]-S-aminomethyl-N6-dihydrolipoyl-L-lysine + CO2 H-protein ping-pong mechanism Gallus gallus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Gallus gallus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.13
-
-
Gallus gallus

Storage Stability

Storage Stability Organism
-20°C, several weeks Gallus gallus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycine + lipoylprotein reaction is stimulated by lipoic acid which is a functional group of the H-protein Gallus gallus S-aminomethyldihydrolipoylprotein + CO2
-
?
glycine + lipoylprotein glycine decarboxylation catalyzed by P-protein alone is extremely low Gallus gallus S-aminomethyldihydrolipoylprotein + CO2
-
?
glycine + lipoylprotein lipoyl protein: H-protein, lipoamide can also act as acceptor Gallus gallus S-aminomethyldihydrolipoylprotein + CO2
-
?
additional information P-protein also catalyzes exchange of carbonyl carbon of glycine with CO2, reaction greatly stimulated by addition of H protein Gallus gallus ?
-
?
additional information the glycine cleavage system consists of 4 protein components: 1. P-protein is a pyridoxal containing protein: a Schiff base is formed between the hydroxyl group of the pyridoxal phosphate and the alpha-NH2 of glycine, the amino group and the alpha-carbon of the glycine are transferred to the lipoamide cofactor of the second enzyme of the complex the H-protein, the alpha-carbonyl group of glycine is lost as CO2, 2. H-protein, 3. T-protein: catalyzes the passage of alpha-carbon from lipoamide of H protein to tetrahydrofolate, alpha-NH2 from glycine is lost as NH4+, 4. L-protein: catalyzes oxidation of reduced lipoamide back to its original form with concomitant reduction of NAD+ to NADH Gallus gallus ?
-
?

Subunits

Subunits Comment Organism
dimer alpha2, 2 * 100000, SDS-PAGE Gallus gallus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Gallus gallus

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate bound Gallus gallus