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Literature summary for 1.4.4.2 extracted from

  • Walker, J.L.; Oliver, D.J.
    Glycine decarboxylase multienzyme complex. Purification and partial characterization from pea leaf mitochondria (1986), J. Biol. Chem., 261, 2214-2221.
    View publication on PubMed
Search for more literature for 1.4.4.2

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol P and H protein alone jointly catalyze the glycine-CO2 exchange reaction in presence of pyridoxal phosphate and dithiothreitol Pisum sativum

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Pisum sativum 5739
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
98000
-
 alpha2, 2 * 98000, SDS-PAGE Pisum sativum
210000
-
 gel filtration Pisum sativum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glycine + lipoylprotein Pisum sativum lipoyl protein: H-protein, lipoamide can also act as acceptor S-aminomethyldihydrolipoylprotein + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Pisum sativum
-
 pea
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pisum sativum

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Pisum sativum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycine + lipoylprotein lipoyl protein: H-protein, lipoamide can also act as acceptor Pisum sativum 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 Pisum sativum ?
-
 ?

Subunits

Subunits Comment Organism
dimer alpha2, 2 * 98000, SDS-PAGE Pisum sativum

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Pisum sativum