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Literature summary for 4.1.1.81 extracted from

  • Cheong, C.G.; Escalante-Semerena, J.C.; Rayment, I.
    Structural studies of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica: The apo, substrate, and product-aldimine complexes (2002), Biochemistry, 41, 9079-9089.
    View publication on PubMed
Search for more literature for 4.1.1.81

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals belong to space group I222 with unit cell dimensions a : 66.6 A, b : 103.2 A, and c : 117.1 A, apo-CobD crystals belong to space group I222 with unit cell dimensions a : 76.0 A, b : 103.3 A, and c : 109.3 A Salmonella enterica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-threonine O-3-phosphate Salmonella enterica de novo synthesis of enzymatic cofactors, cobalamin biosynthetic pathway (R)-1-aminopropan-2-yl phosphate + CO2 precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin ?

Organism

Organism UniProt Comment Textmining
Salmonella enterica
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Salmonella enterica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-threonine O-3-phosphate
-
 Salmonella enterica (R)-1-aminopropan-2-yl phosphate + CO2
-
 ?
L-threonine O-3-phosphate de novo synthesis of enzymatic cofactors, cobalamin biosynthetic pathway Salmonella enterica (R)-1-aminopropan-2-yl phosphate + CO2 precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin ?

Subunits

Subunits Comment Organism
dimer
-
 Salmonella enterica

Synonyms

Synonyms Comment Organism
CobD
-
 Salmonella enterica