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Literature summary extracted from

  • Rudnick, G.; Abeles, R.H.
    Reaction mechanism and structure of the active site of proline racemase (1975), Biochemistry, 14, 4515-4522.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.1.1.4 Bromoacetate
-
Acetoanaerobium sticklandii
5.1.1.4 iodoacetamide
-
Acetoanaerobium sticklandii
5.1.1.4 iodoacetate DL-Pro and pyrrole-2-carboxylate can protect Acetoanaerobium sticklandii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.1.1.4 38000
-
x * 38000, SDS-PAGE Acetoanaerobium sticklandii

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.4 Acetoanaerobium sticklandii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.1.1.4 2 forms of enzyme: one binds L-Pro and the other D-Pro Acetoanaerobium sticklandii

Reaction

EC Number Reaction Comment Organism Reaction ID
5.1.1.4 L-proline = D-proline two-base mechanism in which one base on the enzyme removes the substrate alpha-hydrogen as a proton and the conjugate acid of another base donates a proton to the opposite side of the alpha-carbon Acetoanaerobium sticklandii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.4 L-Pro
-
Acetoanaerobium sticklandii D-Pro
-
?

Subunits

EC Number Subunits Comment Organism
5.1.1.4 ? x * 38000, SDS-PAGE Acetoanaerobium sticklandii