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Literature summary for 5.4.3.5 extracted from

  • Pang, J.; Li, X.; Morokuma, K.; Scrutton, N.S.; Sutcliffe, M.J.
    Large-scale domain conformational change is coupled to the activation of the Co-C bond in the B12-dependent enzyme ornithine 4,5-aminomutase: a computational study (2012), J. Am. Chem. Soc., 134, 2367-2377.
    View publication on PubMed
Search for more literature for 5.4.3.5

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-ornithine Acetoanaerobium sticklandii
-
 (2R,4S)-2,4-diaminopentanoate
-
 ?

Organism

Organism UniProt Comment Textmining
Acetoanaerobium sticklandii
-
-
-

Reaction

Reaction Comment Organism Reaction ID
D-ornithine = (2R,4S)-2,4-diaminopentanoate radical-based catalysis mechanism, closed, active enzyme form modeling, overview Acetoanaerobium sticklandii
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-ornithine
-
 Acetoanaerobium sticklandii (2R,4S)-2,4-diaminopentanoate
-
 ?

Synonyms

Synonyms Comment Organism
OAM
-
 Acetoanaerobium sticklandii
ornithine 4,5-aminomutase
-
 Acetoanaerobium sticklandii

Cofactor

Cofactor Comment Organism Structure
adenosylcobalamin dependent on Acetoanaerobium sticklandii
pyridoxal 5'-phosphate
-
 Acetoanaerobium sticklandii

General Information

General Information Comment Organism
additional information going from the open, catalytically inactive form to the closed, catalytically active form, the Rossmann domain of the enzyme effectively approaches the active site as a rigid body. It undergoes a combination of a about 52° rotation and a 14 A translation to bring AdoCbl, initially positioned about 25 A away, into the active site cavity. This process is coupled to repositioning of the Ado moiety of adenosylcobalamin from the eastern conformation to the northern conformation. Combined quantum mechanics and molecular mechanics calculations further indicate that in the open form, the protein environment does not impact significantly on the Co-C bond homolytic rupture, rendering it unusually stable, and thus catalytically inactive Acetoanaerobium sticklandii