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Literature summary for 5.4.99.4 extracted from

  • Chemaly, S.M.
    alpha-Methyleneglutarate mutase: an adenosylcobalamin-dependent enzyme (1994), S. Afr. J. Chem., 47, 37-47.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
sulfhydryl groups contains active thiol groups Eubacterium barkeri

Inhibitors

Inhibitors Comment Organism Structure
1-Methyl-1,2-cis-cyclopropanedicarboxylate noncompetitive, slight inhibitor Eubacterium barkeri
1-Methyl-1,2-trans-cyclopropanedicarboxylate competitive Eubacterium barkeri
citrate slight Eubacterium barkeri
glutaconate noncompetitive Eubacterium barkeri
iodoacetamide
-
Eubacterium barkeri
Itaconate competitive Eubacterium barkeri
L-malate competitive Eubacterium barkeri
Maleate competitive Eubacterium barkeri
succinate
-
Eubacterium barkeri

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
4 * 70000, SDS-PAGE Eubacterium barkeri
300000
-
gel filtration, sucrose density gradient centrifugation, nondenaturing PAGE Eubacterium barkeri

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Eubacterium barkeri carbon-skeleton rearrangement mechanism. Adenosylcobalamin acts as a carrier for the hydrogen atom that is abstracted from alpha-methyleneglutarate and replaced by the acrylyl group of 2-methyleneglutarate ?
-
?

Organism

Organism UniProt Comment Textmining
Eubacterium barkeri
-
-
-

Oxidation Stability

Oxidation Stability Organism
enzyme containing cobalamin(II) is stable to oxygen and is an inactive form of the enzyme Eubacterium barkeri

Purification (Commentary)

Purification (Comment) Organism
-
Eubacterium barkeri

Reaction

Reaction Comment Organism Reaction ID
2-Methyleneglutarate = 2-methylene-3-methylsuccinate mechanism Eubacterium barkeri
2-Methyleneglutarate = 2-methylene-3-methylsuccinate the steric course of the reaction is such that the acrylyl residue migrates from the beta-carbon to the alpha-carbon of the propionate with inversion of configuration at the alpha-carbon Eubacterium barkeri
2-Methyleneglutarate = 2-methylene-3-methylsuccinate unimolecular free radical rearrangement via 3-butenyl and cyclopropylmethyl intermediates is a reasonable mechanism for the rearrangement step of the enzyme Eubacterium barkeri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-Methyleneglutarate r Eubacterium barkeri 2-Methylene-3-methylsuccinate
-
?
additional information carbon-skeleton rearrangement mechanism. Adenosylcobalamin acts as a carrier for the hydrogen atom that is abstracted from alpha-methyleneglutarate and replaced by the acrylyl group of 2-methyleneglutarate Eubacterium barkeri ?
-
?

Subunits

Subunits Comment Organism
tetramer 4 * 70000, SDS-PAGE Eubacterium barkeri

Cofactor

Cofactor Comment Organism Structure
cobamide acts as a carrier for the hydrogen atom that is abstracted from alpha-methyleneglutarate. The enzyme contains 4 cobalamin molecules per tetramer. The cobalamins consist of adenosylcobalamin and cobalamin(II). Enzyme containing adenosylcobalamin is the active form of the enzyme but the enzyme containing cobalamin(II) is stable to oxygen and is an inactive form of the enzyme Eubacterium barkeri