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Literature summary 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

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.4.99.4 1-Methyl-1,2-cis-cyclopropanedicarboxylate noncompetitive, slight inhibitor Eubacterium barkeri
5.4.99.4 1-Methyl-1,2-trans-cyclopropanedicarboxylate competitive Eubacterium barkeri
5.4.99.4 citrate slight Eubacterium barkeri
5.4.99.4 glutaconate noncompetitive Eubacterium barkeri
5.4.99.4 iodoacetamide
-
 Eubacterium barkeri
5.4.99.4 Itaconate competitive Eubacterium barkeri
5.4.99.4 L-malate competitive Eubacterium barkeri
5.4.99.4 Maleate competitive Eubacterium barkeri
5.4.99.4 succinate
-
 Eubacterium barkeri

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
5.4.99.4 70000
-
 4 * 70000, SDS-PAGE Eubacterium barkeri
5.4.99.4 300000
-
 gel filtration, sucrose density gradient centrifugation, nondenaturing PAGE Eubacterium barkeri

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.4.99.4 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

EC Number Organism UniProt Comment Textmining
5.4.99.4 Eubacterium barkeri
-
-
-

Oxidation Stability

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

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.99.4
-
 Eubacterium barkeri

Reaction

EC Number Reaction Comment Organism Reaction ID
5.4.99.4 2-Methyleneglutarate = 2-methylene-3-methylsuccinate mechanism Eubacterium barkeri
a
5.4.99.4 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
a
5.4.99.4 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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.99.4 2-Methyleneglutarate r Eubacterium barkeri 2-Methylene-3-methylsuccinate
-
 ?
5.4.99.4 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

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

Cofactor

EC Number Cofactor Comment Organism Structure
5.4.99.4 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