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Literature summary extracted from

  • Forouhar, F.; Hussain, M.; Farid, R.; Benach, J.; Abashidze, M.; Edstrom, W.C.; Vorobiev, S.M.; Xiao, R.; Acton, T.B.; Fu, Z.; Kim, J.J.; Miziorko, H.M.; Montelione, G.T.; Hunt, J.F.
    Crystal structures of two bacterial Hmg-CoA lyases suggest a common catalytic mechanism among a family of TIM-barrel metalloenzymes cleaving carbon-carbon bonds (2005), J. Biol. Chem., 281, 7533-7545.
    View publication on PubMed

Application

EC Number Application Comment Organism
4.1.3.4 medicine mutations in this enzyme cause a human autosomal recessive disorder called primary metabolic aciduria Bacillus subtilis
4.1.3.4 medicine mutations in this enzyme cause a human autosomal recessive disorder called primary metabolic aciduria Brucella melitensis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.3.4 expression in Escherichia coli Bacillus subtilis
4.1.3.4 expression in Escherichia coli Brucella melitensis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.3.4 hanging drop vapour diffusion method with 19% (w/v) PEG 3350, 200 mM CaCl2, 10 mM dithiothreitol Brucella melitensis
4.1.3.4 hanging drop vapour diffusion method with 22.5% (w/v) PEG 3350, 210 mM sodium iodide, 5 mM EDTA, 10 mM dithiothreitol Bacillus subtilis
4.1.3.4 hanging-drop vapour diffusion method Bacillus subtilis
4.1.3.4 hanging-drop vapour diffusion method Brucella melitensis

Protein Variants

EC Number Protein Variants Comment Organism
4.1.3.4 A252A decreased Km relative to the wild type enzyme Brucella melitensis
4.1.3.4 C238A increased Km relative to the wild type enzyme Brucella melitensis
4.1.3.4 C238S decreased Km relative to the wild type enzyme Brucella melitensis
4.1.3.4 C240A increased Km relative to the wild type enzyme Bacillus subtilis
4.1.3.4 C240S decreased Km relative to the wild type enzyme Bacillus subtilis
4.1.3.4 D14E decreased Km relative to the wild type enzyme Brucella melitensis
4.1.3.4 D16E decreased Km relative to the wild type enzyme Bacillus subtilis
4.1.3.4 D16N decreased Km relative to the wild type enzyme Bacillus subtilis
4.1.3.4 D176A increased Km relative to the wild type enzyme Brucella melitensis
4.1.3.4 D178A increased Km relative to the wild type enzyme Bacillus subtilis
4.1.3.4 D254A decreased Km relative to the wild type enzyme Bacillus subtilis
4.1.3.4 E11D decreased Km relative to the wild type enzyme Bacillus subtilis
4.1.3.4 E253A decreased Km relative to the wild type enzyme Bacillus subtilis
4.1.3.4 E44A increased Km relative to the wild type enzyme Brucella melitensis
4.1.3.4 E46A increased Km relative to the wild type enzyme Bacillus subtilis
4.1.3.4 E9D decreased Km relative to the wild type enzyme Brucella melitensis
4.1.3.4 H205A increased Km relative to the wild type enzyme Brucella melitensis
4.1.3.4 H205D increased Km relative to the wild type enzyme Brucella melitensis
4.1.3.4 H205R decreased Km relative to the wild type enzyme Brucella melitensis
4.1.3.4 H207A increased Km relative to the wild type enzyme Bacillus subtilis
4.1.3.4 H207D increased Km relative to the wild type enzyme Bacillus subtilis
4.1.3.4 H207R decreased Km relative to the wild type enzyme Bacillus subtilis
4.1.3.4 K297S increased Km relative to the wild type enzyme Bacillus subtilis
4.1.3.4 R13Q increased Km relative to the wild type enzyme Brucella melitensis
4.1.3.4 R15Q increased Km relative to the wild type enzyme Bacillus subtilis
4.1.3.4 V251A decreased Km relative to the wild type enzyme Brucella melitensis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.3.4 Mg2+ can replace Mn2+ required for activity Bacillus subtilis
4.1.3.4 Mg2+ can replace Mn2+ required for activity Brucella melitensis
4.1.3.4 Mn2+ required for activity Bacillus subtilis
4.1.3.4 Mn2+ required for activity Brucella melitensis
4.1.3.4 additional information reaction mechanism involves an invariant Asp-Arg-Glu (DRE)triplet. The Asp ligates the divalent cation, the Arg probably stabilizes charge accumulation in the enolate intermediate, and the Glu maintains the precise structural alignment of the Asp and Arg Bacillus subtilis
4.1.3.4 additional information reaction mechanism involves an invariant Asp-Arg-Glu (DRE)triplet. The Asp ligates the divalent cation, the Arg probably stabilizes charge accumulation in the enolate intermediate, and the Glu maintains the precise structural alignment of the Asp and Arg Brucella melitensis

Organism

EC Number Organism UniProt Comment Textmining
4.1.3.4 Bacillus subtilis O34873
-
-
4.1.3.4 Brucella melitensis Q8YEF2
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.3.4
-
 Bacillus subtilis
4.1.3.4
-
 Brucella melitensis
4.1.3.4 nickel-nitrilotriacetic acid column chromatography and Superdex 75 gel filtration Bacillus subtilis
4.1.3.4 nickel-nitrilotriacetic acid column chromatography and Superdex 75 gel filtration Brucella melitensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.3.4 (S)-3-Hydroxy-3-methylglutaryl-CoA
-
 Bacillus subtilis Acetyl-CoA + acetoacetate
-
 ?
4.1.3.4 (S)-3-Hydroxy-3-methylglutaryl-CoA
-
 Brucella melitensis Acetyl-CoA + acetoacetate
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.3.4 dimer static light scattering, crystal contains two dimers forming a pseudotetramer per asymmetric unit Bacillus subtilis
4.1.3.4 dimer static light scattering, crystal contains two dimers forming a pseudotetramer per asymmetric unit Brucella melitensis

Synonyms

EC Number Synonyms Comment Organism
4.1.3.4 3-hydroxy-3-methylglutarate-CoA lyase
-
 Bacillus subtilis
4.1.3.4 3-hydroxy-3-methylglutarate-CoA lyase
-
 Brucella melitensis
4.1.3.4 HMG-CoA lyase
-
 Bacillus subtilis
4.1.3.4 HMG-CoA lyase
-
 Brucella melitensis
4.1.3.4 HMG-CoA lyase belongs to the family of DRE-TIM metallolyases Bacillus subtilis
4.1.3.4 HMG-CoA lyase belongs to the family of DRE-TIM metallolyases Brucella melitensis