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Literature summary extracted from

  • Campomanes, P.; Kellett, W.F.; Easthon, L.M.; Ozarowski, A.; Allen, K.N.; Angerhofer, A.; Rothlisberger, U.; Richards, N.G.
    Assigning the EPR fine structure parameters of the Mn(II) centers in Bacillus subtilis oxalate decarboxylase by site-directed mutagenesis and DFT/MM calculations (2014), J. Am. Chem. Soc., 136, 2313-2323.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.2 recombinant expression of His6-tagged Mn(II)-substituted W132F enzyme mutant Bacillus subtilis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.2 purified recombinant His6-tagged Mn(II)-substituted W132F enzyme mutant, hanging drop vapour diffusion method, mixing of 0.002 ml of 5 mg/ml protein in 100 mM Tris-HCl, pH 8.5, and 500 mM NaCl with.0.002 ml of well solution containing 100 mM Tris-HCl, pH 8.5, 2 M NaCl, and 10% PEG 6000, 17°C, 2 months, X-ray diffraction structure determination and analysis at 1.9-2.1 A resolution Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.2 W132F site-directed mutagenesis, the mutation causes structural changes in the N-terminal and C-terminal metal center, superimposing of the X-ray crystal structures of the Mn-containing wild-type enzyme, PDB ID 1UW8, and the Co-containing W132F enzyme mutant Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.1.2 Mn2+ dependent on, two Mn(II) centers located in the N- and C-terminal cupin domains of the enzyme, hydrogen bonding interaction between the side chains of a conserved Tryp132 and Glu101 coordinating Mn(II) in the N-terminal domain. Computational analysis of electronic properties of protein-bound Mn(II) ions using X-ray crystal protein structure with PDB ID 1UW8, quantum mechanical/molecular mechanical optimization and modeling, density functional theory and density functional theory/molecular mechanical calculations. Experimental and calculated fine structure parameters of wild-type and W132F mutant enzymes, overview Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.2 oxalate + H+ Bacillus subtilis
-
 formate + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.2 Bacillus subtilis O34714
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.2 recombinant His6-tagged Mn(II)-substituted W132F enzyme mutant by nickel affinity chromatography, dialysis, and ultrafiltration Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.2 oxalate + H+
-
 Bacillus subtilis formate + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.2 OXDC
-
 Bacillus subtilis