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Literature summary extracted from
- The catalysis of the 1,1-proton transfer by alpha-methyl-acyl-CoA racemase is coupled to a movement of the fatty acyl moiety over a hydrophobic, methionine-rich surface (2007), J. Mol. Biol., 367, 1145-1161.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 5.1.99.4 | overexpression in Escherichia coli | Mycobacterium tuberculosis |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 5.1.99.4 | purified recombinant wild-type enzyme in complex with acetyl-CoA, acetoacetyl-CoA, (R,S)-ibuprofenoyl-CoA, (2S)-methylmyristoyl-CoA, or (2R)-methylmyristoyl-CoA, 22°C, hanging-drop vapor-diffusion method, with reservoir solution containing 1.52 M ammonium phosphate, 10 mM BaCl2 at pH 7.0 in 0.0066 ml drops containing a 1:1 v/v mixture of reservoir and protein solution, the latter containing 6 mg/ml in 10 mM potassium phosphate buffer, pH 8.8, X-ray diffraction structure determination and analysis at 1.6-2.3 A resolution | Mycobacterium tuberculosis |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.99.4 | (25-R,S)-3,7,12-trihydroxycoprostanoic acid | competitive inhibition | Mycobacterium tuberculosis |  |
| 5.1.99.4 | (R)-2-methylmyristoyl CoA | binding mode | Mycobacterium tuberculosis | |
| 5.1.99.4 | (R,S)-ibuprofenoyl-CoA | competitive inhibition | Mycobacterium tuberculosis | |
| 5.1.99.4 | (S)-2-methylmyristoyl CoA | binding mode | Mycobacterium tuberculosis | |
| 5.1.99.4 | (S)-ibuprofenoyl-CoA | competitive inhibition | Mycobacterium tuberculosis | |
| 5.1.99.4 | acetoacetyl-CoA | - |
Mycobacterium tuberculosis | |
| 5.1.99.4 | acetyl-CoA | - |
Mycobacterium tuberculosis | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.99.4 | (2S)-2-methylacyl-CoA | Mycobacterium tuberculosis | - |
(2R)-2-methylacyl-CoA | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.99.4 | Mycobacterium tuberculosis | O06543 | - |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 5.1.99.4 | (2S)-2-methylacyl-CoA = (2R)-2-methylacyl-CoA | reaction mechanism, overview, the catalysis of the 1,1-proton transfer by alpha-methyl-acyl-CoA racemase is coupled to a movement of the fatty acyl moiety over a hydrophobic, methionine-rich surface, the mechanism involves the acid/base-pair residues His126 and Asp156, active site geometry, the thioester oxygen atom and the 2-methyl group are in a cisconformation with respect to each other, the thioester oxygen atom fits into an oxyanion hole and the 2-methyl group points into a hydrophobic pocket, Asp127A is a prominent residue in the active site and is located at the bottom of the catalytic site | Mycobacterium tuberculosis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.99.4 | (25S)-3,7,12-trihydroxycoprostanoic acid | - |
Mycobacterium tuberculosis | (25R)-3,7,12-trihydroxycoprostanoic acid | - |
r | |
| 5.1.99.4 | (2S)-2-methylacyl-CoA | - |
Mycobacterium tuberculosis | (2R)-2-methylacyl-CoA | - |
r | |
| 5.1.99.4 | (2S)-2-methylacyl-CoA | substrate binding structure, the S-substrate and the R-substrate bind in an S-pocket and an R-pocket, respectively, the enzyme contains a large number of methionine residues in the acyl binding region, located between the S-pocket and the R-pocket, overview | Mycobacterium tuberculosis | (2R)-2-methylacyl-CoA | - |
r | |
| 5.1.99.4 | (S)-ibuprofenoyl-CoA | binding mode at the active site, binding structure, overview | Mycobacterium tuberculosis | (R)-ibuprofenoyl-CoA | - |
r | |
| 5.1.99.4 | (S)-Pristanoyl-CoA | - |
Mycobacterium tuberculosis | (R)-Pristanoyl-CoA | - |
r | |
| 5.1.99.4 | additional information | structure of the enzyme in complex with acetyl-CoA, acetoacetyl-CoA, (R,S)-ibuprofenoyl-CoA, (2S)-methylmyristoyl-CoA, or (2R)-methylmyristoyl-CoA, overview | Mycobacterium tuberculosis | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 5.1.99.4 | More | structure of the enzyme in complex with acetyl-CoA, acetoacetyl-CoA, (R,S)-ibuprofenoyl-CoA, (2S)-methylmyristoyl-CoA, or (2R)-methylmyristoyl-CoA, overview | Mycobacterium tuberculosis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 5.1.99.4 | alpha-methylacyl coenzyme A racemase | - |
Mycobacterium tuberculosis |
| 5.1.99.4 | MCR | - |
Mycobacterium tuberculosis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 5.1.99.4 | 37 | - |
assay at | Mycobacterium tuberculosis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 5.1.99.4 | 8 | - |
assay at | Mycobacterium tuberculosis |
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