MF7000212 Chorismate mutase (Mycobacterium tuberculosis) 2qbv X-ray 2.00 Homodimer Mycobacterium tuberculosis 18727669 Kim SK, Reddy SK, Nelson BC, Robinson H, Reddy PT, Ladner JE FEBS J. 2008 19 275 4824-35 The Rv0948c gene from Mycobacterium tuberculosis H(37)R(v) encodes a 90 amino acid protein as the natural gene product with chorismate mutase (CM) activity. The protein, 90-MtCM, exhibits Michaelis-Menten kinetics with a k(cat) of 5.5+/-0.2s(-1) and a K(m) of 1500+/-100microm at 37 degrees C and pH7.5. The 2.0A X-ray structure shows that 90-MtCM is an all alpha-helical homodimer (Protein Data Bank ID: 2QBV) with the topology of Escherichia coli CM (EcCM), and that both protomers contribute to each catalytic site. Superimposition onto the structure of EcCM and the sequence alignment shows that the C-terminus helix3 is shortened. The absence of two residues in the active site of 90-MtCM corresponding to Ser84 and Gln88 of EcCM appears to be one reason for the low k(cat). Hence, 90-MtCM belongs to a subfamily of alpha-helical AroQ CMs termed AroQ(delta.) The CM gene (y2828) from Yersinia pestis encodes a 186 amino acid protein with an N-terminal signal peptide that directs the protein to the periplasm. The mature protein, *YpCM, exhibits Michaelis-Menten kinetics with a k(cat) of 70+/-5s(-1) and K(m) of 500+/-50microm at 37 degrees C and pH7.5. The 2.1A X-ray structure shows that *YpCM is an all alpha-helical protein, and functions as a homodimer, and that each protomer has an independent catalytic unit (Protein Data Bank ID: 2GBB). *YpCM belongs to the AroQ(gamma) class of CMs, and is similar to the secreted CM (Rv1885c, *MtCM) from M.tuberculosis. GO:0004106 chorismate mutase activity GO:0005737 cytoplasm GO:0005886 plasma membrane GO:0008652 amino acid biosynthetic process GO:0009095 aromatic amino acid family biosynthetic process, prephenate pathway GO:0046417 chorismate metabolic process GO:0009697 salicylic acid biosynthetic process 2 1 Homooligomeric enzymes Homodimeric enzymes All chains according to the most probable oligomerization state stored in PDBe were considered. A Intracellular chorismate mutase Mycobacterium tuberculosis P9WIC1 28 100 69% MRPEPPHHENAELAAMNLEMLESQPVPEIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELGPDGKDLAILLLRLGRGRLGH 105 secondary structure helix 13 48 secondary structure helix 57 67 secondary structure helix 70 84 pfam PF01817 Chorismate mutase type II 32 88 A-2 Intracellular chorismate mutase Mycobacterium tuberculosis P9WIC1 28 100 69% MRPEPPHHENAELAAMNLEMLESQPVPEIDTLREEIDRLDAEILALVKRRAEVSKAIGKARMASGGTRLVHSREMKVIERYSELGPDGKDLAILLLRLGRGRLGH 105 pfam PF01817 Chorismate mutase type II 32 88 Indirect evidence The full structure participates in mutual synergistic folding. Chorismate mutase type II The enzyme is an intertwined dimer of three helices with connecting loops. The N-terminal helices of the two monomers twine together to form an anti-parallel coiled-coil with a hydrophobic interaction surface. The loop between the first and second helices is disordered (PMID:16914555). A N/A A-2 N/A MF7000162 MF7000212 MF7000163 MF7000211 MF7000164 MF7000165 MF7000209 MF7000210