Mycobacterium tuberculosis strain π Mycobacterium tuberculosis strain π blueTB molecules protein image

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function

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catalyses the condensation step in the fatty acid biosynthesis . It transfers a malonyl from malonyl-ACP onto an Acyl-ACP to form β-ketoacyl-ACP and CO2. Its enyzme classification is .

structure >

 

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The structural model was obtained from PDB entry , and the description from . Click here to search for at PDB.

protein >

is a peptide of with a and a The aminoacid residues involved in the active site are Cys 122, His258 and Asn289. A putative ACP-binding site spans residues 259-263. The sequence contains several additional .

Intragenome comparison reveals homology to the polyketide synthase pks11, pks10 and pks8. Close homologues in are found in Streptomyces. More functional links are available from the .

dna >

The gene is encoded in a In the M. tuberculosis laboratory strain H37Rv it is a known as which corresponds to gene in the clinical isolate CDC 1551. It can be found on the bottom of and the following page.

 

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On the circular M. tuberculosis chromosome lies at .

 

ref >

The following tuberculosis-searches could provide additional information for this specific blueTB entry: To obtain a printable version of this blueTB entry click printVersion. Click the reload button to switch back to sectional view.

blueTB molecules are published by Paul Imboden, Dr. PI Bioconsulting. Authorization to photocopy or reproduce this entry for personal use is granted. Copyright @ 2005 Paul Imboden, Dr. PI Bioconsulting. Last modified May 17, 2008 . Disclaimer: blueTB and the author reserves the right to modify and cancel any statement in these documents and regrets, that he cannot accept any responsibility for the consequences of any such changes. to the best of my knowledge all information is correct, but I cannot accept liability for any errors. References for this blueTB entry are:

Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Barrell BG, et al. Nature, 393:537-44 (1998) and the Mycobacterium tuberculosis sequencing project from the Sanger Centre.

Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains. Fleischmann RD, Alland D, Eisen JA, Carpenter L, White O, Peterson J, DeBoy R, Dodson R, Gwinn M, Haft D, Hickey E, Kolonay JF, Nelson WC, Umayam LA, Ermolaeva M, Salzberg SL, Delcher A, Utterback T, Weidman J, Khouri H, Gill J, Mikula A, Bishai W, Jacobs Jr WR Jr, Venter JC, Fraser CM. J Bacteriol. 184:5479-90 (2002) and the Mycobacterium tuberculosis sequencing project from TIGR .

3. Dr. PI's Mtbook, The Mycobacterium tuberculosis genome in a book. Paul Imboden, Dr.PI Bioconsulting. mtbook.drpi.ch/ Release 1.8.0 Jan 2004, which itself is based mainly on reference 1.

Crystal structure of a substrate complex of Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A. Musayev F, Sachdeva S, Scarsdale JN, Reynolds KA, Wright HT. J Mol Biol. 346:1313-1321 (2005)

Crystal structure of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III. Scarsdale JN, Kazanina G, He X, Reynolds KA, Wright HT. J Biol Chem. 276:20516-20522 (2001)

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