Your browser does not fully support modern features. Please upgrade for a smoother experience.
Submitted Successfully!
Thank you for your contribution! You can also upload a video entry or images related to this topic. For video creation, please contact our Academic Video Service.
Version Summary Created by Modification Content Size Created at Operation
1 handwiki Vivi Li -- 1135 2022-11-03 01:41:28

Video Upload Options

We provide professional Academic Video Service to translate complex research into visually appealing presentations. Would you like to try it?
Cite
If you have any further questions, please contact Encyclopedia Editorial Office.
HandWiki. Beta-ketoacyl-(acyl-carrier-protein) Synthase III. Encyclopedia. Available online: https://encyclopedia.pub/entry/32599 (accessed on 23 September 2026).
HandWiki. Beta-ketoacyl-(acyl-carrier-protein) Synthase III. Encyclopedia. Available at: https://encyclopedia.pub/entry/32599. Accessed September 23, 2026.
HandWiki. "Beta-ketoacyl-(acyl-carrier-protein) Synthase III" Encyclopedia, https://encyclopedia.pub/entry/32599 (accessed September 23, 2026).
HandWiki. (2022, November 03). Beta-ketoacyl-(acyl-carrier-protein) Synthase III. In Encyclopedia. https://encyclopedia.pub/entry/32599
HandWiki. "Beta-ketoacyl-(acyl-carrier-protein) Synthase III." Encyclopedia. Web. 03 November, 2022.
Beta-ketoacyl-(acyl-carrier-protein) Synthase III
Edit

In enzymology, a β-ketoacyl-[acyl-carrier-protein] synthase III (EC 2.3.1.180) is an enzyme that catalyzes the chemical reaction Thus, the two substrates of this enzyme are acetyl-CoA and malonyl-[acyl-carrier-protein], whereas its 3 products are acetoacetyl-[acyl-carrier-protein], CoA, and CO2. This enzyme belongs to the family of transferases, to be specific those acyltransferases transferring groups other than aminoacyl groups. This enzyme participates in fatty acid biosynthesis. β-Ketoacyl-acyl-carrier-protein synthase III is involved in the dissociated (or type II) fatty-acid biosynthesis system that occurs in plants and bacteria. The role of FabH in fatty acid synthesis has been described in Streptomyces glaucescens, Streptococcus pneumoniae, and Streptomyces coelicolor.

coelicolor malonyl-acyl-carrier-protein β-ketoacyl-acyl-carrier-protein

References

  1. "The Mycobacterium tuberculosis FAS-II condensing enzymes: their role in mycolic acid biosynthesis, acid-fastness, pathogenesis and in future drug development". Mol. Microbiol. 64 (6): 1442–54. June 2007. doi:10.1111/j.1365-2958.2007.05761.x. PMID 17555433.  https://dx.doi.org/10.1111%2Fj.1365-2958.2007.05761.x
  2. "Flux Balance Analysis of Mycolic Acid Pathway: Targets for Anti-Tubercular Drugs". PLoS Comput. Biol. 1 (5): e46. October 2005. doi:10.1371/journal.pcbi.0010046. PMID 16261191. Bibcode: 2005PLSCB...1...46R.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1246807
  3. "Genes required for mycobacterial growth defined by high density mutagenesis". Mol. Microbiol. 48 (1): 77–84. April 2003. doi:10.1046/j.1365-2958.2003.03425.x. PMID 12657046.  https://dx.doi.org/10.1046%2Fj.1365-2958.2003.03425.x
  4. "The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli". Structure 8 (2): 185–95. 2000. doi:10.1016/S0969-2126(00)00094-0. PMID 10673437.  https://dx.doi.org/10.1016%2FS0969-2126%2800%2900094-0
  5. PDB: 1HND​, 1HNH​, 1HNJ​; "Refined structures of beta-ketoacyl-acyl carrier protein synthase III". J. Mol. Biol. 307 (1): 341–56. March 2001. doi:10.1006/jmbi.2000.4457. PMID 11243824.  https://www.rcsb.org/structure/1HND
  6. PDB: 1HZP​; "Crystal structure of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III". J. Biol. Chem. 276 (23): 20516–22. June 2001. doi:10.1074/jbc.M010762200. PMID 11278743.  https://www.rcsb.org/structure/1HZP
  7. PDB: 1ZOW​; "Crystal structure and substrate specificity of the β-ketoacyl-acyl carrier protein synthase III (FabH) from Staphylococcus aureus". Protein Sci. 14 (8): 2087–94. August 2005. doi:10.1110/ps.051501605. PMID 15987898.  https://www.rcsb.org/structure/1ZOW
  8. PDB: 1HN9​; "Crystal structure of beta-ketoacyl-acyl carrier protein synthase III. A key condensing enzyme in bacterial fatty acid biosynthesis". J. Biol. Chem. 274 (51): 36465–71. December 1999. doi:10.1074/jbc.274.51.36465. PMID 10593943.  https://www.rcsb.org/structure/1HN9
  9. PDB: 1UB7​Inagaki E, Kuramitsu S, Yokoyama S, Miyano M, Tahirov TH (2007) The Crystal Structure of Beta-Ketoacyl-[Acyl Carrier Protein] Synthase III (Fabh) from Thermus thermophilus. https://www.rcsb.org/structure/1UB7
  10. "Identification and substrate specificity of beta -ketoacyl (acyl carrier protein) synthase III (mtFabH) from Mycobacterium tuberculosis". J. Biol. Chem. 275 (36): 28201–7. September 2000. doi:10.1074/jbc.M003241200. PMID 10840036.  https://dx.doi.org/10.1074%2Fjbc.M003241200
  11. PDB: 1M1M​, 2AJ9​; "Probing the mechanism of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III mtFabH: factors influencing catalysis and substrate specificity". J. Biol. Chem. 280 (37): 32539–47. September 2005. doi:10.1074/jbc.M413216200. PMID 16040614.  https://www.rcsb.org/structure/1M1M
  12. PDB: 1MZS​; "First X-ray cocrystal structure of a bacterial FabH condensing enzyme and a small molecule inhibitor achieved using rational design and homology modeling". J. Med. Chem. 46 (1): 5–8. January 2003. doi:10.1021/jm025571b. PMID 12502353.  https://www.rcsb.org/structure/1MZS
  13. "Structure-based design, synthesis, and study of potent inhibitors of beta-ketoacyl-acyl carrier protein synthase III as potential antimicrobial agents". J. Med. Chem. 48 (5): 1596–609. March 2005. doi:10.1021/jm049141s. PMID 15743201.  https://dx.doi.org/10.1021%2Fjm049141s
  14. "A combined approach of docking and 3D QSAR study of beta-ketoacyl-acyl carrier protein synthase III (FabH) inhibitors". Bioorg. Med. Chem. 14 (5): 1474–82. March 2006. doi:10.1016/j.bmc.2005.10.001. PMID 16275103.  https://dx.doi.org/10.1016%2Fj.bmc.2005.10.001
  15. PDB: 1U6S​; "Crystal structure of a substrate complex of Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthase III (FabH) with lauroyl-coenzyme A". J. Mol. Biol. 346 (5): 1313–21. March 2005. doi:10.1016/j.jmb.2004.12.044. PMID 15713483.  https://www.rcsb.org/structure/1U6S
  16. "The Mycobacterium tuberculosis β-Ketoacyl-Acyl Carrier Protein Synthase III Activity Is Inhibited by Phosphorylation on a Single Threonine Residue". J. Biol. Chem. 284 (10): 6414–24. March 2009. doi:10.1074/jbc.M806537200. PMID 19074144.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2649087
  17. "Drugs that inhibit mycolic acid biosynthesis in Mycobacterium tuberculosis". Curr Pharm Biotechnol 3 (3): 197–225. September 2002. doi:10.2174/1389201023378328. PMID 12164478.  https://dx.doi.org/10.2174%2F1389201023378328
  18. "Biphenyl-based analogues of thiolactomycin, active against Mycobacterium tuberculosis mtFabH fatty acid condensing enzyme". Bioorg. Med. Chem. Lett. 13 (21): 3685–8. November 2003. doi:10.1016/j.bmcl.2003.08.015. PMID 14552758.  https://dx.doi.org/10.1016%2Fj.bmcl.2003.08.015
  19. "Acetylene-based analogues of thiolactomycin, active against Mycobacterium tuberculosis mtFabH fatty acid condensing enzyme". Bioorg. Med. Chem. Lett. 14 (2): 373–6. January 2004. doi:10.1016/j.bmcl.2003.10.061. PMID 14698162.  https://dx.doi.org/10.1016%2Fj.bmcl.2003.10.061
  20. "1,2-Dithiole-3-Ones as Potent Inhibitors of the Bacterial 3-Ketoacyl Acyl Carrier Protein Synthase III (FabH)". Antimicrob. Agents Chemother. 48 (8): 3093–102. August 2004. doi:10.1128/AAC.48.8.3093-3102.2004. PMID 15273125.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=478545
  21. Todd, Matthew H., ed (2009). "Identification of 2-Aminothiazole-4-Carboxylate Derivatives Active against Mycobacterium tuberculosis H37Rv and the β-Ketoacyl-ACP Synthase mtFabH". PLoS ONE 4 (5): e5617. doi:10.1371/journal.pone.0005617. PMID 19440303. Bibcode: 2009PLoSO...4.5617A.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2680598
  22. "Discovery of FabH/FabF Inhibitors from Natural Products". Antimicrob. Agents Chemother. 50 (2): 519–26. February 2006. doi:10.1128/AAC.50.2.519-526.2006. PMID 16436705.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1366929
  23. "Discovery of bacterial fatty acid synthase inhibitors from a Phoma species as antimicrobial agents using a new antisense-based strategy". J. Nat. Prod. 69 (3): 377–80. March 2006. doi:10.1021/np050416w. PMID 16562839.  https://dx.doi.org/10.1021%2Fnp050416w
  24. "Discovery of platencin, a dual FabF and FabH inhibitor with in vivo antibiotic properties". Proceedings of the National Academy of Sciences of the United States of America 104 (18): 7612–6. May 2007. doi:10.1073/pnas.0700746104. PMID 17456595. Bibcode: 2007PNAS..104.7612W.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1863502
  25. Ahmed, Niyaz, ed (2009). "Platensimycin Activity against Mycobacterial β-Ketoacyl-ACP Synthases". PLoS ONE 4 (7): e6306. doi:10.1371/journal.pone.0006306. PMID 19609444. Bibcode: 2009PLoSO...4.6306B.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2707616
  26. "Mycolic Acid Index Susceptibility Method for Mycobacterium tuberculosis". J. Clin. Microbiol. 39 (7): 2642–5. July 2001. doi:10.1128/JCM.39.7.2642-2645.2001. PMID 11427584.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=88200
  27. "Development of a scintillation proximity assay for beta-ketoacyl-acyl carrier protein synthase III". Anal. Biochem. 282 (1): 107–14. June 2000. doi:10.1006/abio.2000.4594. PMID 10860506.  https://dx.doi.org/10.1006%2Fabio.2000.4594
  28. "The growing burden of tuberculosis: global trends and interactions with the HIV epidemic". Arch. Intern. Med. 163 (9): 1009–21. May 2003. doi:10.1001/archinte.163.9.1009. PMID 12742798.  https://dx.doi.org/10.1001%2Farchinte.163.9.1009
  29. "Global Tuberculosis Control 2007". World Health Organization. 2007. Archived from the original on 2010-02-02. https://web.archive.org/web/20100202185311/http://www.who.int/tb/publications/global_report/2007/download_centre/en/index.html. Retrieved 2010-01-02. 
  30. "TB Alliance — An Outdated Treatment". Global Alliance for TB Drug Development. Archived from the original on 2010-01-13. https://web.archive.org/web/20100113165524/http://www.tballiance.org/why/outdated.php. Retrieved 2010-01-02. 
  31. "New Approaches to Filling the Gap in Tuberculosis Drug Discovery". PLoS Med. 4 (11): e293. November 2007. doi:10.1371/journal.pmed.0040293. PMID 17988169.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2062479
  32. "TB Alliance — TB Drug Portfolio". Global Alliance for TB Drug Development. Archived from the original on 2010-01-13. https://web.archive.org/web/20100113155341/http://www.tballiance.org/new/portfolio.php. Retrieved 2010-01-02. 
  33. "New Study Reveals Limitations of a Complex and Challenging Global Tuberculosis Drug Marketplace". TB Alliance Newscenter: News Release. Global Alliance for TB Drug Development. 2007-05-14. http://www.tballiance.org/newscenter/view-brief.php?id=683. Retrieved 2010-01-02. 
  34. "The Economics of TB Drug Development". Global Alliance for TB Drug Development. 2001. http://www.tballiance.org/downloads/publications/TBA_Economics_Report.pdf. Retrieved 2010-01-02. 
More
Upload a video for this entry
Information
Subjects: Cell Biology
Contributor MDPI registered users' name will be linked to their SciProfiles pages. To register with us, please refer to https://encyclopedia.pub/register :
View Times: 848
Entry Collection: HandWiki
Revision: 1 time (View History)
Update Date: 03 Nov 2022
Notice
You are not a member of the advisory board for this topic. If you want to update advisory board member profile, please contact office@encyclopedia.pub.
OK
Confirm
Only members of the Encyclopedia advisory board for this topic are allowed to note entries. Would you like to become an advisory board member of the Encyclopedia?
Yes
No
${ textCharacter }/${ maxCharacter }
Submit
Cancel
There is no comment~
${ textCharacter }/${ maxCharacter }
Submit
Cancel
${ selectedItem.replyTextCharacter }/${ selectedItem.replyMaxCharacter }
Submit
Cancel
Confirm
Are you sure to Delete?
Yes No
Academic Video Service