Sandbox Reserved 321: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 18: Line 18:
The enzyme inhA is coded from the inhA gene that is simillar in sequence to the ''[http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]''gene which plays a role in fatty acid biosynthesis <ref name ="making drugs for inhA">PMID:5882878</ref>. Inha is an NADH dependent trans enoyl-acyl ACP carrier protein that plays a role in the sysnthesis of Mycolic Acid, and is part of a short-chain dehydrogenase/reductase family <ref name ="mech of thioamide drug action">PMID:17227913</ref><ref name ="phosphorylation of inhA">PMID:21143326</ref>.  Mycolic acids are long chain fatty acids that are essential in cell wall formation of the human pathogen ''[http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]''as well as other mycobateria such as ''[http://en.wikipedia.org/wiki/Mycobacterium_leprae Mycobacterium leprae]''<ref name ="TB">PMID2568869:</ref>. Inha has been propsed as the target of the thionamide drugs, ethionamide (ETH)  and isoniazid (INH), which have been used in treatment of mycobacterial infections <ref name ="phosphorylation of inhA">PMID:21143326</ref>.   
The enzyme inhA is coded from the inhA gene that is simillar in sequence to the ''[http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]''gene which plays a role in fatty acid biosynthesis <ref name ="making drugs for inhA">PMID:5882878</ref>. Inha is an NADH dependent trans enoyl-acyl ACP carrier protein that plays a role in the sysnthesis of Mycolic Acid, and is part of a short-chain dehydrogenase/reductase family <ref name ="mech of thioamide drug action">PMID:17227913</ref><ref name ="phosphorylation of inhA">PMID:21143326</ref>.  Mycolic acids are long chain fatty acids that are essential in cell wall formation of the human pathogen ''[http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]''as well as other mycobateria such as ''[http://en.wikipedia.org/wiki/Mycobacterium_leprae Mycobacterium leprae]''<ref name ="TB">PMID2568869:</ref>. Inha has been propsed as the target of the thionamide drugs, ethionamide (ETH)  and isoniazid (INH), which have been used in treatment of mycobacterial infections <ref name ="phosphorylation of inhA">PMID:21143326</ref>.   


==Structure==
==Structure of inhA==


The overall strucuture of the inhA enzyme of ''[http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]'' consists of a single domain with two substructures<ref name ="making drugs for inhA">PMID:5882878</ref>.  
The overall strucuture of the inhA enzyme of ''[http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]'' consists of a single domain with two substructures<ref name ="making drugs for inhA">PMID:5882878</ref>.  


===Substructure 1===
===Substructure 1 of inhA===


Substructure one consists of 6 parallel β strands and 4 α helices interwoven together to form a core α/β structure that contains the n-terminal domain</scene><ref name ="making drugs for inhA">PMID:5882878</ref>.  
Substructure one consists of 6 parallel β strands and 4 α helices interwoven together to form a core α/β structure that contains the n-terminal domain<ref name ="making drugs for inhA">PMID:5882878</ref>.  
The first substructure can be further broken down into <scene name='Sandbox_Reserved_321/Substructure1section1/7'>two sections</scene> consisting of two β strands <scene name='Sandbox_Reserved_321/B-1_and_b-2/4'>(B-1 and B-2)</scene>and two short α helicies <scene name='Sandbox_Reserved_321/A-1_and_a-2/2'>(A-1 and A-2) </scene><ref name ="making drugs for inhA">PMID:5882878</ref>.  The first section is connected to the second by a β strand (B-3) that crosses over the two domains, and leads into the second section initiating at the fourth α helix (A-4)</scene><ref name ="making drugs for inhA">PMID:5882878</ref>.  A-4 then leads into a fifth strand β (B-5), followed by a 25 residue α helix (A-5), and finally the last strand β (B-6)</scene><ref name ="making drugs for inhA">PMID:5882878</ref>.  
The first substructure can be further broken down into two sections, the <scene name='Sandbox_Reserved_321/Substructure1section1/7'>first section</scene> consisting of two β strands <scene name='Sandbox_Reserved_321/B-1_and_b-2/4'>(B-1 and B-2)</scene>and two short α helicies <scene name='Sandbox_Reserved_321/A-1_and_a-2/2'>(A-1 and A-2)</scene><ref name ="making drugs for inhA">PMID:5882878</ref>.   
The first section is connected to the <scene name='Sandbox_Reserved_321/Section2substructure1/1'>second section</scene> by a β strand <scene name='Sandbox_Reserved_321/B-3/1'>(B-3)</scene> that crosses over the two domains, and leads into the second section initiating at the fourth α helix (A-4)</scene><ref name ="making drugs for inhA">PMID:5882878</ref>.  A-4 then leads into a fifth strand β (B-5), followed by a 25 residue α helix (A-5), and finally the last strand β (B-6)<ref name ="making drugs for inhA">PMID:5882878</ref>.
===Substructure 2 of inhA===


===Substructure 2===
Substructure two contains the c-terminal region of the molecule and consists of a small β strand (B-7), and two α helicies (A-6 and A-7) which are conected by a short five residue loop<ref name ="making drugs for inhA">PMID:5882878</ref>.   
 
 
==Physiological Function==


==Role in the Mycolic Acid Pathway==
==Role in the Mycolic Acid Pathway==
==Physiological Function==


==Protein Superfamilly==
==Protein Superfamilly==
Retrieved from "https://proteopedia.org/Sandbox_Reserved_321"