Dihydropteroate synthase: Difference between revisions

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Michal Harel, Alexander Berchansky, Joel L. Sussman

Revision as of 13:11, 20 October 2017 view source Joel L. Sussman (talk \| contribs) ConfirmAccount, Editor, Journal, Mutation, Print3D, Tester, Bureaucrats, Administrators 7,920 edits No edit summary ← Older edit		Revision as of 13:13, 20 October 2017 view source Joel L. Sussman (talk \| contribs) ConfirmAccount, Editor, Journal, Mutation, Print3D, Tester, Bureaucrats, Administrators 7,920 edits No edit summary Newer edit →
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	<StructureSection load='' size='350' side='right' scene='' caption='Dihydropteroate synthase complex with sulfate (PDB code [[1tws]])'>		<StructureSection load='1tws' size='350' side='right' scene='' caption='Dihydropteroate synthase complex with sulfate (PDB code [[1tws]])'>
	'''Dihydropteroate synthase''' (DHPS) catalyzes the condensation of 6-hydroxymethyl-7,8-dihydropteridine pyrophosphate to para-aminobenzoic acid (PABA) to form 7,8-dihydropteroate. DHPs is a key enzyme in folate synthesis. Folate is necessary for nucleic acid synthesis. DHPS is found in bacteria and not in eukaryotes. Hence, it makes a target to sulfonamide antibiotics. Some DHPS contain a dihydro-6-hydroxymethylpterin pyrophosphokinase domain at their N terminal and are named PPPK-DHPS.		'''Dihydropteroate synthase''' (DHPS) catalyzes the condensation of 6-hydroxymethyl-7,8-dihydropteridine pyrophosphate to para-aminobenzoic acid (PABA) to form 7,8-dihydropteroate. DHPs is a key enzyme in folate synthesis. Folate is necessary for nucleic acid synthesis. DHPS is found in bacteria and not in eukaryotes. Hence, it makes a target to sulfonamide antibiotics. Some DHPS contain a dihydro-6-hydroxymethylpterin pyrophosphokinase domain at their N terminal and are named PPPK-DHPS.