Dihydropteroate synthase: Difference between revisions

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Revision as of 14:18, 13 November 2013 view source Alexander Berchansky (talk \| contribs) 29,637 edits No edit summary ← Older edit		Revision as of 14:27, 10 December 2013 view source Alexander Berchansky (talk \| contribs) 29,637 edits No edit summary Newer edit →
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	<StructureSection load='' size='450' side='right' scene='~~Journal:JBSD:24~~/Cv/1' caption=''>		<StructureSection load='' size='450' side='right' scene='49/493691/Cv/1' caption=''>
	'''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.