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evolution
enzymes FabH from Gram-positive and Gram-negative bacteria are known to have distinct preferences for acyl-CoA primers. This is functionally important, as the substrate specificity of the enzyme governs the fatty acid profile of the organism. FabH from Escherichia coli and other Gram-negative organisms are selective for acetyl-CoA and produce straight-chain fatty acids, while the FabH enzymes of Gram-positive bacteria such as bacilli prefer branched-chain primers and produce branched-chain fatty acids
evolution
enzymes FabH from Gram-positive and Gram-negative bacteria are known to have distinct preferences for acyl-CoA primers. This is functionally important, as the substrate specificity of the enzyme governs the fatty acid profile of the organism. FabH from Escherichia coli and other Gram-negative organisms are selective for acetyl-CoA and produce straight-chain fatty acids, while the FabH enzymes of Gram-positive bacteria such as bacilli prefer branched-chain primers and produce branched-chain fatty acids
evolution
FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa
evolution
FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa
evolution
FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa
evolution
FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa
evolution
FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa
evolution
FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa
evolution
FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa
evolution
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FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa
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evolution
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enzymes FabH from Gram-positive and Gram-negative bacteria are known to have distinct preferences for acyl-CoA primers. This is functionally important, as the substrate specificity of the enzyme governs the fatty acid profile of the organism. FabH from Escherichia coli and other Gram-negative organisms are selective for acetyl-CoA and produce straight-chain fatty acids, while the FabH enzymes of Gram-positive bacteria such as bacilli prefer branched-chain primers and produce branched-chain fatty acids
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evolution
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FabH is prevalent and necessary in a large number of clinical pathogens, such as Gram-positive and -negative bacteria, anaerobic bacteria, mycobacteria, chlamydia, and protozoa
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metabolism
beta-ketoacyl-acyl carrier protein synthase III, FabH, carries out first the first condensation reaction in fatty acid biosynthesis, which determines the type of fatty acid produced in bacteria
metabolism
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KASIII is involved in the biosynthesis of short-chain-length/medium-chain-length polyhydroxyalkanoate, pathway overview
metabolism
enzyme FabH catalyzes the initiation reaction of fatty acid biosynthesis
metabolism
FabB, FabF, and FabH are the condensing enzymes in te fatty acid synthesis system FAS II that play an important role in the initiation and elongation of fatty acid chains. FabB and FabF use acyl-ACPs as primers, while FabH uses acetyl-CoA as an acyl donor, which makes it unique among the FAS II condensing enymes
metabolism
FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview
metabolism
FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview
metabolism
FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview
metabolism
FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview
metabolism
FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview
metabolism
FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview
metabolism
FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview
metabolism
the beta-ketoacyl-acyl carrier protein (ACP) synthases, FabB, FabF, and FabH, catalyse the Claisen condensation of fatty acyl-thioesters and malonyl-ACP to form a 3-oxoacyl-ACP intermediate elongated by two carbon atoms. The initial cycle of elongation is catalysed by FabH, involving condensation of malonyl-ACP and acetyl-CoA, while subsequent cycles of elongation are performed by FabB or FabF
metabolism
the initiation ketosynthase FabH is the sole rate-limiting enzyme of the fatty acid synthesis of Synechococcus sp. PCC 700. Reconstitution of the fatty acid synthase system, FAS. FabH ketosynthase initiates product synthesis by condensing malonyl-ACP with acetyl-CoA to form acetoacetyl-ACP
metabolism
enzyme overexpression increases pinocembrin production in recombinant Escherichia coli
metabolism
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isoforms FabH1 and FabH2 have major roles in straight-chain fatty acid and branched-chain fatty acid biosynthesis, respectively
metabolism
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the enzyme is involved in pactamycin biosynthesis
metabolism
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the enzyme is involved in the biosynthesis of 2,5-dialkylresorcinol
metabolism
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the enzyme is involved in the biosynthesis of A33853
metabolism
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the enzyme is involved in the biosynthesis of abyssomicin
metabolism
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the enzyme is involved in the biosynthesis of aclacinomycin
metabolism
the enzyme is involved in the biosynthesis of alkylquinolone
metabolism
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the enzyme is involved in the biosynthesis of alnumycin
metabolism
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the enzyme is involved in the biosynthesis of asukamycin
metabolism
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the enzyme is involved in the biosynthesis of avilamycin
metabolism
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the enzyme is involved in the biosynthesis of benastatin
metabolism
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the enzyme is involved in the biosynthesis of calicheamicin
metabolism
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the enzyme is involved in the biosynthesis of cervimycin
metabolism
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the enzyme is involved in the biosynthesis of chlorothricin
metabolism
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the enzyme is involved in the biosynthesis of corallopyronin
metabolism
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the enzyme is involved in the biosynthesis of daunorubicin
metabolism
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the enzyme is involved in the biosynthesis of esmeraldin
metabolism
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the enzyme is involved in the biosynthesis of evernimicin
metabolism
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the enzyme is involved in the biosynthesis of FK506
metabolism
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the enzyme is involved in the biosynthesis of fredericamycin
metabolism
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the enzyme is involved in the biosynthesis of frenolicin
metabolism
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the enzyme is involved in the biosynthesis of hedamycin
metabolism
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the enzyme is involved in the biosynthesis of kijanimicin
metabolism
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the enzyme is involved in the biosynthesis of lipstatin
metabolism
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the enzyme is involved in the biosynthesis of mevalonate/terpenoid
metabolism
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the enzyme is involved in the biosynthesis of myxopyronin
metabolism
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the enzyme is involved in the biosynthesis of neocarazostatin
metabolism
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the enzyme is involved in the biosynthesis of pactamycin
metabolism
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the enzyme is involved in the biosynthesis of photopyrone
metabolism
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the enzyme is involved in the biosynthesis of reveromycin
metabolism
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the enzyme is involved in the biosynthesis of RK-682
metabolism
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the enzyme is involved in the biosynthesis of salinomycin
metabolism
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the enzyme is involved in the biosynthesis of tetracycline SF2575n
metabolism
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the enzyme is involved in the biosynthesis of tetronomycin
metabolism
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the enzyme is involved in the biosynthesis of tiacumicin
metabolism
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the enzyme is involved in the biosynthesis of tiacumicin
metabolism
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the enzyme is involved in the biosynthesis of trehangelin
metabolism
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the enzyme is involved in the biosynthesis of undecylprodiginine
metabolism
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the LstAB protein plays a role in the biosynthesis of lipstatin
metabolism
catalytic model, a structurally disordered apo-ecFabH dimer orders on binding either the first substrate, acetyl-CoA, or the inhibitor MeSSCoA, and is restored to a disordered state on binding of malonyl-ACP
metabolism
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the enzyme is involved in the biosynthesis of myxopyronin
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metabolism
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the enzyme is involved in the biosynthesis of photopyrone
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metabolism
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the enzyme is involved in the biosynthesis of pactamycin
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metabolism
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FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview
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metabolism
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the enzyme is involved in the biosynthesis of salinomycin
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metabolism
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the enzyme is involved in the biosynthesis of corallopyronin
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metabolism
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the enzyme is involved in the biosynthesis of abyssomicin
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metabolism
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the enzyme is involved in the biosynthesis of chlorothricin
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metabolism
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the enzyme is involved in the biosynthesis of esmeraldin
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metabolism
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the enzyme is involved in the biosynthesis of trehangelin
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metabolism
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the enzyme is involved in the biosynthesis of frenolicin
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metabolism
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the enzyme is involved in the biosynthesis of fredericamycin
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metabolism
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beta-ketoacyl-acyl carrier protein synthase III, FabH, carries out first the first condensation reaction in fatty acid biosynthesis, which determines the type of fatty acid produced in bacteria
-
metabolism
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isoforms FabH1 and FabH2 have major roles in straight-chain fatty acid and branched-chain fatty acid biosynthesis, respectively
-
metabolism
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FabH catalyzes the first condensation of acetyl-CoA with malonyl-ACP to form beta-ketobutyryl-ACP and CO2, initiating the cycle of fatty acid elongation, FASII pathway, detailed overview
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metabolism
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the enzyme is involved in the biosynthesis of tiacumicin
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metabolism
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the enzyme is involved in the biosynthesis of calicheamicin
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metabolism
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the enzyme is involved in the biosynthesis of cervimycin
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metabolism
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the enzyme is involved in the biosynthesis of undecylprodiginine
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metabolism
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the enzyme is involved in the biosynthesis of avilamycin
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metabolism
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the enzyme is involved in the biosynthesis of chlorothricin
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metabolism
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the enzyme is involved in the biosynthesis of esmeraldin
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metabolism
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the enzyme is involved in the biosynthesis of 2,5-dialkylresorcinol
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metabolism
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the enzyme is involved in the biosynthesis of aclacinomycin
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metabolism
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the enzyme is involved in the biosynthesis of kijanimicin
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physiological function
FabH initiates elongation in fatty acid synthesis FAS-II, type II fatty acid biosynthesis pathway overview
physiological function
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FabH is an important enzyme in the elongation steps of fatty-acid biosynthesis
physiological function
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FabH is central to the initiation of fatty acid biosynthesis
physiological function
FabH links FAS-I and FAS-II catalyzing the condensation of FAS-I-derived acyl-CoAs with malonyl-ACP. FabH represents a potential regulatory key point of the mycolic acid pathway
physiological function
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KAS III is a condensing enzyme that initiates fatty acid biosynthesis
physiological function
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the enzyme plays an important role in fatty acid synthesis initiation in Plasmodium falciparum, overview
physiological function
beta-ketoacyl-ACP-synthase III is a key condensing enzyme in the type II fatty acid synthesis system. The pathway in bacteria is essential for growth and survival
physiological function
beta-ketoacyl-acyl carrier protein synthase III (FabH) is an essential enzyme in the FASII pathway, which catalyzes the first step in the pathway, the condensation of acyl-CoA primers with malonyl-ACP
physiological function
beta-ketoacyl-acyl carrier protein synthase III (FabH) is an essential enzyme in the FASII pathway, which catalyzes the first step in the pathway, the condensation of acyl-CoA primers with malonyl-ACP
physiological function
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beta-ketoacyl-acyl carrier protein synthase is a condensing enzyme catalyzing the initial elongation step of type II fatty acid biosynthetic process and acyl carrier protein (ACP) facilitates the shuttling of the fatty acyl intermediates to the active site of the respective enzymes in the pathway
physiological function
enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway
physiological function
enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway
physiological function
enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway
physiological function
enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway
physiological function
enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway
physiological function
enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway
physiological function
enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway
physiological function
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enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway
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physiological function
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beta-ketoacyl-acyl carrier protein synthase III (FabH) is an essential enzyme in the FASII pathway, which catalyzes the first step in the pathway, the condensation of acyl-CoA primers with malonyl-ACP
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physiological function
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FabH links FAS-I and FAS-II catalyzing the condensation of FAS-I-derived acyl-CoAs with malonyl-ACP. FabH represents a potential regulatory key point of the mycolic acid pathway
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physiological function
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enzyme FabH also plays a key regulatory role through a long-chain acyl-ACP in the rate of new chain initiation of the entire synthetic pathway
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physiological function
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FabH is an important enzyme in the elongation steps of fatty-acid biosynthesis
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additional information
active site and substrate binding, ligand binding, molecular dynamics simulations and binding site mapping, detailed overview
additional information
enzyme structure and active site architecture, comparison with FabF, EC 2.3.1.179. Possible substrate and inhibitor interactions of Yersinia pestis FabH, Arg151 of YpFabH clashes with the adenine ring of CoA
additional information
FabH has a catalytic triad of Cys112/His244/Asn274
additional information
FabH has a catalytic triad of Cys112/His244/Asn274
additional information
FabH has a catalytic triad of Cys112/His244/Asn274
additional information
FabH has a catalytic triad of Cys112/His244/Asn274
additional information
FabH has a catalytic triad of Cys112/His244/Asn274
additional information
FabH has a catalytic triad of Cys112/His244/Asn274
additional information
molecular dynamics simulations to characterize the conformational space accessible to enzyme homologues under native conditions, using the FabH crystal structure PDB ID 1MZS, with a bound indole analogue inhibitor, to start. Analysis of protein-ligand interactions in the ecFabH co-crystal structure
additional information
molecular dynamics simulations to characterize the conformational space accessible to enzyme homologues under native conditions, using the FabH crystal structure PDB ID 3IL5 to start. Analysis of protein-ligand interactions in the efFabH co-crystal structure
additional information
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three-dimensional structure analysis, homology modeling and docking studies of beta-ketoacyl-ACP synthase III, FabH, enzyme involved in type II fatty acid biosynthesis of Chlorella variabilis, protein-protein docking and molecular dynamics simulation protocols. The FabH-ACP complex has the lowest docking energy score and shows the binding of ACP to the electropositive FabH surface with strong hydrogen bond interactions. The substrate-complexed FabH adopts a more stable conformation than the free enzyme. The FabH structure retains its stability throughout the simulation although noticeable displacements are observed in the loop regions. Molecular simulation studies suggest the importance of crucial hydrogen bonding of the conserved Arg91 of FabH with Glu53 and Asp56 of ACP for exhibiting high affinity between the enzyme and substrate
additional information
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FabH has a catalytic triad of Cys112/His244/Asn274
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additional information
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active site and substrate binding, ligand binding, molecular dynamics simulations and binding site mapping, detailed overview
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additional information
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molecular dynamics simulations to characterize the conformational space accessible to enzyme homologues under native conditions, using the FabH crystal structure PDB ID 3IL5 to start. Analysis of protein-ligand interactions in the efFabH co-crystal structure
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additional information
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FabH has a catalytic triad of Cys112/His244/Asn274
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