Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0348321 (Haemophilus)
 15,372 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of a commercially available, chemically defined enrichment (Iso-VitaleX; BBL Microbiology Systems, Cockeysville, Md.) on the growth of 10 strains of Haemophilus somnus was studied. A 6- to 10-fold increase in growth, as measured turbidimetrically, was observed when Iso VitaleX was added to a basal medium of brain heart infusion broth to a final concentration of 1% (vol/vol). Thiamine pyrophosphate (cocarboxylase), a constituent component of Iso VitaleX, was found to be the only growth-promoting factor, and it could be used as a substitute for Iso VitaleX. An equimolar concentration (2.2 microM) of thiamine monophosphate promoted growth equal to that of thiamine pyrophosphate. Thiamine was nonstimulatory for all 10 strains tested. When alkaline thermal-treated brain heart infusion broth was used as the basal medium, 7 of the 10 strains had an absolute requirement for thiamine monophosphate or thiamine pyrophosphate. The three remaining strains showed minimal growth when thiamine was added to this basal medium; however, excellent growth was observed when thiamine monophosphate or thiamine pyrophosphate was utilized. Factor X (hemin) was found to further enhance the growth when concentrations of 5 to 10 micrograms/ml were coupled with thiamine pyrophosphate. No increase in growth was observed when factor V (nicotinamide adenine dinucleotide) was coupled with thiamine pyrophosphate. This is the first report of a growth factor requirement for H. somnus.
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PMID:Thiamine pyrophosphate (cocarboxylase) as a growth factor for Haemophilus somnus. 727 48

Acetohydroxyacid synthase (AHAS; EC 2.2.1.6) is a thiamin diphosphate- (ThDP)- and FAD-dependent enzyme that catalyzes the first common step in the biosynthetic pathway of the branched-amino acids (BCAAs) leucine, isoleucine, and valine. The gene from Haemophilus influenzae that encodes the AHAS catalytic subunit was cloned, overexpressed in Escherichia coli BL21(DE3), and purified to homogeneity. The purified H. influenzae AHAS catalytic subunit (Hin-AHAS) appeared as a single band on SDS-PAGE gel, with a molecular mass of approximately 63 kDa. The enzyme catalyzes the condensation of two molecules of pyruvate to form acetolactate, with a K(m) of 9.2mM and the specific activity of 1.5 micromol/min/mg. The cofactor activation constant (K(c)=13.5 microM) and the dissociation constant (K(d)=3.3 microM) of ThDP were also determined by enzymatic assay and tryptophan fluorescence quenching studies, respectively. We screened a chemical library to discover new inhibitors of the Hin AHAS catalytic subunit. Through which, AVS-2087 (IC(50)=0.53 microM), KSW30191 (IC(50)=1.42 microM), and KHG20612 (IC(50)=4.91 microM) displayed potent inhibition as compare to sulfometuron methyl (IC(50)=276.31 microM).
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PMID:Identification of the catalytic subunit of acetohydroxyacid synthase in Haemophilus influenzae and its potent inhibitors. 1771 99