Search results for "Acyl carrier protein"

showing 3 items of 3 documents

Citrate lyases of lactic acid bacteria

1998

Citrate Iyase is a key enzyme of the citrate metabolism which is involved in flavor and texture of many fermented milk products. Citrate Iyase which catalyses the cleavage of citrate into oxaloacetate and acetate is a multienzyme complex composed of three proteins: an acyl carrier protein (ACP); a citrate, acetate-ACP transferase; and a citryl-S-ACP Iyase. The citrate Iyase is active only when the thioester residue of the prosthetic group bound to ACP is acetylated. In the presence of citrate, the transferase mediates the formation of citryl-S-acyl carrier protein by acyl exchange and liberation of acetate. Then the Iyase subunit cleaves the citryl-S-ACP with libe- ration of oxaloacetate an…

biologyATP citrate lyasefood and beverages[SDV.IDA] Life Sciences [q-bio]/Food engineeringbiology.organism_classificationCofactorLactic acidchemistry.chemical_compoundAcyl carrier protein[SDV.AEN] Life Sciences [q-bio]/Food and NutritionBiochemistrychemistryLeuconostoc mesenteroidesbiology.proteinTransferaseLeuconostocCitrate synthaselipids (amino acids peptides and proteins)ComputingMilieux_MISCELLANEOUSFood Science
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Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster

1998

ABSTRACT A citrate lyase (EC 4.1.3.6 ) was purified 25-fold from Leuconostoc mesenteroides and was shown to contain three subunits. The first 42 amino acids of the β subunit were identified, as well as an internal peptide sequence spanning some 20 amino acids into the α subunit. Using degenerated primers from these sequences, we amplified a 1.2-kb DNA fragment by PCR from Leuconostoc mesenteroides subsp. cremoris . This fragment was used as a probe for screening a Leuconostoc genomic bank to identify the structural genes. The 2.7-kb gene cluster encoding citrate lyase of L. mesenteroides is organized in three open reading frames, citD , citE , and citF , encoding, respectively, the three ci…

DNA BacterialATP citrate lyaseMolecular Sequence DataGene ExpressionBiologymedicine.disease_causeMicrobiologyBacterial ProteinsCarbon-Sulfur LigasesMultienzyme ComplexesGene clusterAcyl Carrier ProteinEscherichia colimedicineLeuconostocAmino Acid SequenceCloning MolecularMolecular BiologyEscherichia coliBase SequenceSequence Homology Amino AcidStructural geneOxo-Acid-LyasesSequence Analysis DNALyasebiology.organism_classificationEnzymes and ProteinsMolecular biologyOxaloacetate decarboxylaseBiochemistryGenes BacterialLeuconostoc mesenteroidesMultigene FamilyCoenzyme A-TransferasesLeuconostoc
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2015

Bacterial infections remain a serious health concern, in particular causing life-threatening infections of hospitalized and immunocompromised patients. The situation is exacerbated by the rise in antibacterial drug resistance, and new treatments are urgently sought. In this endeavour, accurate structures of molecular targets can support early-stage drug discovery. Here, crystal structures, in three distinct forms, of recombinantPseudomonas aeruginosaβ-ketoacyl-(acyl-carrier-protein) synthase II (FabF) are presented. This enzyme, which is involved in fatty-acid biosynthesis, has been validated by genetic and chemical means as an antibiotic target in Gram-positive bacteria and represents a po…

Gram-negative bacteriabiologyAcyl carrier protein synthaseStereochemistryDrug discoveryPlatensimycinBiophysicsActive sitePlasma protein bindingCondensed Matter Physicsbiology.organism_classificationLigand (biochemistry)Biochemistry3. Good healthchemistry.chemical_compoundchemistryBiochemistryStructural BiologyGeneticsbiology.proteinBinding siteActa Crystallographica Section F Structural Biology Communications
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