The enzyme requires thiamine diphosphate and catalyses the first step in the clavulanic-acid-biosynthesis pathway. The 2-hydroxy-3-oxo group transferred from glyceraldehyde 3-phosphate is isomerized during transfer to form the 2-carboxyethyl group.
the enzyme requires thiamine diphosphate and catalyses the first step in the clavulanic-acid-biosynthesis pathway, the 2-hydroxy-3-oxo group transferred from glyceraldehyde 3-phosphate is isomerized during transfer to form the 2-carboxyethyl group, detailed mechanism
The enzyme requires thiamine diphosphate and catalyses the first step in the clavulanic-acid-biosynthesis pathway. The 2-hydroxy-3-oxo group transferred from glyceraldehyde 3-phosphate is isomerized during transfer to form the 2-carboxyethyl group.
N2-(2-carboxyethyl)-L-arginine is the immediate precursor to the first beta-lactam during the biosynthesis of the clinically important serine beta-lactamase inhibitor, clavulanic acid, in Streptomyces clavuligerus
CEAS catalyzes the first reaction in the shared biosynthetic pathway leading to clavulanic acid and 5S clavams, ceaS1 and ceaS2 genes are regulated by different mechanisms, ceaS1 may be more closely associated with the production of 5S clavams via a CcaR-independent pathway, whereas ceaS2 is associated with clavulanic acid production and is regulated by the transcriptional activator CcaR
N2-(2-carboxyethyl)-L-arginine is the immediate precursor to the first beta-lactam during the biosynthesis of the clinically important serine beta-lactamase inhibitor, clavulanic acid, in Streptomyces clavuligerus
CEAS catalyzes the first reaction in the shared biosynthetic pathway leading to clavulanic acid and 5S clavams, ceaS1 and ceaS2 genes are regulated by different mechanisms, ceaS1 may be more closely associated with the production of 5S clavams via a CcaR-independent pathway, whereas ceaS2 is associated with clavulanic acid production and is regulated by the transcriptional activator CcaR
thiamine diphosphate-dependent enzyme, the thiamine diphosphate binding region is situated across two subunits of the closely associated dimer, two binding regions per dimer, binding is facilitated by a combination of hydrogen bonding and formation of a complex with a single Mg2+ ion, mode of binding, CEAS must rely heavily on the cofactor for general acid/base catalysis
analysis of the nutritional regulation of ceaS1 and ceaS2 expression, ceaS1 is transcribed in complex soy medium only, whereas ceaS2 is transcribed in both soy and defined starch-asparagine media
deletion of the gene encoding isoform ceaS1 results in complete loss of clavam biosynthesis when grown in liquid soy medium. The failure to produce clavam metabolites is due to reduced or abolished transcription of isoform ceaS1 in the ceaS2 mutants. When the same mutants are grown on solid soy medium, clavam production is restored and ceaS1 is produced, albeit at low levels compared to the wild-type
2 * 60776, electrospray ionization mass spectrometry and sequence calculation without the N-terminal methionine, CEAS exists in two oligomeric solution states, monomer structure, subunit interactions
4 * 60776, electrospray ionization mass spectrometry and sequence calculation without the N-terminal methionine, dimer of two more tightly associated dimers, CEAS exists in two oligomeric solution states, monomer structure, subunit interactions
2 * 60776, electrospray ionization mass spectrometry and sequence calculation without the N-terminal methionine, CEAS exists in two oligomeric solution states, monomer structure, subunit interactions
4 * 60776, electrospray ionization mass spectrometry and sequence calculation without the N-terminal methionine, dimer of two more tightly associated dimers, CEAS exists in two oligomeric solution states, monomer structure, subunit interactions
crystal structures of tetrameric CEAS-thiamin diphosphate in complex with the substrate analogues 5-guanidinovaleric acid and tartrate, crystals of 2 morphologies are grown by the hanging-drop vapour diffusion technique using 1.6 M ammonium sulfate as precipitant, in the presence of 0.1 M HEPES, pH 7.4, and a 3fold molar excess of thiamin diphosphate
ceaS1 mutants with reduced clavulanic acid production compared with wild-type strain, ceaS1/ceaS2 double mutants and ceaS2 frameshift mutants with completely blocked clavulanic acid biosynthesis
ceaS1 mutants with reduced clavulanic acid production compared with wild-type strain, ceaS1/ceaS2 double mutants and ceaS2 frameshift mutants with completely blocked clavulanic acid biosynthesis
ceaS1 and ceaS2, ceaS2 is located in the clavulanic acid gene cluster, ceaS1 in the paralogue gene cluster, study of the transcriptional regulation of the genes
Streptomyces venezuelae YJ028 is utilized as the heterologous host for the expression of four structural clavulanic acid biosynthesis genes, which encode carboxyethylarginine synthase (ceas2), beta-lactam synthetase (bls2), clavaminate synthase (cas2), and proclavaminate amidinohydrolase (pah2). The genes are cloned into pIBR25 expression vector containing ermE promoter to generate pBS4. The cas2 gene is also cloned into pSET152 to generate pCas2. It is then integrated into the genome of Streptomyces venezuelae YJ028
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcription of isoform ceaS1 is reduced or abolished in isoform ceaS2 mutants grown in liquid soy medium, despite the location of ceaS1 on a replicon completely separate from that of ceaS2. In addition, the CeaS1 protein as well as the CeaS2 protein is absent from the ceaS2 mutants. When the mutants are grown on solid soy medium, clavam production is restored and CeaS1 is produced, albeit at low levels compared to the wild type
transcription of isoform ceaS1 is reduced or abolished in isoform ceaS2 mutants grown in liquid soy, despite the location of ceaS1 on a replicon completely separate from that of ceaS2. In addition, the CeaS1 protein as well as the CeaS2 protein is absent from the ceaS2 mutants. When the mutants are grown on solid soy medium, clavam production is restored and CeaS1 is produced, albeit at low levels compared to the wild type
clavulanic acid intermediates: deoxygaunidinoproclavaminic acid, guanidinoproclavaminic acid, and dihydroclavaminic acid are heterologously produced in Streptomyces venezuelae recombinant using four sets of early genes from the clavulanic acid biosynthetic pathway
in an industrial clavulanic acid-overproducer Streptomyces clavuligerus DEPA, carboxyethylarginine synthase (Ceas2), clavaldehyde dehydrogenase (Car) and carboxyethyl-arginine betalactam synthase (Bls2) are overrepesented, whereas the enzymes of two other secondary metabolites are underrepresented
Tahlan, K.; Park, H.U.; Wong, A.; Beatty, P.H.; Jensen, S.E.
Two sets of paralogous genes encode the enzymes involved in the early stages of clavulanic acid and clavam metabolite biosynthesis in Streptomyces clavuligerus
An rplKDelta29-PALG-32 mutation leads to reduced expression of the regulatory genes ccaR and claR and very low transcription of the ceaS2 gene for clavulanic acid biosynthesis in Streptomyces clavuligerus