Information on EC 2.5.1.66 - N2-(2-carboxyethyl)arginine synthase

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The expected taxonomic range for this enzyme is: Streptomyces clavuligerus

EC NUMBER
COMMENTARY hide
2.5.1.66
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RECOMMENDED NAME
GeneOntology No.
N2-(2-carboxyethyl)arginine synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
D-glyceraldehyde 3-phosphate + L-arginine = N2-(2-carboxyethyl)-L-arginine + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C-N bond formation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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clavulanate biosynthesis
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Clavulanic acid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
glyceraldehyde-3-phosphate:L-arginine N2-(2-hydroxy-3-oxopropyl) transferase (2-carboxyethyl-forming)
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.
CAS REGISTRY NUMBER
COMMENTARY hide
250207-48-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate + L-arginine
N2-(2-carboxyethyl)-L-arginine + phosphate
show the reaction diagram
D-glyceraldehyde 3-phosphate + L-lysine
N2-(2-carboxyethyl)-L-lysine + phosphate
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-glyceraldehyde 3-phosphate + L-arginine
N2-(2-carboxyethyl)-L-arginine + phosphate
show the reaction diagram
D-glyceraldehyde 3-phosphate + L-lysine
N2-(2-carboxyethyl)-L-lysine + phosphate
show the reaction diagram
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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requirement
thiamine diphosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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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
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
59078
x * 59078, CeaS1, sequence calculation
60776
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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
130000
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dimer, CEAS exists in two oligomeric solution states, gel filtration
240000
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tetramer, CEAS exists in two oligomeric solution states, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 59078, CeaS1, sequence calculation
dimer
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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
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CEAS complexed with thiamine diphosphate and Mg2+, selenomethionine-substituted CEAS, vapor diffusion method, X-ray analysis
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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
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant CEAS
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cea S gene of the gene cluster for clavulanic acid biosynthesis, genomic organization
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ceas gene, expression in Escherichia coli BL21(DE3), first gene in the clavulanic acid cluster, orf2
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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
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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; 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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information