Literature summary for 2.5.1.66 extracted from

Caines, M.E.C.; Elkins, J.M.; Hewitson, K.S.; Schofield, C.J.
Crystal structure and mechanistic implications of N2-(2-carboxyethyl)arginine synthase, the first enzyme in the clavulanic acid biosynthesis pathway (2004), J. Biol. Chem., 279, 5685-5692.

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Cloned(Commentary)

Cloned (Comment)	Organism
ceas gene, expression in Escherichia coli BL21(DE3), first gene in the clavulanic acid cluster, orf2	Streptomyces clavuligerus

Crystallization (Commentary)

Crystallization (Comment)	Organism
CEAS complexed with thiamine diphosphate and Mg2+, selenomethionine-substituted CEAS, vapor diffusion method, X-ray analysis	Streptomyces clavuligerus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	cofactor, present at the active site, mode of binding, formation of a complex with a single Mg2+ ion facilitates binding of thiamine diphosphate	Streptomyces clavuligerus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
60776	-	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	Streptomyces clavuligerus
60776	-	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	Streptomyces clavuligerus
130000	-	dimer, CEAS exists in two oligomeric solution states, gel filtration	Streptomyces clavuligerus
240000	-	tetramer, CEAS exists in two oligomeric solution states, gel filtration	Streptomyces clavuligerus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
D-glyceraldehyde 3-phosphate + L-arginine	Streptomyces clavuligerus	first enzyme in the clavulanic acid biosynthesis pathway	N2-(2-carboxyethyl)-L-arginine + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Streptomyces clavuligerus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant CEAS	Streptomyces clavuligerus

Reaction

Reaction	Comment	Organism	Reaction ID
D-glyceraldehyde 3-phosphate + L-arginine = N2-(2-carboxyethyl)-L-arginine + phosphate	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	Streptomyces clavuligerus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-glyceraldehyde 3-phosphate + L-arginine	first enzyme in the clavulanic acid biosynthesis pathway	Streptomyces clavuligerus	N2-(2-carboxyethyl)-L-arginine + phosphate	-	?
D-glyceraldehyde 3-phosphate + L-arginine	CEAS structure, substrate binding sites, detailed mechanism	Streptomyces clavuligerus	N2-(2-carboxyethyl)-L-arginine + phosphate	-	?

Subunits

Subunits	Comment	Organism
dimer	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	Streptomyces clavuligerus
tetramer	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	Streptomyces clavuligerus

Synonyms

Synonyms	Comment	Organism
CEA synthetase	-	Streptomyces clavuligerus
CEAS	-	Streptomyces clavuligerus
N2-(2-carboxyethyl)arginine synthetase	-	Streptomyces clavuligerus

Cofactor

Cofactor	Comment	Organism	Structure
thiamine diphosphate	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	Streptomyces clavuligerus

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Release 2023.1 (January 2023)