Team:NPU-China/BasicParts

/* Table */

Name	Type	Description	Length
BBa_K2347005	Coding	DHAP/G3P->acrylic acid	1719bp
BBa_K2347006	Coding	glycerol->DHA	1113bp
BBa_K2347007	Coding	DHA->DHAP	1827bp
BBa_K2347008	Coding	NADH->NAD+	618bp

CEAS, which is N2- (2-carboxyethyl) arginine synthase, is an enzyme in Streptomyces clavuligerus, EC 2.5.1.66. CEAS is a TPP-related enzyme, can catalyze the condensation of D-G3P and L-Arg with the involvement of TPP and magnesium ions (thiamine pyrophosphate) to produce N2- (2-carboxyethyl) arginine, which will continue to participate in the biosynthesis of clavulanic acid as the first intermediate. According to the earlier literature, CEAS (N2-(2-carboxyethyl) arginine synthase) was a synergistic effect of Ceas1 and Ceas, namely, N2- (2-carboxyethyl) arginine came from the condensation of G3P and L-Arg, which was catalyzed by Ceas1 and Ceas2. The process would be accompanied by the formation of acrylic acid[1]. But with the deepening of the study, Matthew E.C. Caines found that Ceas2 played the main role in the catalytic process. And they speculated the catalytic mechanism of Ceas2, as shown below [2].

[1] MERSKI M, TOWNSEND C A. Observation of an Acryloyl–Thiamin Diphosphate Adduct in the First Step of Clavulanic Acid Biosynthesis [J]. Journal of the American Chemical Society, 2007, 129(51): 15750-1.
[2] CAINES M E, ELKINS J M, HEWITSON K S, et al. Crystal structure and mechanistic implications of N2-(2-carboxyethyl)arginine synthase, the first enzyme in the clavulanic acid biosynthesis pathway [J]. Journal of Biological Chemistry, 2004, 279(7): 5685-92.