Difference between revisions of "Team:NPU-China/BasicParts"

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                         2.5.1.66. CEAS is a TPP-related enzyme, can catalyze the condensation of D-G3P and L-Arg with the
 
                         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,
 
                         involvement of TPP and magnesium ions (thiamine pyrophosphate) to produce N2- (2-carboxyethyl) arginine,
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                         which will continue to participate in the biosynthesis of clavulanic acid as the first intermediate.
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                         which will continue to participate in the biosynthesis of clavulanic acid as the first intermediate.<br>
−
                         According to the earlier literature, CEAS (N2-(2-carboxyethyl) arginine synthase) was a synergistic
+
                          <img src="https://static.igem.org/mediawiki/2017/a/ac/Ceas2.png" class="img-responsive">
 +
                         <br>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
 
                         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
 
                         and L-Arg, which was catalyzed by Ceas1 and Ceas2. The process would be accompanied by the formation

Revision as of 17:59, 1 November 2017

/* Table */

Name Type Description Length
BBa_K2347000 Coding DHAP/G3P->acrylic acid 1719bp
BBa_K2347001 Coding glycerol->DHA 1113bp
BBa_K2347002 Coding DHA->DHAP 1827bp
BBa_K2347003 Coding H2O2->O2 1584bp
BBa_K2347004 Coding NADH->NAD+ 618bp

Our best basic part, ceaS2

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.