Difference between revisions of "Part:BBa K2287024"
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It is a coding sequence of glycinamide ribonucleotide synthetase that catalyzes the transformation from PRA to GAR in de novo purine biosynthesis. | It is a coding sequence of glycinamide ribonucleotide synthetase that catalyzes the transformation from PRA to GAR in de novo purine biosynthesis. | ||
− | |||
===Usage and Biology=== | ===Usage and Biology=== | ||
+ | De novo purine nucleotide synthesis is a necessary procedure in almost every organism to satisfy the basic living and reproducing needs. | ||
+ | In the prime step of the pathway, PRPP is transformed from R5P with the catalysis of Prs. An ATP provides a pyrophosphate and turns into AMP in the same procedure.(fig.1) | ||
+ | [[Image:Prs.jpg|thumb|350px|center|'''Figure 1''': phosphoribosylpyrophosphate synthase catalyzes the transformation from R5P to PRPP]] | ||
+ | The formation of PRA is the first committed step of the pathway. PurF catalyzes the attachment of an amino group to C-1 of PRPP.(fig.2) | ||
+ | [[Image:PurF.jpg|thumb|350px|center|'''Figure 2''': glutamine phosphoribosylpyrophosphate amidotransferase catalyzes the transformation from R5P to PRPP in de novo purine biosynthesis]] | ||
+ | The resulting PRA is highly volatile. Purine rings are then built up on this structure. The second step is the addition of three atoms from glycine to turn PRA into GRA, helped along by enzyme <b>PurD</b> and energy provided by an ATP.(fig.3). | ||
+ | [[Image:PurD.jpg|150px|thumb|left|'''Figure 3''': glycinamide ribonucleotide synthetase catalyzes the transformation from PRA to GAR in de novo purine biosynthesis]] | ||
+ | Then N10-formyltetrahydrofolate formylates the glycine amino group which turns GAR into FGAR, and a nitrogen is contributed by glutamine transforming FGAR to FGAM, before dehydration and ring closure yield the AIR by PurM.(fig.4) | ||
+ | [[Image:PurM.jpg|150px|thumb|right|'''Figure 4''': aminoimidazole ribonucleotide synthetase catalyzes the transformation from FGAM to AIR in de novo purine biosynthesis]] | ||
+ | To complete the second ring in the purine structure, a carboxyl group is first added and transforms AIR into CAIR. Then, CAIR is transformed into SACAIR with enzyme PurC and energy provided by an ATP.(fig.5) | ||
+ | [[Image:PurC.jpg|thumb|350px|center|'''Figure 5''': succinylaminoimidazolecarboxamide ribonucleotide synthetase catalyzes the transformation from CAIR to SAICAR in de novo purine biosynthesis]] | ||
+ | After another 3 steps, we have the first intermediate with a complete purine ring is inosinate (IMP). The total pathway of de novo purine biosynthesis is showed below.(fig.6) | ||
+ | [[Image:Overproduce.jpg|thumb|350px|center|'''Figure 6''': The total pathway of de novo purine biosynthesis]] | ||
+ | We overexpressed PurD to achieve the mass synthesis of purine. Consequently, more purines than before participant in the circuits we designed and were used to synthesize uric acid when co-expressed with [https://parts.igem.org/Part:BBa_K2287022 rhXOR]. | ||
+ | |||
+ | ===References=== | ||
+ | 1.Lehninger, A. L., Nelson, D. L. 1., & Cox, M. M. (2008). Lehninger principles of biochemistry (5th ed.). New York ; New Delhi: W.H. Freeman.<br> | ||
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<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> |
Latest revision as of 14:17, 1 November 2017
purD
It is a coding sequence of glycinamide ribonucleotide synthetase that catalyzes the transformation from PRA to GAR in de novo purine biosynthesis.
Usage and Biology
De novo purine nucleotide synthesis is a necessary procedure in almost every organism to satisfy the basic living and reproducing needs. In the prime step of the pathway, PRPP is transformed from R5P with the catalysis of Prs. An ATP provides a pyrophosphate and turns into AMP in the same procedure.(fig.1)
The formation of PRA is the first committed step of the pathway. PurF catalyzes the attachment of an amino group to C-1 of PRPP.(fig.2)
The resulting PRA is highly volatile. Purine rings are then built up on this structure. The second step is the addition of three atoms from glycine to turn PRA into GRA, helped along by enzyme PurD and energy provided by an ATP.(fig.3).
Then N10-formyltetrahydrofolate formylates the glycine amino group which turns GAR into FGAR, and a nitrogen is contributed by glutamine transforming FGAR to FGAM, before dehydration and ring closure yield the AIR by PurM.(fig.4)
To complete the second ring in the purine structure, a carboxyl group is first added and transforms AIR into CAIR. Then, CAIR is transformed into SACAIR with enzyme PurC and energy provided by an ATP.(fig.5)
After another 3 steps, we have the first intermediate with a complete purine ring is inosinate (IMP). The total pathway of de novo purine biosynthesis is showed below.(fig.6)
We overexpressed PurD to achieve the mass synthesis of purine. Consequently, more purines than before participant in the circuits we designed and were used to synthesize uric acid when co-expressed with rhXOR.
References
1.Lehninger, A. L., Nelson, D. L. 1., & Cox, M. M. (2008). Lehninger principles of biochemistry (5th ed.). New York ; New Delhi: W.H. Freeman.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 789
Illegal AgeI site found at 1029 - 1000COMPATIBLE WITH RFC[1000]