Difference between revisions of "Part:BBa K2287021"
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De novo purine nucleotide synthesis is a necessary procedure in almost every organism to satisfy the basic living and reproducing needs. | 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 <b>Prs</b>. An ATP provides a pyrophosphate and turns into AMP in the same procedure.(fig.1) | In the prime step of the pathway, PRPP is transformed from R5P with the catalysis of <b>Prs</b>. An ATP provides a pyrophosphate and turns into AMP in the same procedure.(fig.1) | ||
− | [[Image:Prs.jpg|thumb|350px|'''Figure 1''': phosphoribosylpyrophosphate synthase catalyzes the transformation from R5P to PRPP]] | + | [[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) | 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|'''Figure 2''': glutamine phosphoribosylpyrophosphate amidotransferase catalyzes the transformation from R5P to PRPP in de novo purine biosynthesis]] | + | [[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 PurD and energy provided by an ATP.(fig.3). | 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). | ||
− | [[Image:PurD.jpg| | + | [[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) | 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| | + | [[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) | 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|'''Figure 5''': succinylaminoimidazolecarboxamide ribonucleotide synthetase catalyzes the transformation from CAIR to SAICAR in de novo purine biosynthesis]] | + | [[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) | 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|'''Figure 6''': The total pathway of de novo purine biosynthesis]] | + | [[Image:Overproduce.jpg|thumb|350px|center|'''Figure 6''': The total pathway of de novo purine biosynthesis]] |
− | + | ||
We overexpressed Prs 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. | We overexpressed Prs 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=== | ===References=== |
Revision as of 14:10, 1 November 2017
prs
This is the coding sequence of phosphoribosylpyrophosphate synthase that catalyzes the transformation from R5P to PRPP 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 Prs 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]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]