Difference between revisions of "Part:BBa K2086001"

(Usage and Biology)
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<partinfo>BBa_K2086001 short</partinfo>
 
<partinfo>BBa_K2086001 short</partinfo>
  
The E. coli serA gene encodes the D-3-phosphoglycerate dehydrogenase, which catalyzes the first committed step in the biosynthesis of serine.  Serine is an essential amino acid for E. coli growth in minimal medium.  Deletion of the serA gene leads to a serine auxotroph, which can be rescued either by the expression of a protein with the same catalytic activity as SerA or by the addition of serine in the growth media.
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The E. coli serA gene encodes the D-3-phosphoglycerate dehydrogenase, which catalyzes the first committed step in the biosynthesis of serine.  Serine is an essential amino acid for E. coli growth in minimal medium.  Deletion of the serA gene leads to a serine auxotroph, which can be rescued either by the expression of a protein with the same catalytic activity as SerA or by the addition of serine in the growth media.  
  
  
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===Usage and Biology===
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===Biology and Our Application===
 
[[Image:T--UNebraska-Lincoln--Biosynthesis.gif|450px|thumb|right|'''Figure 1:''' The serine biosynthesis pathway. Provided by: EcoCyc, a member of the BioCyc database collection http://ecocyc.org/ECOLI/NEW-IMAGE?type=PATHWAY&object=SERSYN-PWY&show-citations=NIL]]
 
[[Image:T--UNebraska-Lincoln--Biosynthesis.gif|450px|thumb|right|'''Figure 1:''' The serine biosynthesis pathway. Provided by: EcoCyc, a member of the BioCyc database collection http://ecocyc.org/ECOLI/NEW-IMAGE?type=PATHWAY&object=SERSYN-PWY&show-citations=NIL]]
Serine is an amino acid produced in <i>E. coli</i> K12 through the metabolic pathway shown in <b>Figure 1</b>. The SerA gene codes for D-3-Phosphoglycerate Dehydrogenase, the enzyme responsible for catalyzing the committed step of serine biosynthesis. Without SerA, <i>E. coli</i> are unable to grow without sufficient supplementation of other amino acids [1].
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Serine is an amino acid produced in <i>E. coli</i> K12 through the metabolic pathway shown in <b>Figure 1</b>. The SerA gene codes for D-3-Phosphoglycerate Dehydrogenase, the enzyme responsible for catalyzing the committed step of serine biosynthesis. Without SerA, <i>E. coli</i> are unable to grow without sufficient supplementation of other amino acids [1].  
  
 
[1]. PAULA D. RAVNIKAR AND RONALD L. SOMERVILLE: Genetic Characterization of a Highly Efficient Alternate Pathway of
 
[1]. PAULA D. RAVNIKAR AND RONALD L. SOMERVILLE: Genetic Characterization of a Highly Efficient Alternate Pathway of

Revision as of 21:37, 16 October 2016


Serine Repeat Antigen (SerA)

The E. coli serA gene encodes the D-3-phosphoglycerate dehydrogenase, which catalyzes the first committed step in the biosynthesis of serine. Serine is an essential amino acid for E. coli growth in minimal medium. Deletion of the serA gene leads to a serine auxotroph, which can be rescued either by the expression of a protein with the same catalytic activity as SerA or by the addition of serine in the growth media.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 293
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Biology and Our Application

Figure 1: The serine biosynthesis pathway. Provided by: EcoCyc, a member of the BioCyc database collection http://ecocyc.org/ECOLI/NEW-IMAGE?type=PATHWAY&object=SERSYN-PWY&show-citations=NIL

Serine is an amino acid produced in E. coli K12 through the metabolic pathway shown in Figure 1. The SerA gene codes for D-3-Phosphoglycerate Dehydrogenase, the enzyme responsible for catalyzing the committed step of serine biosynthesis. Without SerA, E. coli are unable to grow without sufficient supplementation of other amino acids [1].

[1]. PAULA D. RAVNIKAR AND RONALD L. SOMERVILLE: Genetic Characterization of a Highly Efficient Alternate Pathway of Serine Biosynthesis in Escherichia coli. http://jb.asm.org/content/169/6/2611.full.pdf