Difference between revisions of "Part:BBa K1790002"
 
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YniC is a sugar phosphatase belonging to the superfamily of haloacid dehalogenase (HAD)-like hydrolases. Its preferred substrate is 2-deoxyglucose-6-phosphate. The phosphatase activity of YniC was first discovered in a high-throughput screen of purified proteins.  
 
YniC is a sugar phosphatase belonging to the superfamily of haloacid dehalogenase (HAD)-like hydrolases. Its preferred substrate is 2-deoxyglucose-6-phosphate. The phosphatase activity of YniC was first discovered in a high-throughput screen of purified proteins.  
 
Phosphatase activity of YniC is dependent on the presence of a divalent cation such as Mg2+, which appears to affect substrate binding.  
 
Phosphatase activity of YniC is dependent on the presence of a divalent cation such as Mg2+, which appears to affect substrate binding.  
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Mutagenesis of the predicted catalytic Asp residues in YniC results in loss of phosphatase activity. A yniC deletion mutant is more sensitive to the presence of 2-deoxyglucose in the growth medium than wild type, while a strain overexpressing yniC tolerates higher concentrations of 2-deoxyglucose. 2-deoxyglucose is taken up by E. coli and is phosphorylated to 2-deoxyglucose-6P, a toxic analog of glucose-6P.
 
  
 
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Latest revision as of 03:48, 12 September 2015

HAD

YniC is a sugar phosphatase belonging to the superfamily of haloacid dehalogenase (HAD)-like hydrolases. Its preferred substrate is 2-deoxyglucose-6-phosphate. The phosphatase activity of YniC was first discovered in a high-throughput screen of purified proteins. Phosphatase activity of YniC is dependent on the presence of a divalent cation such as Mg2+, which appears to affect substrate binding.

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GlnH

The GlnHPQ high-affinity glutamine transport system is a member of the ATP-Binding Cassette (ABC) Superfamily of transporters. Based on sequence similarity, GlnH is the periplasmic glutamine-binding protein, GlnQ is the ATP-binding component, and GlnP is the membrane component of the ABC transporter.


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