codon-optimized orf encoding a. fulgidus cofe Search Results


codon-optimized orf encoding a. fulgidus cofe  (GenScript corporation)
90
GenScript corporation codon-optimized orf encoding a. fulgidus cofe
A poly-γ-glutamate tail is shown with variable L -glutamate numbers and terminated by a non-reactive nitro functional group. Calculated masses of nitro-terminated folate and F 420 molecules are provided for comparison to experimental results – the central number indicates the total residue count in the tail including the chain terminator residue. The masses take into account functional group protonation within the mass spectrometer operating in positive ion mode and are provided to 4 decimal places to match the precision of the high-resolution LC-MS experiment. The table of data provides the identity and experimentally measured masses of substrate, predominant polyglutamylated product, and nitro-terminated product. Enzymes systems investigated are human FPGS (hFPGS), Mycobacterium tuberculosis FPGS ( Mtb -FPGS), Archaeoglobus <t>fulgidus</t> <t>CofE</t> ( Af -CofE), and Mycobacterium tuberculosis FbiB ( Mtb -FbiB).
Codon Optimized Orf Encoding A. Fulgidus Cofe, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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codon-optimized orf encoding a. fulgidus cofe - by Bioz Stars, 2026-06
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A poly-γ-glutamate tail is shown with variable L -glutamate numbers and terminated by a non-reactive nitro functional group. Calculated masses of nitro-terminated folate and F 420 molecules are provided for comparison to experimental results – the central number indicates the total residue count in the tail including the chain terminator residue. The masses take into account functional group protonation within the mass spectrometer operating in positive ion mode and are provided to 4 decimal places to match the precision of the high-resolution LC-MS experiment. The table of data provides the identity and experimentally measured masses of substrate, predominant polyglutamylated product, and nitro-terminated product. Enzymes systems investigated are human FPGS (hFPGS), Mycobacterium tuberculosis FPGS ( Mtb -FPGS), Archaeoglobus fulgidus CofE ( Af -CofE), and Mycobacterium tuberculosis FbiB ( Mtb -FbiB).

Journal: Nature Communications

Article Title: Poly-γ-glutamylation of biomolecules

doi: 10.1038/s41467-024-45632-1

Figure Lengend Snippet: A poly-γ-glutamate tail is shown with variable L -glutamate numbers and terminated by a non-reactive nitro functional group. Calculated masses of nitro-terminated folate and F 420 molecules are provided for comparison to experimental results – the central number indicates the total residue count in the tail including the chain terminator residue. The masses take into account functional group protonation within the mass spectrometer operating in positive ion mode and are provided to 4 decimal places to match the precision of the high-resolution LC-MS experiment. The table of data provides the identity and experimentally measured masses of substrate, predominant polyglutamylated product, and nitro-terminated product. Enzymes systems investigated are human FPGS (hFPGS), Mycobacterium tuberculosis FPGS ( Mtb -FPGS), Archaeoglobus fulgidus CofE ( Af -CofE), and Mycobacterium tuberculosis FbiB ( Mtb -FbiB).

Article Snippet: The codon-optimized ORF encoding A. fulgidus CofE was synthesized and cloned (GenScript) into pProEX-HTb for expression in E. coli BL21 (DE3) LOBSTR cells .

Techniques: Functional Assay, Comparison, Residue, Mass Spectrometry, Liquid Chromatography with Mass Spectroscopy