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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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A single amino acid substitution (Asp leads to Asn) in a phosphoglycerate kinase variant (PGK München) associated with enzyme deficiency.

The structural abnormality of the phosphoglycerate kinase variant, PGK München, associated with red cell enzyme deficiency and heat instability, was elucidated by a microscale peptide-mapping method. A single amino acid substitution, from aspartic acid in the normal enzyme to asparagine in the variant enzyme, was found. From the known amino acid sequence of normal human phosphoglycerate kinase, the substitution is in the aspartic acid residue located at 268th position from the NH2-terminal of the protein.[1]

References

  1. A single amino acid substitution (Asp leads to Asn) in a phosphoglycerate kinase variant (PGK München) associated with enzyme deficiency. Fujii, H., Krietsch, W.K., Yoshida, A. J. Biol. Chem. (1980) [Pubmed]
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