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Literature summary for 2.3.1.37 extracted from

  • Cheltsov, A.V.; Guida, W.C.; Ferreira, G.C.
    Circular permutation of 5-aminolevulinate synthase: effect on folding, conformational stability, and structure (2003), J. Biol. Chem., 278, 27945-27955.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information circularly permuted enzyme variants with N-terminal amino acids corrosponding to L25, Q69, N404, N408 and a monomeric protein consisting of two wild-type enzyme subunits covalently linked through the N-terminus of one subunit to the C-terminuns of the other. Analysis of guanidine hydrochloride-induced unfolding, conformational stability, and structure Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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Renatured (Commentary)

Renatured (Comment) Organism
complete reversibility of guanidine hydrochloride-induced unfolding Mus musculus