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Literature summary for 3.1.2.6 extracted from

  • Dragani, B.; Cocco, R.; Ridderstroem, M.; Stenberg, G.; Mannervik, B.; Aceto, A.
    Unfolding and refolding of human glyoxalase II and its single-tryptophan mutants (1999), J. Mol. Biol., 291, 481-490.
    View publication on PubMed
Search for more literature for 3.1.2.6

Protein Variants

Protein Variants Comment Organism
W199F mid-point of unfolding transition curve is not very different from that of wild-type. Stability of the active site is slightly affected Homo sapiens
W57F mid-point of unfolding transition curve is not very different from that of wild-type enzyme. Stability of the active site is slightly affected Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
Guanidine-HCl below 1 M, inactivation occurs without loss of the secondary structure Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Km-values of wild-type and mutant enzymes Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ essential for maintainance of native structure of the enzyme. Binding to the apoenzyme occurs during an essential step of refolding Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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