3.5.99.8: 5-nitroanthranilic acid aminohydrolase
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For detailed information about 5-nitroanthranilic acid aminohydrolase, go to the full flat file.
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Synonyms
5NAA aminohydrolase, 5NAA deaminase, 5NAA-A, 5NAA-aminohydrolase, NAAA
ECTree
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Metals Ions
Metals Ions on EC 3.5.99.8 - 5-nitroanthranilic acid aminohydrolase
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Mn2+
additional information
NaaA contains the sequence HEAWH (amino acid residues 108 to 112), which is similar to the zinc binding motif HEXXH
additional information
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NaaA contains the sequence HEAWH (amino acid residues 108 to 112), which is similar to the zinc binding motif HEXXH
additional information
the enzyme is a metalloprotease family member, it can use several divalent transition metals for catalysis. The metal in 5NAA-A is labile but readily loaded in the presence of substrate. Adjacent to the 5NAA binding site is a triad of residues (His86-Glu196-Asn124) in a location equivalent to that of the corresponding M20 metalloprotease His2-Glu2-Asp metal binding motif. 5NAA-A requires metal ions for hydrolysis, and several transition metal ions are suitable. Fastest rates are observed in the presence of Mn2+, Fe2+ facilitates turnover but data cannot be fit to the Michaelis-Menten equation, like Cu2+, metal binding analysis, overview