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Literature summary extracted from

  • Krug, U.; Alexander, N.S.; Stein, R.A.; Keim, A.; Mchaourab, H.S.; Straeter, N.; Meiler, J.
    Characterization of the domain orientations of E. coli 5'-nucleotidase by fitting an ensemble of conformers to DEER distance distributions (2016), Structure, 24, 43-56 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.5 K191C/G398C the mutations affect the enzyme activity Escherichia coli
3.1.3.5 K191C/K532C the mutations affect the enzyme activity Escherichia coli
3.1.3.5 K191C/Q452C the mutations affect the enzyme activity Escherichia coli
3.1.3.5 T124C/G398C the mutations affect the enzyme activity Escherichia coli
3.1.3.5 T124C/K532C the mutations affect the enzyme activity Escherichia coli
3.1.3.5 T124C/Q452C the mutations affect the enzyme activity Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.3.5 alpha,beta-methylene-ADP
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.5 a 5'-ribonucleotide + H2O Escherichia coli
-
 a ribonucleoside + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.5 Escherichia coli P07024
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.5 5'-AMP + H2O
-
 Escherichia coli adenosine + phosphate
-
 ?
3.1.3.5 a 5'-ribonucleotide + H2O
-
 Escherichia coli a ribonucleoside + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.3.5 5NT
-
 Escherichia coli