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Literature summary for 3.1.3.5 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

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

Inhibitors

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli P07024
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
5NT
-
Escherichia coli