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Literature summary extracted from

  • Bitra, A.; Hussain, B.; Tanwar, A.S.; Anand, R.
    Identification of function and mechanistic insights of guanine deaminase from Nitrosomonas europaea: role of the C-terminal loop in catalysis (2013), Biochemistry, 52, 3512-3522.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.5.4.3 in complex with 8-azaguanine, hanging drop vapor diffusion method Nitrosomonas europaea

Protein Variants

EC Number Protein Variants Comment Organism
3.5.4.3 E143X the mutation results in a complete loss of activity Nitrosomonas europaea
3.5.4.3 E79X the mutation results in a complete loss of activity Nitrosomonas europaea
3.5.4.3 additional information the mutant form of the enzyme with the deletion of the extreme nine amino acids does not exhibit any enzyme activity Nitrosomonas europaea

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.4.3 Zn2+ dependent on Nitrosomonas europaea

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.4.3 ammeline + H2O Nitrosomonas europaea
-
?
-
?
3.5.4.3 guanine + H2O Nitrosomonas europaea
-
xanthine + NH3
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.5.4.3 Nitrosomonas europaea Q82Y41
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.4.3 ammeline + H2O
-
Nitrosomonas europaea ?
-
?
3.5.4.3 guanine + H2O
-
Nitrosomonas europaea xanthine + NH3
-
?

Subunits

EC Number Subunits Comment Organism
3.5.4.3 homodimer x-ray crystallography Nitrosomonas europaea

Synonyms

EC Number Synonyms Comment Organism
3.5.4.3 NE0047
-
Nitrosomonas europaea

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.5.4.3 120
-
guanine pH and temperature not specified in the publication Nitrosomonas europaea