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Literature summary extracted from

  • Arif, S.; Patil, A.; Varshney, U.; Vijayan, M.
    Biochemical and structural studies of Mycobacterium smegmatis MutT1, a sanitization enzyme with unusual modes of association (2017), Acta Crystallogr. Sect. D, 73, 349-364 .
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.6.1.69 structures of the apoenzyme and of ligand-bound enzyme in the presence of 8-oxo-GTP or 8-oxo-dGTP. The molecules arrange themselves in a head-to-tail fashion in which domain 1 is brought into contact with domain 2 of a neighbouring molecule. The binding site for NTP (site A) is almost exclusively made up of residues from domain 1, while those for NDP (site B) and NMP (site C) are at the interface between domain 1 and neighbour domain 2 Mycolicibacterium smegmatis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.69 Mg2+ required Mycolicibacterium smegmatis

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.69 Mycolicibacterium smegmatis A0QUZ2
-
-
3.6.1.69 Mycolicibacterium smegmatis ATCC 700084 A0QUZ2
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.69 8-oxo-dGTP + H2O
-
Mycolicibacterium smegmatis 8-oxo-dGDP + phosphate
-
?
3.6.1.69 8-oxo-dGTP + H2O
-
Mycolicibacterium smegmatis ATCC 700084 8-oxo-dGDP + phosphate
-
?
3.6.1.69 8-oxo-GTP + H2O
-
Mycolicibacterium smegmatis 8-oxo-GDP + phosphate
-
?
3.6.1.69 8-oxo-GTP + H2O
-
Mycolicibacterium smegmatis ATCC 700084 8-oxo-GDP + phosphate
-
?
3.6.1.69 additional information under high concentrations and over long periods, the full-length enzyme as well as domain 1 catalyses the hydrolysis of the nucleoside triphosphates to the respective nucleoside monophosphates and pyrophosphate. No substrates: GTP, dGTP Mycolicibacterium smegmatis ?
-
?
3.6.1.69 additional information under high concentrations and over long periods, the full-length enzyme as well as domain 1 catalyses the hydrolysis of the nucleoside triphosphates to the respective nucleoside monophosphates and pyrophosphate. No substrates: GTP, dGTP Mycolicibacterium smegmatis ATCC 700084 ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.6.1.69 MSMEG_2390
-
Mycolicibacterium smegmatis

General Information

EC Number General Information Comment Organism
3.6.1.69 physiological function enzyme is made up of a Nudix domain (domain1) and a histidine phosphatase domain (domain 2). Domain 1 alone hydrolyses nucleoside triphosphates less efficiently Mycolicibacterium smegmatis