Literature summary for 1.7.2.2 extracted from

Trofimov, A.A.; Polyakov, K.M.; Tikhonova, T.V.; Tikhonov, A.V.; Safonova, T.N.; Boyko, K.M.; Dorovatovskii, P.V.; Popov, V.O.
Covalent modifications of the catalytic tyrosine in octahaem cytochrome c nitrite reductase and their effect on the enzyme activity (2012), Acta Crystallogr. Sect. D, 68, 144-153.

Crystallization (Commentary)

Crystallization (Comment)	Organism
modified form of the enzyme that contains an additional covalent bond between residues Tyr303 and Gln360 in complex with phosphate to 1.45 A resolution, and with sulfite to 1.8 A resolution, structure of unmodified enzyme in complex with nitrite to 1.83 A resolution. Structure reveal the presence of a covalent bond between the CE2 atom of the catalytic Tyr303 and the S atom of Cys305, which might be responsible for the higher nitrite reductase activity. The formation of the second covalent bond by Tyr303 leads to a decrease in both the nitrite and sulfite reductase activities of the enzyme. Tyr303 is located at the exit from the putative proton-transport channel to the active site	Thioalkalivibrio nitratireducens

Crystallization (Comment)

Organism

modified form of the enzyme that contains an additional covalent bond between residues Tyr303 and Gln360 in complex with phosphate to 1.45 A resolution, and with sulfite to 1.8 A resolution, structure of unmodified enzyme in complex with nitrite to 1.83 A resolution. Structure reveal the presence of a covalent bond between the CE2 atom of the catalytic Tyr303 and the S atom of Cys305, which might be responsible for the higher nitrite reductase activity. The formation of the second covalent bond by Tyr303 leads to a decrease in both the nitrite and sulfite reductase activities of the enzyme. Tyr303 is located at the exit from the putative proton-transport channel to the active site

Thioalkalivibrio nitratireducens

Organism

Organism	UniProt	Comment	Textmining
Thioalkalivibrio nitratireducens	Q5F2I3	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
nitrite + reduced methyl viologen	-	Thioalkalivibrio nitratireducens	NH3 + oxidized methyl viologen + H2O	-	?
sulfite + reduced methyl viologen	-	Thioalkalivibrio nitratireducens	H2S + oxidized methyl viologen + H2O	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
0.023	-	sulfite	modified enzyme that contains an additional covalent bond between residues Tyr303 and Gln360, pH 7.0, 20°C	Thioalkalivibrio nitratireducens
0.039	-	sulfite	unmodified enzyme, pH 7.0, 20°C	Thioalkalivibrio nitratireducens
1195	-	nitrite	modified enzyme that contains an additional covalent bond between residues Tyr303 and Gln360, pH 7.0, 20°C	Thioalkalivibrio nitratireducens
2860	-	nitrite	unmodified enzyme, pH 7.0, 20°C	Thioalkalivibrio nitratireducens