Literature summary for 1.16.1.1 extracted from

Rennex, D.; Cummings, R.T.; Pickett, M.; Walsh, C.T.; Bradley, M.
Role of tyrosine residues in Hg(II) detoxification by mercuric reductase from Bacillus sp. strain RC607 (1993), Biochemistry, 32, 7475-7478.

Search for more literature for 1.16.1.1

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Bacillus sp. (in: Bacteria)

Protein Variants

Protein Variants	Comment	Organism
Y264F	Km-value for Hg2+ is 5fold lower compared to the Km-value of the wild-type enzyme, turn-over number is reduced by 164fold	Bacillus sp. (in: Bacteria)
Y264F/Y605F	Km-value for Hg2+ is 5fold lower than the Km-value of the wild-type enzyme, turnover-number is reduced by 1091fold	Bacillus sp. (in: Bacteria)
Y605F	Km-value for Hg2+ is 1.3fold higher compared to the Km-value of the wild-type enzyme, turnover-number is reduced by 6.3fold	Bacillus sp. (in: Bacteria)

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.03	-	Hg2+	-	Bacillus sp. (in: Bacteria)

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
69000	-	x * 69000, SDS-PAGE	Bacillus sp. (in: Bacteria)

Organism

Organism	UniProt	Comment	Textmining
Bacillus sp. (in: Bacteria)	-	-	-
Bacillus sp. (in: Bacteria) RC607	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Bacillus sp. (in: Bacteria)

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Hg2+ + NADPH	-	Bacillus sp. (in: Bacteria)	Hg + NADP+ + H+	-	?
Hg2+ + NADPH	-	Bacillus sp. (in: Bacteria) RC607	Hg + NADP+ + H+	-	?
additional information	Tyr264 and Tyr605 are involved in substrate binding, Tyr264 is important for catalysis, possibly by destabilizing the binding of Hg(II) to the two ligating thiolates at the active site	Bacillus sp. (in: Bacteria)	?	-	?
additional information	Tyr264 and Tyr605 are involved in substrate binding, Tyr264 is important for catalysis, possibly by destabilizing the binding of Hg(II) to the two ligating thiolates at the active site	Bacillus sp. (in: Bacteria) RC607	?	-	?

Subunits

Subunits	Comment	Organism
?	x * 69000, SDS-PAGE	Bacillus sp. (in: Bacteria)

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
12	-	Hg2+	-	Bacillus sp. (in: Bacteria)

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	-	Bacillus sp. (in: Bacteria)

Cofactor

Cofactor	Comment	Organism	Structure
NADPH	-	Bacillus sp. (in: Bacteria)

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Release 2023.1 (January 2023)