Literature summary for 3.1.26.4 extracted from

Jongruja, N.; You, D.; Kanaya, E.; Koga, Y.; Takano, K.; Kanaya, S.
The N-terminal hybrid binding domain of RNase HI from Thermotoga maritima is important for substrate binding and Mg2+-dependent activity (2010), FEBS J., 277, 4474-4489 .

Search for more literature for 3.1.26.4

Cloned(Commentary)

Cloned (Comment)	Organism
overproduced in Escherichia coli	Thermotoga maritima

Protein Variants

Protein Variants	Comment	Organism
additional information	removal of the hybrid binding domain severely reduces the Mg2+-dependent activity of the enzyme by 750fold without significantly affecting the Mn2+-dependent activity	Thermotoga maritima
W22A	the mutation at the hybrid binding domain does not significantly affect the structure of enzyme. The pH, salt and metal ion dependencies of the mutant enzyme are similar to those of the wild-type enzyme. Its maximal Mn2+-dependent activity is also similar to that of wild-type enzyme. However, its maximal Mg2+-dependent activity is 7.5fold lower than that of the wild-type enzyme. The binding affinity of the mutant enzyme to the substrate is 21fold higher than that of the wild-type enzyme	Thermotoga maritima

Metals/Ions

Metals/Ions	Comment	Organism	Structure
KCl	requires 50 mm KCl for maximal activity	Thermotoga maritima
Mg2+	the enzyme (Tma-RNase HI) and the C-terminal RNase H domain (Tma-CD) exhibit the highest activities in the presence of 1 mM MgCl2 and 0.1-5 mM MnCl2. Both proteins exhibit little activity (less than 0.01% of the maximal activity) in the presence of NiCl2, ZnCl2, CoCl2 or CaCl2. Tma-RNase HI prefers Mg2+ to Mn2+ because its maximal Mg2+-dependent activity is higher than its maximal Mn2+-dependent activity by 16fold. The enzyme specifically loses most of the Mg2+-dependent activity on removal of the hybrid binding domain and 87% of it by the mutation at the hybrid binding domain	Thermotoga maritima
Mn2+	the enzyme (Tma-RNase HI) and the C-terminal RNase H domain (Tma-CD) exhibit the highest activities in the presence of 1 mM MgCl2 and 0.1-5 mM MnCl2. Both proteins exhibit little activity (less than 0.01% of the maximal activity) in the presence of NiCl2, ZnCl2, CoCl2 or CaCl2. Tma-RNase HI prefers Mg2+ to Mn2+ because its maximal Mg2+-dependent activity is higher than its maximal Mn2+-dependent activity by 16fold	Thermotoga maritima

Organism

Organism	UniProt	Comment	Textmining
Thermotoga maritima	Q9X122	-	-
Thermotoga maritima DSM 3109	Q9X122	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Thermotoga maritima

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
RNA/DNA hybrid + H2O	-	Thermotoga maritima	?	-	?
RNA/DNA hybrid + H2O	-	Thermotoga maritima DSM 3109	?	-	?

Synonyms

Synonyms	Comment	Organism
ribonuclease H I	-	Thermotoga maritima
RNase HI	-	Thermotoga maritima

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)