Literature summary for 3.6.1.13 extracted from

Yoshiba, S.; Ooga, T.; Nakagawa, N.; Shibata, T.; Inoue, Y.; Yokoyama, S.; Kuramitsu, S.; Masui, R.
Structural insights into the Thermus thermophilus ADP-ribose pyrophosphatase mechanism via crystal structures with the bound substrate and metal (2004), J. Biol. Chem., 279, 37163-37174.

Crystallization (Commentary)

Crystallization (Comment)	Organism
Zn2+-bound enzyme, binary complex with ADPribose, ternary complex with Zn2+ and ADPribose, ternary complex with Gd3+ and ADPribose, product complex with AMP and Mg2+, product complex with ribose 5'-phosphate and Zn2+, mutant enzyme E82Q with ligands Mg2+ and SO42-, mutant enzyme E86Q with ligands Mg2+ and ADPribose, mutant enzyme E82Q with ligands Zn2+ and SO42-, mutant enzyme E86Q with ligands Zn2+ and ADPribose	Thermus thermophilus

Crystallization (Comment)

Organism

Zn2+-bound enzyme, binary complex with ADPribose, ternary complex with Zn2+ and ADPribose, ternary complex with Gd3+ and ADPribose, product complex with AMP and Mg2+, product complex with ribose 5'-phosphate and Zn2+, mutant enzyme E82Q with ligands Mg2+ and SO42-, mutant enzyme E86Q with ligands Mg2+ and ADPribose, mutant enzyme E82Q with ligands Zn2+ and SO42-, mutant enzyme E86Q with ligands Zn2+ and ADPribose

Thermus thermophilus

Protein Variants

Protein Variants	Comment	Organism
D126N	the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 40% of the of the wild-type enzyme	Thermus thermophilus
D128N	the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 74% of the of the wild-type enzyme	Thermus thermophilus
E127Q	the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 114% of the of the wild-type enzyme	Thermus thermophilus
E129Q	the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 32% of the of the wild-type enzyme	Thermus thermophilus
E82Q	the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 0.0006% of the of the wild-type enzyme	Thermus thermophilus
E86Q	the ratio of turnover-number to Km-value with ADPribose as substrate and Mg2+ as activator is 0.0034% of the of the wild-type enzyme	Thermus thermophilus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
0.031	-	ADPribose	mutant enzyme D126N, in presence of Mg2+	Thermus thermophilus
0.044	-	ADPribose	mutant enzyme E129Q, in presence of Mg2+	Thermus thermophilus
0.058	-	ADPribose	mutant enzyme D128N, in presence of Mg2+	Thermus thermophilus
0.071	-	ADPribose	mutant enzyme E127Q, in presence of Mg2+	Thermus thermophilus
0.09	-	ADPribose	mutant enzyme E86Q, in presence of Mg2+	Thermus thermophilus
0.11	-	ADPribose	wild-type enzyme, in presence of Mg2+	Thermus thermophilus
0.215	-	ADPribose	mutant enzyme E82Q, in presence of Zn2+	Thermus thermophilus
0.325	-	ADPribose	mutant enzyme E86Q, in presence of Zn2+	Thermus thermophilus
0.36	-	ADPribose	mutant enzyme E82Q, in presence of Mg2+	Thermus thermophilus
0.37	-	ADPribose	wild-type enzyme, in presence of Zn2+	Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ADP-ribose + H2O	Thermus thermophilus	the enzyme plays a key role in regulating the intracellular ADPribose levels, and prevents nonenzymatic ADP-ribosylation	AMP + D-ribose 5-phosphate	-	?
ADP-ribose + H2O	Thermus thermophilus HB8 / ATCC 27634 / DSM 579	the enzyme plays a key role in regulating the intracellular ADPribose levels, and prevents nonenzymatic ADP-ribosylation	AMP + D-ribose 5-phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	-	-	-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
ADP-ribose + H2O	-	Thermus thermophilus	AMP + D-ribose 5-phosphate	-	?
ADP-ribose + H2O	the enzyme plays a key role in regulating the intracellular ADPribose levels, and prevents nonenzymatic ADP-ribosylation	Thermus thermophilus	AMP + D-ribose 5-phosphate	-	?
ADP-ribose + H2O	-	Thermus thermophilus HB8 / ATCC 27634 / DSM 579	AMP + D-ribose 5-phosphate	-	?
ADP-ribose + H2O	the enzyme plays a key role in regulating the intracellular ADPribose levels, and prevents nonenzymatic ADP-ribosylation	Thermus thermophilus HB8 / ATCC 27634 / DSM 579	AMP + D-ribose 5-phosphate	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
0.00011	-	ADP-ribose	mutant enzyme E82Q, in presence of Mg2+	Thermus thermophilus
0.00014	-	ADP-ribose	mutant enzyme E82Q, in presence of Zn2+	Thermus thermophilus
0.00015	-	ADP-ribose	mutant enzyme E86Q, in presence of Mg2+	Thermus thermophilus
0.00032	-	ADP-ribose	mutant enzyme E86Q, in presence of Zn2+	Thermus thermophilus
0.7	-	ADP-ribose	mutant enzyme D126N, in presence of Mg2+	Thermus thermophilus
0.7	-	ADP-ribose	mutant enzyme E129Q, in presence of Mg2+	Thermus thermophilus
2	8	ADP-ribose	wild-type enzyme, in presence of Zn2+	Thermus thermophilus
2.2	-	ADP-ribose	mutant enzyme D128N, in presence of Mg2+	Thermus thermophilus
4.1	-	ADP-ribose	mutant enzyme E127Q, in presence of Mg2+	Thermus thermophilus
5.7	-	ADP-ribose	wild-type enzyme, in presence of Mg2+	Thermus thermophilus