Literature summary for 3.5.1.42 extracted from

Karuppiah, V.; Thistlethwaite, A.; Dajani, R.; Warwicker, J.; Derrick, J.P.
Structure and mechanism of the bifunctional CinA enzyme from Thermus thermophilus (2014), J. Biol. Chem., 289, 33187-33197.

Cloned(Commentary)

Cloned (Comment)	Organism
gene cinA, recombinant expression of His6-tagged enzyme with a thrombin cleavage site at the N terminus in Escherichia coli strain T7	Thermus thermophilus

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant detagged enzyme free or in complex with nicotinate mononucleotide, or AMP/Mg2+, or ATP/Mg2+, or ribose-ADP/Mg2+, sitting drop vapor diffusion, mixing of 200 nl of protein with 200 nl of well solution containing 0.2 M Na2SO4, 0.1 M Bis-Tris propane, pH 6.5, and 20% w/v, PEG 3350 at 20°C, rodlike crystals, 5-7 days, X-ray diffraction structure determination and analysis at 1.98-2.46 A resolution, molecular replacement and modeling	Thermus thermophilus

Crystallization (Comment)

Organism

purified recombinant detagged enzyme free or in complex with nicotinate mononucleotide, or AMP/Mg2+, or ATP/Mg2+, or ribose-ADP/Mg2+, sitting drop vapor diffusion, mixing of 200 nl of protein with 200 nl of well solution containing 0.2 M Na2SO4, 0.1 M Bis-Tris propane, pH 6.5, and 20% w/v, PEG 3350 at 20°C, rodlike crystals, 5-7 days, X-ray diffraction structure determination and analysis at 1.98-2.46 A resolution, molecular replacement and modeling

Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
beta-nicotinamide D-ribonucleotide + H2O	Thermus thermophilus	-	beta-nicotinate D-ribonucleotide + NH3	-	?
beta-nicotinamide D-ribonucleotide + H2O	Thermus thermophilus DSM 579	-	beta-nicotinate D-ribonucleotide + NH3	-	?
beta-nicotinamide D-ribonucleotide + H2O	Thermus thermophilus HB8 / ATCC 27634 / DSM 579	-	beta-nicotinate D-ribonucleotide + NH3	-	?

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	Q5SHB0	gene cinA	-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579	Q5SHB0	gene cinA	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His6-tagged enzyme from Escherichia coli strain T7 by nickel affinity chromatgraphy, cleavage of the tag by thrombin, anion exchange chromatography, and gel filtration	Thermus thermophilus

Reaction

Reaction	Comment	Organism	Reaction ID
beta-nicotinamide D-ribonucleotide + H2O = beta-nicotinate D-ribonucleotide + NH3	catalytic mechanism, overview	Thermus thermophilus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
beta-nicotinamide D-ribonucleotide + H2O	-	Thermus thermophilus	beta-nicotinate D-ribonucleotide + NH3	-	?
beta-nicotinamide D-ribonucleotide + H2O	-	Thermus thermophilus DSM 579	beta-nicotinate D-ribonucleotide + NH3	-	?
beta-nicotinamide D-ribonucleotide + H2O	-	Thermus thermophilus HB8 / ATCC 27634 / DSM 579	beta-nicotinate D-ribonucleotide + NH3	-	?
additional information	CinA is a bifunctional enzyme exhibiting both nicotinamide mononucleotide deamidase and ADP-ribose diphosphatase activities, ligand binding structures and catalytic mechanism analysis for both activities, overview	Thermus thermophilus	?	-	?
additional information	CinA is a bifunctional enzyme exhibiting both nicotinamide mononucleotide deamidase and ADP-ribose diphosphatase activities, ligand binding structures and catalytic mechanism analysis for both activities, overview	Thermus thermophilus DSM 579	?	-	?
additional information	CinA is a bifunctional enzyme exhibiting both nicotinamide mononucleotide deamidase and ADP-ribose diphosphatase activities, ligand binding structures and catalytic mechanism analysis for both activities, overview	Thermus thermophilus HB8 / ATCC 27634 / DSM 579	?	-	?

Subunits

Subunits	Comment	Organism
dimer	an unusual asymmetric dimer, with three domains for each chain, the C-terminal domain harbors the nicotinamide mononucleotide deamidase activity. The asymmetry in the CinA dimer arises from two alternative orientations of the N-terminal COG1058 domains, only one of which forms a contact with the KH-type domain from the other chain, effectively closing the active site into, we propose, a catalytically competent state	Thermus thermophilus

Synonyms

Synonyms	Comment	Organism
CinA	-	Thermus thermophilus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Thermus thermophilus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8	-	assay at	Thermus thermophilus

General Information

General Information	Comment	Organism
evolution	the enzyme's N-terminal domain belongs to the COG1058 family and is associated with the ADP-ribose pyrophosphatase activity	Thermus thermophilus
metabolism	the enzyme is associated with natural competence and is proposed to have a function as an enzyme participating in the pyridine nucleotide cycle, which recycles products formed by non-redox uses of NAD+	Thermus thermophilus