Nuclease

2',3'-Cyclic-nucleotide 3'-phosphodiesterase (EC 3.1.4.37): the brain enzyme acts on 2',3'-cyclic AMP more rapidly than on the UMP or CMP derivatives.

2',3'-Cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16) hydrolyses 3'-nucleoside monophosphates and bis-4-nitrophenyl phosphate, but not 3'-deoxynucleotides.

1-Methyladenosine nucleosidase (EC 3.2.2.13) belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds.

18S rRNA (adenine1779-N6/adenine1780-N6)-Dimethyltransferase (EC 2.1.1.183): dIM1 is involved in pre-rRNA processing.

18S rRNA (guanine1575-N7)-Methyltransferase (EC 2.1.1.309), found in eukaryotes, is involved in pre-rRNA processing.

16S rRNA (uracil1498-N3)-methyltransferase (EC 2.1.1.193) specifically methylates uracil 1498 at the N3 position in 16S rRNA.

2-Haloacid dehalogenase (configuration-retaining) (EC 3.8.1.11) can dehalogenate (S)- and (R)-2-haloalkanoic acids into the corresponding (S)- and (R)-hydroxyalkanoic acids, respectively, while retaining the configuration at the C-2 position.

Deoxyribonuclease II, Bovine (EC 3.1.22.1) hydrolyzes deoxyribonucleotide linkages in native and denatured DNA yielding products with 3'-phosphates. In vitro, its optimum pH range is 4.5-5.0. Deoxyribonuclease II, Bovine (EC 3.1.22.1) also acts upon p-nitrophenyl-phosphodiesters at pH 5.6-5.9.

Guanylate Kinase, Porcine (EC 2.7.4.8), is an enzyme that transfers phosphorus-containing groups (phosphotransferases) using phosphate groups as acceptors. Guanylate Kinase is involved in purine metabolism. Its two substrates are ATP and GMP, and its two products are ADP and GDP.

Nucleoside Phosphorylase, bacterial (EC 2.4.2.1), is a pentosesyltransferase. Nucleoside Phosphorylase participates in three metabolic pathways: purine metabolism, pyrimidine metabolism, and nicotinic acid and nicotinamide metabolism. Its two substrates are purine nucleosides and phosphates, and its two products are purines and α-D-ribose-1-phosphate.

Adenosine 5'-Triphosphatase, Porcine (EC 3.6.1.3) is a class of enzymes that catalyze the decomposition of ATP into ADP and a free phosphate ion. This dephosphorylation reaction releases energy, which the enzyme (in most cases) harnesses to drive other chemical reactions that would not otherwise occur.

Uridine phosphorylase, E. coli (EC 2.4.2.3) catalyzes the reversible phosphorolysis of uridine with the formation of ribose-1-phosphate and uracil.

Calmodulin-dependent protein kinase II, Rat, is a serine-threonine protein kinase involved in neurotransmitter release, stimulation-induced gene expression control, and microtubule-associated protein phosphorylation.

Polyphosphate kinase (RsPPK; PPK), Propionibacterium shermanii is the Polyphosphate kinase (HY-E70426) derived from Propionibacterium shermanii. Polyphosphate kinase is a key enzyme in bacteria that catalyzes the reversible conversion between inorganic polyphosphate (polyP) and nucleoside phosphates (ATP/ADP/AMP, etc.). Polyphosphate kinase antagonizes the expression of virulence genes regulated by (p) ppGpp, PigR, MglA and SspA in Francisella tularensis. Polyphosphate kinase can be used in studies related to tularemia.

S-(5'-Adenosyl)-L-homocysteine Hydrolase, Rabbit (EC 3.3.1.1) is an enzyme in vertebrates which catabolizes S-adenosyl-L-homocysteine.

Protein Kinase C,Rat (EC 2.7.1.37) is a family of protein kinase enzymes that are involved in controlling the function of other proteins through the phosphorylation of hydroxyl groups of serine and threonine amino acid residues on these proteins. Protein Kinase C in turn are activated by signals such as increases in the concentration of diacylglycerol (DAG) or calcium ions (Ca²⁺).

Myokinase, Rabbit (EC 2.7.4.3) for research on ATP metabolism and enzymatic activity.

Adenosine-5'-triphosphate Sulfurylase, Saccharomyces cerevisiae (EC 2.7.7.4) belongs to the transferase family. Its two substrates are ATP and sulfate, and its two products are diphosphate and adenosine sulfate. Adenosine-5'-triphosphate Sulfurylase, Saccharomyces cerevisiae participates in three metabolic pathways: purine metabolism, selenoamino acid metabolism, and sulfur metabolism.

Prokaryotic thymidylate kinase (EC 2.7.4.9) is an enzyme that transfers phosphorus-containing groups (phosphotransferases) using phosphate groups as acceptors. Prokaryotic thymidylate kinase participates in pyrimidine metabolism. Its two substrates are ATP and dTMP, and its two products are ADP and dTDP.

Thermally stable RNase H degrades the RNA strand of a DNA-RNA hybrid without affecting the DNA or unhybridized RNA strands, significantly improving sensitivity and selectivity. Thermally stable RNase H has optimal activity at 65°C and remains active at 95°C.