This enzyme belongs to the family of hydrolases, specifically those glycosylases that hydrolyse N-glycosyl compounds. The systematic name of this enzyme class is purine-nucleoside ribohydrolase. Other names in common use include nucleosidase, purine beta-ribosidase, purine nucleoside hydrolase, purine ribonucleosidase, ribonucleoside hydrolase, nucleoside hydrolase, N-ribosyl purine ribohydrolase, nucleosidase g, N-D-ribosylpurine ribohydrolase, inosine-adenosine-guanosine preferring nucleoside hydrolase, purine-specific nucleoside N-ribohydrolase, IAG-nucleoside hydrolase, and IAG-NH. This enzyme participates in purine metabolism and nicotinate and nicotinamide metabolism.
Purine nucleoside phosphorylase, PNP, PNPase or inosine phosphorylase is an enzyme that in humans is encoded by the NP gene. It catalyzes the chemical reaction
In molecular biology, Small nucleolar RNA TBR17 is a non-coding RNA (ncRNA) molecule identified in Trypanosoma brucei which functions in the modification of other small nuclear RNAs (snRNAs). This type of modifying RNA is usually located in the nucleolus of the eukaryotic cell which is a major site of snRNA biogenesis. It is known as a small nucleolar RNA (snoRNA) and also often referred to as a guide RNA.
In enzymology, a trypanothione synthase (EC 6.3.1.9) is an enzyme that catalyzes the chemical reaction
In enzymology, a nucleoside-diphosphatase (EC 3.6.1.6) is an enzyme that catalyzes the chemical reaction
In enzymology, a nucleoside-triphosphate diphosphatase (EC 3.6.1.19) is an enzyme that catalyzes the chemical reaction
The enzyme 2′,3′-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1.4.16) catalyzes the reaction
In enzymology, an adenosine nucleosidase (EC 3.2.2.7) is an enzyme that catalyzes the chemical reaction
In enzymology, an AMP nucleosidase (EC 3.2.2.4) is an enzyme that catalyzes the chemical reaction
In enzymology, an inosine nucleosidase (EC 3.2.2.2) is an enzyme that catalyzes the chemical reaction
In enzymology, a methylthioadenosine nucleosidase (EC 3.2.2.16) is an enzyme that catalyzes the chemical reaction
In enzymology, a NAD+ glycohydrolase (EC 3.2.2.5) is an enzyme that catalyzes the chemical reaction
In enzymology, a ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase (EC 3.2.2.6) is a bifunctional enzyme that catalyzes the chemical reaction
In enzymology, a N-methyl nucleosidase (EC 3.2.2.25) is an enzyme that catalyzes the chemical reaction
In enzymology, a ribosylpyrimidine nucleosidase (EC 3.2.2.8) is an enzyme that catalyzes the chemical reaction
In enzymology, an uridine nucleosidase (EC 3.2.2.3) is an enzyme that catalyzes the chemical reaction
In enzymology, a hydroxyisourate hydrolase (EC 3.5.2.17) is an enzyme that catalyzes the chemical reaction
In enzymology, a pyrimidine-nucleoside phosphorylase is an enzyme that catalyzes the chemical reaction
Diphosphoinositol polyphosphate phosphohydrolase 1 is an enzyme that in humans is encoded by the NUDT3 gene.
NUDIX hydrolases are a superfamily of hydrolytic enzymes capable of cleaving nucleoside diphosphates linked to x, hence their name. The reaction yields nucleoside monophosphate (NMP) plus X-P. Substrates hydrolysed by nudix enzymes comprise a wide range of organic pyrophosphates, including nucleoside di- and triphosphates, dinucleoside and diphosphoinositol polyphosphates, nucleotide sugars and RNA caps, with varying degrees of substrate specificity. Enzymes of the NUDIX superfamily are found in all types of organisms, including eukaryotes, bacteria and archaea.
Unsaturated chondroitin disaccharide hydrolase (EC 3.2.1.180, UGL, unsaturated glucuronyl hydrolase) is an enzyme with systematic name beta-D-4-deoxy-Delta4-GlcAp-(1->3)-beta-D-GalNAc6S hydrolase. This enzyme catalyses the following chemical reaction
References
HEPPEL LA, HILMOE RJ (1952). "[Phosphorolysis and hydrolysis of purine ribosides by enzymes from yeast.]". J. Biol. Chem. 198 (2): 683–94. PMID12999785.
Kalckar HM. "Biosynthetic aspects of nucleosides and nucleic acids". Pubbl. Staz. Napoli. Zool.: 87–103.
Takagi Y, Horecker BL (1956). "Purification and properties of a bacterial riboside hydrolyase". J. Biol. Chem. 225 (1): 77–86. PMID13416219.
Mazumder-Shivakumar D, Bruice TC (2005). "Computational study of IAG-nucleoside hydrolase: determination of the preferred ground state conformation and the role of active site residues". Biochemistry. 44 (21): 7805–17. doi:10.1021/bi047394h. PMID15909995.
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