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Literature summary extracted from

  • Krasnikov, B.F.; Chien, C.H.; Nostramo, R.; Pinto, J.T.; Nieves, E.; Callaway, M.; Sun, J.; Huebner, K.; Cooper, A.J.
    Identification of the putative tumor suppressor Nit2 as omega-amidase, an enzyme metabolically linked to glutamine and asparagine transamination (2009), Biochimie, 91, 1072-1080.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.3 Nit2-amplified DNA is obtained by PCR of Nit2 cDNA clnoed from human liver cDNA Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.3 0.0054
-
 2-Oxoglutaramate 37°C, pH 8.5, vmax: 20.6 micromol/mg*min Rattus norvegicus
3.5.1.3 3
-
 2-Oxoglutaramate apparent Km, 37°C, pH 8.5, vmax: 5.9 micromol/mg*min Homo sapiens
3.5.1.3 9
-
 2-Oxoglutaramate Km (open chain form), 37°C, pH 8.5, vmax: 5.9 micromol/mg*min Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.3 26000
-
 1 * 31000 + 1 * 26000, or 2 * 31000, not distinguishable, calculated from sequence, the 26000 Da subunit is a glutathione S-transferase subunit, the 31000 Da the catalytic subunit of omega-amidase Rattus norvegicus
3.5.1.3 27000
-
 1 * 30000 + 1 * 27000, or 2 * 30000, not distinguishable, SDS-PAGE, the 27000 Da subunit is a glutathione S-transferase subunit, the 30000 Da the catalytic subunit of omega-amidase Rattus norvegicus
3.5.1.3 30000
-
 1 * 30000 + 1 * 27000, or 2 * 30000, not distinguishable, SDS-PAGE, the 27000 Da subunit is a glutathione S-transferase subunit, the 30000 Da the catalytic subunit of omega-amidase Rattus norvegicus
3.5.1.3 30000
-
 2 * 30000, SDS-PAGE, there is no glutathione S-transferase isoform like determined for the Nit2 enzyme in rat Homo sapiens
3.5.1.3 31000
-
 1 * 31000 + 1 * 26000, or 2 * 31000, not distinguishable, calculated from sequence, the 26000 Da subunit is a glutathione S-transferase subunit, the 31000 Da the catalytic subunit of omega-amidase Rattus norvegicus
3.5.1.3 58000
-
 SDS-PAGE Rattus norvegicus
3.5.1.3 60000
-
 gel filtration on Sephadex G-200 Rattus norvegicus
3.5.1.3 62000
-
 gel filtration Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.3 2-oxoglutaramate + H2O Homo sapiens the in vivo substrates are generated by transamination of glutamine and asparagine, respectively 2-oxoglutarate + NH3
-
 ?
3.5.1.3 2-oxoglutaramate + H2O Rattus norvegicus the in vivo substrates are generated by transamination of glutamine and asparagine, respectively 2-oxoglutarate + NH3
-
 ?
3.5.1.3 2-oxosuccinamate + H2O Homo sapiens the in vivo substrates are generated by transamination of glutamine and asparagine, respectively oxaloacetate + NH3
-
 ?
3.5.1.3 2-oxosuccinamate + H2O Rattus norvegicus the in vivo substrates are generated by transamination of glutamine and asparagine, respectively oxaloacetate + NH3
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.3 Homo sapiens
-
-
-
3.5.1.3 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.3
-
 Homo sapiens
3.5.1.3 from rat liver Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.1.3 HeLa cell
-
 Homo sapiens
-
3.5.1.3 liver
-
 Homo sapiens
-
3.5.1.3 liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.3 2-oxoglutaramate + H2O the in vivo substrates are generated by transamination of glutamine and asparagine, respectively Homo sapiens 2-oxoglutarate + NH3
-
 ?
3.5.1.3 2-oxoglutaramate + H2O the in vivo substrates are generated by transamination of glutamine and asparagine, respectively Rattus norvegicus 2-oxoglutarate + NH3
-
 ?
3.5.1.3 2-oxosuccinamate + H2O the in vivo substrates are generated by transamination of glutamine and asparagine, respectively Homo sapiens oxaloacetate + NH3
-
 ?
3.5.1.3 2-oxosuccinamate + H2O the in vivo substrates are generated by transamination of glutamine and asparagine, respectively Rattus norvegicus oxaloacetate + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.3 dimer 1 * 30000 + 1 * 27000, or 2 * 30000, not distinguishable, SDS-PAGE, the 27000 Da subunit is a glutathione S-transferase subunit, the 30000 Da the catalytic subunit of omega-amidase Rattus norvegicus
3.5.1.3 dimer 1 * 31000 + 1 * 26000, or 2 * 31000, not distinguishable, calculated from sequence, the 26000 Da subunit is a glutathione S-transferase subunit, the 31000 Da the catalytic subunit of omega-amidase Rattus norvegicus
3.5.1.3 homodimer 2 * 30000, SDS-PAGE, there is no glutathione S-transferase isoform like determined for the Nit2 enzyme in rat Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.5.1.3 NIT2 a tumor suppressor protein Homo sapiens
3.5.1.3 NIT2 a tumor suppressor protein Rattus norvegicus
3.5.1.3 Nit2/omega-amidase
-
 Homo sapiens
3.5.1.3 Nit2/omega-amidase
-
 Rattus norvegicus
3.5.1.3 nitrilase-like protein 2
-
 Homo sapiens
3.5.1.3 nitrilase-like protein 2
-
 Rattus norvegicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.5.1.3 37
-
 assay at Homo sapiens
3.5.1.3 37
-
 assay at Rattus norvegicus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.1.3 8.5
-
 assay at Homo sapiens
3.5.1.3 8.5
-
 assay at Rattus norvegicus

General Information

EC Number General Information Comment Organism
3.5.1.3 physiological function omega-amidase plays an important role in removing potentially toxic intermediates by converting 2-oxoglutaramate and 2-oxosuccinamate to biologically useful 2-oxoglutarate and oxaloacetate, respectively. It is also important in nitrogen and sulfur metabolism Rattus norvegicus