Any feedback?
Information on EC 3.5.1.3 - omega-amidase and Organism(s) Homo sapiens
for references in articles please use BRENDA:EC3.5.1.3Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.5.1.3 omega-amidaseIUBMB Comments
Acts on glutaramate, succinamate and their 2-oxo derivatives.
Specify your search results
Word Map
- 3.5.1.3
- alpha-ketoglutaramate
- asparagine
-
transamination
- ammonia
- oxaloacetate
- succinamate
- glutaminase
-
transamidase
- analysis
- medicine
- biotechnology
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
omega-amidase, omega-amidodicarboxylate amidohydrolase, nitrilase-like protein 2, omega-amidase/nit2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-keto acid omega-amidase
-
-
-
-
alpha-keto acid-omega-amidase
-
-
-
-
amidase, omega
-
-
-
-
dicarboxylate omega-amidase
-
-
-
-
NIT2
nitrilase-like protein 2
omega-amido dicarboxylate amidohydrolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
transamidation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
omega-amidodicarboxylate amidohydrolase
Acts on glutaramate, succinamate and their 2-oxo derivatives.
CAS REGISTRY NUMBER
COMMENTARY
9025-19-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxoglutaramate + H2O
2-oxoglutarate + NH3
-
the in vivo substrates are generated by transamination of glutamine and asparagine, respectively
-
-
?
2-oxosuccinamate + H2O
oxaloacetate + NH3
-
the in vivo substrates are generated by transamination of glutamine and asparagine, respectively
-
-
?
additional information
?
-
-
enzyme of glutamine-transaminase-omega-amidase pathway, role in degradation of glutamine
-
-
?
additional information
?
-
-
enzyme of glutamine-transaminase-omega-amidase pathway, role in degradation of glutamine
-
-
?
additional information
?
-
-
enzyme of glutamine-transaminase-omega-amidase pathway, role in degradation of glutamine
-
-
?
additional information
?
-
-
second enzyme of the enzyme system capable of converting glutamine to ammonia and capable of generating relatively large amounts of ammonia from glutamine, the glutaminase II pathway, glutamine transaminase, EC 2.6.1.15 plus omega-amidase, EC 3.5.1.3 pathway
-
-
?
additional information
?
-
-
second enzyme of the enzyme system capable of converting glutamine to ammonia and capable of generating relatively large amounts of ammonia from glutamine, the glutaminase II pathway, glutamine transaminase, EC 2.6.1.15 plus omega-amidase, EC 3.5.1.3 pathway
-
-
?
additional information
?
-
-
pathway for brain glutamine metabolism involves glutamine transaminase-omega-maidase pathway, L-glutamine: 2-oxo-acid amino-transferase, EC 2.6.1.15 and omega-amidodicarboxylate amidohydrolase, EC 3.5.1.3
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxosuccinamate + H2O
oxaloacetate + NH3
-
the in vivo substrates are generated by transamination of glutamine and asparagine, respectively
-
-
?
2-oxoglutaramate + H2O
2-oxoglutarate + NH3
-
the in vivo substrates are generated by transamination of glutamine and asparagine, respectively
-
-
?
additional information
?
-
-
enzyme of glutamine-transaminase-omega-amidase pathway, role in degradation of glutamine
-
-
?
additional information
?
-
-
enzyme of glutamine-transaminase-omega-amidase pathway, role in degradation of glutamine
-
-
?
additional information
?
-
-
enzyme of glutamine-transaminase-omega-amidase pathway, role in degradation of glutamine
-
-
?
additional information
?
-
-
second enzyme of the enzyme system capable of converting glutamine to ammonia and capable of generating relatively large amounts of ammonia from glutamine, the glutaminase II pathway, glutamine transaminase, EC 2.6.1.15 plus omega-amidase, EC 3.5.1.3 pathway
-
-
?
additional information
?
-
-
second enzyme of the enzyme system capable of converting glutamine to ammonia and capable of generating relatively large amounts of ammonia from glutamine, the glutaminase II pathway, glutamine transaminase, EC 2.6.1.15 plus omega-amidase, EC 3.5.1.3 pathway
-
-
?
additional information
?
-
-
pathway for brain glutamine metabolism involves glutamine transaminase-omega-maidase pathway, L-glutamine: 2-oxo-acid amino-transferase, EC 2.6.1.15 and omega-amidodicarboxylate amidohydrolase, EC 3.5.1.3
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9
2-Oxoglutaramate
-
Km (open chain form), 37°C, pH 8.5, vmax: 5.9 micromol/mg*min
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme may be regarded as a repair enzyme for salvaging L-2-hydroxysuccinamate (as L-malate), and, working in conjunction with L-2-hydroxyglutarate dehydrogenase, for salvaging L-2-hydroxyglutaramate (as 2-oxoglutarate)
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NIT2_HUMAN
276
0
30608
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
-
2 * 30000, SDS-PAGE, there is no glutathione S-transferase isoform like determined for the Nit2 enzyme in rat
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
-
2 * 30000, SDS-PAGE, there is no glutathione S-transferase isoform like determined for the Nit2 enzyme in rat
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Nit2-amplified DNA is obtained by PCR of Nit2 cDNA clnoed from human liver cDNA
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
use of soluble omega-amidase-glutamate dehydrogenase to determine alpha-ketoglutaramate in biological samples
medicine
-
in patients with liver disease and encephalopathy there is a good correlation between degree of neurological dysfunction and increase in alpha-ketoglutaramate in cerebrospinal fluid, omega-amidase is suitable for determination of alpha-ketoglutaramate
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cooper, A.J.L.; Duffy, T.E.; Meister, A.
alpha-Keto acid omega-amidase from rat liver
Methods Enzymol.
113
350-358
1985
Embryophyta, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae
Makar, T.K.; Nedergaard, M.; Preuss, A.; Hertz, L.; Cooper, A.J.L.
Glutamine transaminase K and omega-amidase activities in primary cultures of astrocytes and neurons and in embryonic chick forebrain: marked induction of brain glutamine transaminase K at time of hatching
J. Neurochem.
62
1983-1988
1994
Gallus gallus, Homo sapiens, Mus musculus, Rattus norvegicus
Cooper, A.J.L.; Meister, A.
The glutamine transaminase-omega-amidase pathway
CRC Crit. Rev. Biochem.
4
281-303
1977
Canis lupus familiaris, Embryophyta, Enterococcus faecalis, Escherichia coli, Homo sapiens, Lactuca sativa, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Spinacia oleracea
Cooper, A.J.L.; Cross, M.
The glutamine transaminase-omega-amidase system in rat and human brain
J. Neurochem.
28
771-778
1977
Homo sapiens, Rattus norvegicus
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
Biochimie
91
1072-1080
2009
Homo sapiens, Rattus norvegicus
EXTERNAL LINKS (specific for EC-Number 3.5.1.3)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
