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Information on EC 3.5.1.3 - omega-amidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q8RUF8

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.3 omega-amidase
IUBMB Comments
Acts on glutaramate, succinamate and their 2-oxo derivatives.
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q8RUF8
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The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
omega-amidase, omega-amidase/nit2, omega-amidodicarboxylate amidohydrolase, nitrilase-like protein 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alpha-keto acid omega-amidase
-
-
-
-
alpha-keto acid-omega-amidase
-
-
-
-
amidase, omega
-
-
-
-
dicarboxylate omega-amidase
-
-
-
-
omega-amido dicarboxylate amidohydrolase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
transamidation
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
omega-amidodicarboxylate amidohydrolase
Acts on glutaramate, succinamate and their 2-oxo derivatives.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-19-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-hydroxysuccinamate + H2O
malate + NH3
show the reaction diagram
-
-
-
?
2-oxoglutaramate + H2O
2-oxoglutarate + NH3
show the reaction diagram
the product of glutamine transamination, 2-oxoglutaramate, can be hydrolyzed by the enzyme omega-amidase to form and ammonia
-
-
?
2-oxosuccinamate + H2O
oxaloacetate + NH3
show the reaction diagram
additional information
?
-
the recombinant omega-amidase is equally active with 2-oxosuccinamate, 2-oxoglutaramate and 2-hydroxysuccinamate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-oxosuccinamate + H2O
oxaloacetate + NH3
show the reaction diagram
the product of asparagine transamination, 2-oxosuccinamate, can be hydrolyzed by the enzyme omega-amidase to form oxaloacetate and ammonia
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.58
2-hydroxysuccinamate
pH 8.5, 30°C, recombinant His-tagged enzyme
4.43
2-Oxoglutaramate
pH 8.5, 30°C, recombinant His-tagged enzyme
6.13
2-oxosuccinamate
pH 8.5, 30°C, recombinant His-tagged enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene At5g12040
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the enzyme contains a chloroplast transit peptide of 60 residues at the N-terminus
Manually annotated by BRENDA team
additional information
second methionine residue in the deduced amino acid sequence, Met63, is located two residues C-terminal to the predicted cleavage site of the chloroplast transit peptide, N-terminal to Ser61. Alternative translation initiation from the corresponding downstream start codon can produce a cytosolic isoform, lacking the chloroplast transit peptide
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
omega-amidase is involved in the metabolism of asparagine, and probably is also closely coupled with glutamine transamination in the methionine salvage cycle
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NILP3_ARATH
369
0
40330
Swiss-Prot
Chloroplast (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
x * 40300, about, sequence calculation, x * 34000, recombinant His-tagged enzyme without transit peptide, SDS-PAGe
40300
x * 40300, about, sequence calculation, x * 34000, recombinant His-tagged enzyme without transit peptide, SDS-PAGe
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 40300, about, sequence calculation, x * 34000, recombinant His-tagged enzyme without transit peptide, SDS-PAGe
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminally His-tagged enzyme lacking the chloroplast transit peptide from Escherichia coli by nickel affinity chromatography and desalting gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene At5g12040, DNA and amino acid sequence determination and analysis, expression of N-terminally His-tagged recombinant enzyme lacking the chloroplast transit peptide, commencing at Met63, in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, Q.; Marsolais, F.
Identification and characterization of omega-amidase as an enzyme metabolically linked to asparagine transamination in Arabidopsis
Phytochemistry
99
36-43
2014
Arabidopsis thaliana (Q8RUF8), Arabidopsis thaliana Col (Q8RUF8)
Manually annotated by BRENDA team