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Literature summary for 3.5.1.3 extracted from

  • Zhang, Q.; Marsolais, F.
    Identification and characterization of omega-amidase as an enzyme metabolically linked to asparagine transamination in Arabidopsis (2014), Phytochemistry, 99, 36-43.
    View publication on PubMed
Search for more literature for 3.5.1.3

Cloned(Commentary)

Cloned (Comment) Organism
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 Arabidopsis thaliana

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.43
-
 2-Oxoglutaramate pH 8.5, 30°C, recombinant His-tagged enzyme Arabidopsis thaliana
5.58
-
 2-hydroxysuccinamate pH 8.5, 30°C, recombinant His-tagged enzyme Arabidopsis thaliana
6.13
-
 2-oxosuccinamate pH 8.5, 30°C, recombinant His-tagged enzyme Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast the enzyme contains a chloroplast transit peptide of 60 residues at the N-terminus Arabidopsis thaliana 9507
-
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 Arabidopsis thaliana
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34000
-
 x * 40300, about, sequence calculation, x * 34000, recombinant His-tagged enzyme without transit peptide, SDS-PAGe Arabidopsis thaliana
40300
-
 x * 40300, about, sequence calculation, x * 34000, recombinant His-tagged enzyme without transit peptide, SDS-PAGe Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-oxosuccinamate + H2O Arabidopsis thaliana the product of asparagine transamination, 2-oxosuccinamate, can be hydrolyzed by the enzyme omega-amidase to form oxaloacetate and ammonia oxaloacetate + NH3
-
 ?
2-oxosuccinamate + H2O Arabidopsis thaliana Col the product of asparagine transamination, 2-oxosuccinamate, can be hydrolyzed by the enzyme omega-amidase to form oxaloacetate and ammonia oxaloacetate + NH3
-
 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana Q8RUF8 gene At5g12040
-
Arabidopsis thaliana Col Q8RUF8 gene At5g12040
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His-tagged enzyme lacking the chloroplast transit peptide from Escherichia coli by nickel affinity chromatography and desalting gel filtration Arabidopsis thaliana

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-hydroxysuccinamate + H2O
-
 Arabidopsis thaliana malate + NH3
-
 ?
2-hydroxysuccinamate + H2O
-
 Arabidopsis thaliana Col malate + NH3
-
 ?
2-oxoglutaramate + H2O the product of glutamine transamination, 2-oxoglutaramate, can be hydrolyzed by the enzyme omega-amidase to form and ammonia Arabidopsis thaliana 2-oxoglutarate + NH3
-
 ?
2-oxoglutaramate + H2O the product of glutamine transamination, 2-oxoglutaramate, can be hydrolyzed by the enzyme omega-amidase to form and ammonia Arabidopsis thaliana Col 2-oxoglutarate + NH3
-
 ?
2-oxosuccinamate + H2O
-
 Arabidopsis thaliana oxaloacetate + NH3
-
 ?
2-oxosuccinamate + H2O the product of asparagine transamination, 2-oxosuccinamate, can be hydrolyzed by the enzyme omega-amidase to form oxaloacetate and ammonia Arabidopsis thaliana oxaloacetate + NH3
-
 ?
2-oxosuccinamate + H2O
-
 Arabidopsis thaliana Col oxaloacetate + NH3
-
 ?
2-oxosuccinamate + H2O the product of asparagine transamination, 2-oxosuccinamate, can be hydrolyzed by the enzyme omega-amidase to form oxaloacetate and ammonia Arabidopsis thaliana Col oxaloacetate + NH3
-
 ?
additional information the recombinant omega-amidase is equally active with 2-oxosuccinamate, 2-oxoglutaramate and 2-hydroxysuccinamate Arabidopsis thaliana ?
-
 ?
additional information the recombinant omega-amidase is equally active with 2-oxosuccinamate, 2-oxoglutaramate and 2-hydroxysuccinamate Arabidopsis thaliana Col ?
-
 ?

Subunits

Subunits Comment Organism
? x * 40300, about, sequence calculation, x * 34000, recombinant His-tagged enzyme without transit peptide, SDS-PAGe Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
 assay at Arabidopsis thaliana

General Information

General Information Comment Organism
metabolism omega-amidase is involved in the metabolism of asparagine, and probably is also closely coupled with glutamine transamination in the methionine salvage cycle Arabidopsis thaliana