(Q38563900)

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ω-Amidase: an underappreciated, but important enzyme in L-glutamine and L-asparagine metabolism; relevance to sulfur and nitrogen metabolism, tumor biology and hyperammonemic diseases.

scientific article published on 11 August 2015

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Europe PubMed Central

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22 February 2020

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Europe PubMed Central

ω-Amidase: an underappreciated, but important enzyme in L-glutamine and L-asparagine metabolism; relevance to sulfur and nitrogen metabolism, tumor biology and hyperammonemic diseases (English)

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22 February 2020

corrigendum / erratum

Erratum to: ω-Amidase: an underappreciated, but important enzyme in L-glutamine and L-asparagine metabolism; relevance to sulfur and nitrogen metabolism, tumor biology and hyperammonemic diseases.

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Boris Krasnikov

8

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22 February 2020

Travis T Denton

7

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22 February 2020

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Arthur J L Cooper

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22 February 2020

Yevgeniya I Shurubor

2

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22 February 2020

Thambi Dorai

3

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22 February 2020

John T Pinto

4

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22 February 2020

Elena P Isakova

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22 February 2020

Yulia I Deryabina

6

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22 February 2020

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11 August 2015

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22 February 2020

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22 February 2020

48

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22 February 2020

1

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22 February 2020

1-20

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22 February 2020

Functional Proteomic and Structural Insights into Molecular Recognition in the Nitrilase Family Enzymes † ‡

1 reference

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Catalysis in the nitrilase superfamily

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Pathophysiology of brain dysfunction in hyperammonemic syndromes: The many faces of glutamine

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Sulfur-containing cyclic ketimines and imino acids. A novel family of endogenous products in the search for a role

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Structural insights into the catalytic active site and activity of human Nit2/ω-amidase: kinetic assay and molecular dynamics simulation

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The role of glutamine transaminase K (GTK) in sulfur and alpha-keto acid metabolism in the brain, and in the possible bioactivation of neurotoxicants

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Fluorometric determination of alpha-ketosuccinamic acid in rat tissues

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Evidence that glutamine transaminase and omega-amidase potentially act in tandem to close the methionine salvage cycle in bacteria and plants.

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Concentrations of asparagine in tissues of prepubertal rats after enzymic or dietary depletion of asparagine (Short Communication)

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Mitochondrial aspartate aminotransferase: a third kynurenate-producing enzyme in the mammalian brain

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pH dependence, substrate specificity and inhibition of human kynurenine aminotransferase I.

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21 January 2018

Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II

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Biochemical and structural properties of mouse kynurenine aminotransferase III

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Alternative functions of the brain transsulfuration pathway represent an underappreciated aspect of brain redox biochemistry with significant potential for therapeutic engagement

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21 January 2018

Hits, Fhits and Nits: beyond enzymatic function.

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21 January 2018

Molecular identification of omega-amidase, the enzyme that is functionally coupled with glutamine transaminases, as the putative tumor suppressor Nit2.

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21 January 2018

Reduced kynurenine aminotransferase-I activity in SHR rats may be due to lack of KAT-Ib activity

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21 January 2018

Evidence for genetic heterogeneity in D-2-hydroxyglutaric aciduria

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21 January 2018

Assay and purification of omega-amidase/Nit2, a ubiquitously expressed putative tumor suppressor, that catalyzes the deamidation of the alpha-keto acid analogues of glutamine and asparagine

1 reference

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21 January 2018

Identification of the putative tumor suppressor Nit2 as omega-amidase, an enzyme metabolically linked to glutamine and asparagine transamination

1 reference

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21 January 2018

Urinary 2-hydroxy-5-oxoproline, the lactam form of α-ketoglutaramate, is markedly increased in urea cycle disorders.

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21 January 2018

A missense mutation in kynurenine aminotransferase-1 in spontaneously hypertensive rats.

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Metabolite damage and its repair or pre-emption

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21 January 2018

Identification of a mitochondrial form of kynurenine aminotransferase/glutamine transaminase K from rat brain

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Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.

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Asparagine catabolism in rat liver mitochondria

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21 January 2018

Tissue expression and translational control of rat kynurenine aminotransferase/glutamine transaminase K mRNAs

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Measurement of rat brain kynurenine aminotransferase at physiological kynurenine concentrations

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The concentration of asparagine in the tissues of rats treated with growth hormone

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Studies on the Mechanism of Glutamine Synthesis; Isolation and Properties of the Enzyme from Sheep Brain*

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Glutaminase activity determines cytotoxicity of L-asparaginases on most leukemia cell lines.

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Kynurenine aminotransferase III and glutamine transaminase L are identical enzymes that have cysteine S-conjugate β-lyase activity and can transaminate L-selenomethionine

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