Kynureninase - OmicsDI

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Metabolite Name

SM 9:1;2O/18:5 (1)
PC 17:1_18:1 (1)
2-(1H-benzimidazol-2-yl)-3-(1,3-benzodioxol-5-yl)acrylonitrile (1)
PC 9:0_9:0 (1)
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PC 32:4_28:6 (1)
PC 22:4_22:4 (1)
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PS 18:1_20:5 (1)
SHexCer 20:1;2O/17:0 (1)
PS 44:12 (1)
DGCC 42:6_44:12 (1)
TG 18:5_26:7_30:8 (1)
PC 18:0_19:1 (1)
LPC 30:0 (1)
PE O-26:7_18:4 (1)
PC 17:2_22:6 (1)
LPE 40:7 (1)
Deoxycytidine 5'-monophosphate (1)
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LPC 44:12 (1)
PC O-36:8 (1)
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Lab affiliation

CECAD-Cluster of Excellence, University of Cologne, Joseph-Stelzmann-Str. 26, D-50931, Cologne, Germany; Department II of Internal Medicine, Faculty of Medicine and University Hospital Cologne, University of Cologne, Kerpener Str. 62, D-50937, Cologne, Germany; Center for Molecular Medicine Cologne (CMMC), University of Cologne, Robert-Koch-Str. 21, D-50931, Cologne, Germany (1)
Department of Biology, University of Prince Edward Island (1)
Department of Chemistry and Biochemistry, The University of Texas at Dallas (1)

Tags

xref:PubMed:23359068 (1)
xref:PubMed:35928791 (1)

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Crystal structure of Homo sapiens kynureninase.

Not available

S-EPMC2531291 | biostudies-literature

Upregulated Kynurenine Pathway Enzymes in Aortic Atherosclerotic Aneurysm: Macrophage Kynureninase Downregulates Inflammation.

Not available

S-EPMC8592691 | biostudies-literature

Distinct mechanistic, conformational and substrate selectivity profiles emerging in the evolution of high catalytic activity enzymes via parallel trajectories

Recent laboratory evolution studies have demonstrated that parallel evolutionary trajectories can lead to genetically distinct enzymes with high activity towards a non-preferred substrate. However, it is unknown whether such genetically distinct enzymes have convergent conformational dynamics and me...

ORGANISM(S): Homo sapiens (Human)

2024-07-29 | PXD053893 | Pride