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Literature summary for 3.5.1.119 extracted from

  • Eustis, I.C.; Huang, J.; Pilkerton, M.E.; Whedon, S.D.; Chatterjee, C.
    A time-resolved Foerster resonance energy transfer assay to measure activity of the deamidase of the prokaryotic ubiquitin-like protein (2015), Anal. Biochem., 487, 27-29 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.119

Application

Application Comment Organism
medicine since Dop is necessary for persistent infection by Mycobacterium tuberculosis, its selective inhibition holds potential for tuberculosis therapy Mycobacterium tuberculosis

Cloned(Commentary)

Cloned (Comment) Organism
-
 Corynebacterium glutamicum

Inhibitors

Inhibitors Comment Organism Structure
additional information in order to facilitate high-throughput screens for Dop inhibitors, a time-resolved Förster resonance energy transfer-based assay for enzyme (Dop) function is deleveloped. The time-resolved Förster resonance energy transfer-based assay is successfully applied to determine the Michaelis constant for ATP-binding and to test the co-factor tolerance of the enzyme Corynebacterium glutamicum
additional information in order to facilitate high-throughput screens for Dop inhibitors, a time-resolved Förster resonance energy transfer-based assay for enzyme (Dop) function is deleveloped. The time-resolved Förster resonance energy transfer-based assay is successfully applied to determine the Michaelis constant for ATP-binding and to test the co-factor tolerance of the enzyme Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum Q8NQE1
-
-
Corynebacterium glutamicum ATCC 13032 Q8NQE1
-
-
Mycobacterium tuberculosis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Corynebacterium glutamicum

Synonyms

Synonyms Comment Organism
deamidase of Pup
-
 Mycobacterium tuberculosis
deamidase of Pup
-
 Corynebacterium glutamicum
Dop
-
 Mycobacterium tuberculosis
Dop
-
 Corynebacterium glutamicum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Corynebacterium glutamicum
37
-
 assay at Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Mycobacterium tuberculosis
7.4
-
 assay at Corynebacterium glutamicum

Cofactor

Cofactor Comment Organism Structure
ATP absolutely required for enzyme function Mycobacterium tuberculosis
ATP absolutely required for enzyme function Corynebacterium glutamicum

General Information

General Information Comment Organism
metabolism the enzyme is essential for the infectivity of Mycobacterium tuberculosisis Mycobacterium tuberculosis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
additional information
-
 additional information in order to facilitate high-throughput screens for inhibitors, a time-resolved Förster resonance energy transfer-based assay for enzyme (Dop) function is deleveloped. The time-resolved Förster resonance energy transfer-based assay is successfully applied to determine the Michaelis constant for ATP-binding and to test the co-factor tolerance of the enzyme Mycobacterium tuberculosis
additional information
-
 additional information in order to facilitate high-throughput screens for Dop inhibitors, a time-resolved Förster resonance energy transfer-based assay for enzyme (Dop) function is deleveloped. The time-resolved Förster resonance energy transfer-based assay is successfully applied to determine the Michaelis constant for ATP-binding and to test the co-factor tolerance of the enzyme Corynebacterium glutamicum