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Literature summary for 1.5.1.30 extracted from

  • Leitsch, D.; Janssen, B.; Kolarich, D.; Johnson, P.; Duchene, M.
    Trichomonas vaginalis flavin reductase 1 and its role in metronidazole resistance (2014), Mol. Microbiol., 91, 198-208 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.5.1.30

Cloned(Commentary)

Cloned (Comment) Organism
gene TVAG_517010, DNA and amino acid sequence determination and analysis, quantitative RT-PCR expression analysis of FR1 in metronidazole-susceptible isolates C1, G3, JH31A and Tv2 , re-introduction of FR1 into an aerobically-resistant strain, transfection of the highly metronidazole-resistant isolate B7268 with the FR1 gene restores metronidazole susceptibility Trichomonas vaginalis

Inhibitors

Inhibitors Comment Organism Structure
riboflavin FR1 inhibition by possibly either by the semiquinone or the fully reduced form Trichomonas vaginalis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
FMNH2 + NADP+ Trichomonas vaginalis
-
 FMN + NADPH + H+
-
 r
FMNH2 + NADP+ Trichomonas vaginalis G3
-
 FMN + NADPH + H+
-
 r
additional information Trichomonas vaginalis FR is a relevant source of hydrogen peroxide but superoxide radical anions are a minor by-product of the reaction ?
-
 ?
additional information Trichomonas vaginalis G3 FR is a relevant source of hydrogen peroxide but superoxide radical anions are a minor by-product of the reaction ?
-
 ?

Organism

Organism UniProt Comment Textmining
Trichomonas vaginalis A2GH85
-
-
Trichomonas vaginalis G3 A2GH85
-
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information analysis of enzyme FR1 expression in metronidazole-susceptible isolates C1, G3, JH31A and Tv2: the highly metronidazole-resistant cell line of strain C1, C1res, and the clinical isolate B7268 lack detectable FRs. The residual FR activity found in CDC085 and LA1 likely results from alternative FRs that are highly expressed Trichomonas vaginalis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FMNH2 + NADP+
-
 Trichomonas vaginalis FMN + NADPH + H+
-
 r
FMNH2 + NADP+
-
 Trichomonas vaginalis G3 FMN + NADPH + H+
-
 r
additional information FR is a relevant source of hydrogen peroxide but superoxide radical anions are a minor by-product of the reaction Trichomonas vaginalis ?
-
 ?
additional information FR is a relevant source of hydrogen peroxide but superoxide radical anions are a minor by-product of the reaction Trichomonas vaginalis G3 ?
-
 ?

Synonyms

Synonyms Comment Organism
flavin reductase 1
-
 Trichomonas vaginalis
FR1
-
 Trichomonas vaginalis
TVAG_517010
-
 Trichomonas vaginalis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Trichomonas vaginalis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
 assay at Trichomonas vaginalis

Cofactor

Cofactor Comment Organism Structure
additional information FR1 displays only 3% activity when NADH is added instead of NADPH Trichomonas vaginalis
NADP+
-
 Trichomonas vaginalis
NADPH
-
 Trichomonas vaginalis

General Information

General Information Comment Organism
metabolism Trichomonas vaginalis has two different enzymatic pathways to remove intracellular oxygen, i.e. NADH oxidase, which is inhibited by metronidazole, and flavin reductase Trichomonas vaginalis
physiological function regarding all flavin reductase enzymes in Trichomonas vaginalis, FR1 is responsible for the flavin reductase activity. Hydrogen peroxide is the main if not the single product of FR1. FR1 displays a 10 to 20fold higher affinity to FMN than enzymes FR5 and FR6. Also the affinity of FR1 to FAD is at least 10fold higher than observed with FR5 and FR6 but the Vmax is considerably lower (roughly 33% of the Vmax for FMN). In contrast, FR5 and FR6 display higher affinity for riboflavin than FR1, which is inhibited by riboflavin Trichomonas vaginalis