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Literature summary extracted from

  • Novotna, J.; Neuzil, J.; Hostalek, Z.
    Spectrophotometric identification of 8-hydroxy-5-deazaflavin. NADPH oxidoreductase activity in Streptomyces producing tetracyclines (1989), FEMS Microbiol. Lett., 59, 241-246.
No PubMed abstract available

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.40 Kitasatospora aureofaciens
-
-
-
1.5.1.40 Kitasatospora aureofaciens 84/25
-
-
-
1.5.1.40 Streptomyces rimosus
-
-
-
1.5.1.40 Streptomyces rimosus P
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.5.1.40 mycelium
-
 Kitasatospora aureofaciens
-
1.5.1.40 mycelium
-
 Streptomyces rimosus
-
1.5.1.40 spore
-
 Kitasatospora aureofaciens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.40 coenzyme F0 + NADPH + H+ i.e. 7,8-didemethyl-8-hydroxy-5-deazariboflavin. The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate Kitasatospora aureofaciens reduced coenzyme F0 + NADP+
-
 ?
1.5.1.40 coenzyme F0 + NADPH + H+ i.e. 7,8-didemethyl-8-hydroxy-5-deazariboflavin. The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate Streptomyces rimosus reduced coenzyme F0 + NADP+
-
 ?
1.5.1.40 coenzyme F0 + NADPH + H+ i.e. 7,8-didemethyl-8-hydroxy-5-deazariboflavin. The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate Streptomyces rimosus P reduced coenzyme F0 + NADP+
-
 ?
1.5.1.40 coenzyme F0 + NADPH + H+ i.e. 7,8-didemethyl-8-hydroxy-5-deazariboflavin. The enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate Kitasatospora aureofaciens 84/25 reduced coenzyme F0 + NADP+
-
 ?
1.5.1.40 coenzyme F420 + NADPH + H+ the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate. No activity with NAD+ Kitasatospora aureofaciens reduced coenzyme F420 + NADP+
-
 ?
1.5.1.40 coenzyme F420 + NADPH + H+ the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate. No activity with NAD+ Streptomyces rimosus reduced coenzyme F420 + NADP+
-
 ?
1.5.1.40 coenzyme F420 + NADPH + H+ the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate. No activity with NAD+ Streptomyces rimosus P reduced coenzyme F420 + NADP+
-
 ?
1.5.1.40 coenzyme F420 + NADPH + H+ the enzyme has an absolute requirement for both the 5-deazaflavin structure and the presence of an 8-hydroxy group in the substrate. No activity with NAD+ Kitasatospora aureofaciens 84/25 reduced coenzyme F420 + NADP+
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.5.1.40 37
-
 assay at Kitasatospora aureofaciens
1.5.1.40 37
-
 assay at Streptomyces rimosus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.5.1.40 7.4
-
 assay at Kitasatospora aureofaciens
1.5.1.40 7.4
-
 assay at Streptomyces rimosus

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.40 NADP+ no activity with NAD+ Kitasatospora aureofaciens
1.5.1.40 NADP+ no activity with NAD+ Streptomyces rimosus
1.5.1.40 NADPH no activity with NADH Kitasatospora aureofaciens
1.5.1.40 NADPH no activity with NADH Streptomyces rimosus