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Literature summary for 1.1.1.153 extracted from

  • Supangat, S.; Park, S.O.; Seo, K.H.; Lee, S.Y.; Park, Y.S.; Lee, K.H.
    Role of Phe-99 and Trp-196 of sepiapterin reductase from Chlorobium tepidum in the production of L-threo-tetrahydrobiopterin (2008), Acta Biochim. Biophys. Sin. (Shanghai), 40, 513-518.
    View publication on PubMed
Search for more literature for 1.1.1.153

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Chlorobaculum tepidum

Protein Variants

Protein Variants Comment Organism
F99A the mutant shows 3.9fold higher Km and lower Vmax (8.95%) than the wild type enzyme Chlorobaculum tepidum
W196A the mutant shows 8.7fold higher Km and lower Vmax (5.64%) than the wild type enzyme Chlorobaculum tepidum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00018
-
 sepiapterin wild type enzyme Chlorobaculum tepidum
0.00072
-
 sepiapterin mutant enzyme F99A Chlorobaculum tepidum
0.0016
-
 sepiapterin mutant enzyme W196A Chlorobaculum tepidum

Organism

Organism UniProt Comment Textmining
Chlorobaculum tepidum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA bead chromatography, MonoQ column chromatography, and Superdex 200 gel filtration Chlorobaculum tepidum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6-pyruvoyl tetrahydropterin + 2 NADPH + 2 H+
-
 Chlorobaculum tepidum L-threo-(6R,1'S,2'S)-5,6,7,8-tetrahydrobiopterin + NADP+
-
 ?
sepiapterin + NADPH + H+
-
 Chlorobaculum tepidum 7,8-dihydrobiopterin + NADP+
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
72
-
 the melting temperature of the wild type enzyme is at 72.77°C Chlorobaculum tepidum

Cofactor

Cofactor Comment Organism Structure
NADPH
-
 Chlorobaculum tepidum