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Literature summary for 1.1.1.193 extracted from

  • Chen, S.; Yen, T.; Chang, T.; Liaw, S.
    Evolution of archaeal Rib7 and eubacterial RibG reductases in riboflavin biosynthesis Substrate specificity and cofactor preference (2018), Biochem. Biophys. Res. Commun., 503, 195-201 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D33A the mutant shows 0.1-0.6% activity compared to the wild type enzyme Methanosarcina mazei
D33K inactive Methanosarcina mazei
D33N inactive Methanosarcina mazei
D57N the mutant shows 0.1-0.6% activity compared to the wild type enzyme Methanosarcina mazei
E156Q inactive Methanosarcina mazei
K151A inactive Bacillus subtilis
K151D inactive Bacillus subtilis
K151E inactive Bacillus subtilis
N9A the mutant shows 0.1-0.6% activity compared to the wild type enzyme Methanosarcina mazei
R91A the mutation eliminates the endogenous NADPH binding and switches preference of the enzyme to NADH Methanosarcina mazei
S29A the mutant shows 0.1-0.6% activity compared to the wild type enzyme Methanosarcina mazei
S88E the mutation eliminates the endogenous NADPH binding and switches preference of the enzyme to NADH Methanosarcina mazei

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Methanosarcina mazei
-
-
-

Synonyms

Synonyms Comment Organism
Rib7
-
Methanosarcina mazei
RibG
-
Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Methanosarcina mazei