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Literature summary for 1.5.1.37 extracted from

  • Loftie-Eaton, W.; Taylor, M.; Horne, K.; Tuffin, M.; Burton, S.; Cowan, D.
    Balancing redox cofactor generation and ATP synthesis key microaerobic responses in thermophilic fermentations (2013), Biotechnol. Bioeng., 110, 1057-1065 .
    View publication on PubMed
Search for more literature for 1.5.1.37

Cloned(Commentary)

Cloned (Comment) Organism
quantitative real-time PCR enzyme expression analysis Parageobacillus thermoglucosidasius

Protein Variants

Protein Variants Comment Organism
additional information substitution of an NADH dehydrogenase (downregulated) by an upregulated NADH:FAD oxidoreductase and upregulation of an ATP synthase subunit Parageobacillus thermoglucosidasius

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
FADH2 + NAD+ Parageobacillus thermoglucosidasius
-
 FAD + NADH + H+
-
 r
FADH2 + NAD+ Parageobacillus thermoglucosidasius NCIMB 11955
-
 FAD + NADH + H+
-
 r

Organism

Organism UniProt Comment Textmining
Parageobacillus thermoglucosidasius
-
-
-
Parageobacillus thermoglucosidasius NCIMB 11955
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FADH2 + NAD+
-
 Parageobacillus thermoglucosidasius FAD + NADH + H+
-
 r
FADH2 + NAD+
-
 Parageobacillus thermoglucosidasius NCIMB 11955 FAD + NADH + H+
-
 r

Synonyms

Synonyms Comment Organism
NADH:FAD oxidoreductase
-
 Parageobacillus thermoglucosidasius

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Parageobacillus thermoglucosidasius
NADH
-
 Parageobacillus thermoglucosidasius

Expression

Organism Comment Expression
Parageobacillus thermoglucosidasius upregulation of the NADH:FAD oxidoreductase due to silencing of an NADH dehydrogenase up

General Information

General Information Comment Organism
additional information substitution of an NADH dehydrogenase (down-regulated) by an up-regulated NADH:FAD oxidoreductase and upregulation of an ATP synthase subunit, alongside the observed shifts in the TCA cycle, suggested that an oxygen-scavenging electron transport chain likely remains active during low redox conditions Parageobacillus thermoglucosidasius