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Literature summary for 2.3.1.61 extracted from

  • Guo, H.; Madzak, C.; Du, G.; Zhou, J.
    Mutagenesis of conserved active site residues of dihydrolipoamide succinyltransferase enhances the accumulation of alpha-ketoglutarate in Yarrowia lipolytica (2016), Appl. Microbiol. Biotechnol., 100, 649-659.
    View publication on PubMed
Search for more literature for 2.3.1.61

Activating Compound

Activating Compound Comment Organism Structure
ATP
-
 Yarrowia lipolytica

Cloned(Commentary)

Cloned (Comment) Organism
subcloning in Escherichia coli strain JM109 Yarrowia lipolytica

Protein Variants

Protein Variants Comment Organism
D423A site-directed mutagenesis, the corresponding Km value of the D423A variant is 233% of the wild-type enzyme Km, while the kcat value of the variant is 4% compared to the wild-type enzyme Yarrowia lipolytica
D423E site-directed mutagenesis, the corresponding activity of the D423E variant is 30% of the wild-type activity Yarrowia lipolytica
D423G site-directed mutagenesis, the corresponding Km value of the D423S variant is 200% of the wild-type enzyme Km Yarrowia lipolytica
D423S site-directed mutagenesis, the corresponding Km value of the D423S variant is 161% of the wild-type enzyme Km, while the kcat value of the variant is 9% compared to the wild-type enzyme Yarrowia lipolytica
H419del site-directed mutagenesis, the mutant is almost inactive Yarrowia lipolytica
H419S site-directed mutagenesis, the mutant shows a the kcat value of 6% compared to the wild-type Yarrowia lipolytica

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Yarrowia lipolytica

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Yarrowia lipolytica 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Yarrowia lipolytica

Organism

Organism UniProt Comment Textmining
Yarrowia lipolytica Q6C5L8
-
-
Yarrowia lipolytica E 150 Q6C5L8
-
-

Synonyms

Synonyms Comment Organism
dihydrolipoamide succinyltransferase
-
 Yarrowia lipolytica
DLST
-
 Yarrowia lipolytica

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 assay at Yarrowia lipolytica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Yarrowia lipolytica

General Information

General Information Comment Organism
malfunction individual overexpression of dihydrolipoamide succinyltransferase, which serves as the inner core of KGDH, decreases overall activity of the enzyme complex, overexpression of mutated DLST not only impairs balanced assembly of KGDH, but also disrupts the catalytic integrity of the enzyme complex Yarrowia lipolytica
additional information the catalytic reaction of the enzyme depend on active site residues His419 and Asp423 Yarrowia lipolytica