Literature summary for 3.7.1.5 extracted from

Weiss, A.K.H.; Naschberger, A.; Loeffler, J.R.; Gstach, H.; Bowler, M.W.; Holzknecht, M.; Cappuccio, E.; Pittl, A.; Etemad, S.; Dunzendorfer-Matt, T.; Scheffzek, K.; Liedl, K.R.; Jansen-Duerr, P.
Structural basis for the bi-functionality of human oxaloacetate decarboxylase FAHD1 (2018), Biochem. J., 475, 3561-3576 .

Search for more literature for 3.7.1.5

Cloned(Commentary)

Cloned (Comment)	Organism
expression in BL21(DE3) Escherichia coli LysS cells	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method at 18°C, crystal structure of the enzyme (FAHD1) protein in complex with its cofactor Mg2+, cocrystallization with oxalate and high resolution for the enzyme (FAHD1) in complex with oxalate	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
E33A	significant reduction in oxaloacetate decarboxylase activity and complete abrogation of the acylpyruvate hydrolase activity	Homo sapiens
H30A	significant reduction in oxaloacetate decarboxylase activity and complete abrogation of the acylpyruvate hydrolase activity	Homo sapiens
K123A	oxaloacetate decarboxylase activity and acylpyruvate hydrolase activity are abolished	Homo sapiens
additional information	mutation of amino acids H30, E33 and K123 each had discernible influence on the acylpyruvate hydrolase and/or oxaloacetate decarboxylase activity of FAHD1, suggesting distinct catalytic mechanisms for both activities	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
oxalate	competitive inhibitor	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0405	-	Acetylpyruvate	pH 7.4, 25°C, wild-type enzyme	Homo sapiens
0.0421	-	Acetylpyruvate	pH 7.4, 25°C, mutant enzyme E33A	Homo sapiens
0.0819	-	Acetylpyruvate	pH 7.4, 25°C, mutant enzyme H30A	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrion	-	Homo sapiens	5739	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q6P587	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
acetylpyruvate + H2O	bi-functional enzyme displaying both acylpyruvate hydrolase and oxaloacetate decarboxylase activity	Homo sapiens	acetate + pyruvate	-	?

Synonyms

Synonyms	Comment	Organism
FAH domain-containing protein 1	-	Homo sapiens
FAHD1	-	Homo sapiens

General Information

General Information	Comment	Organism
metabolism	the enzyme is important for mitochondrial function. It acts antagonistically to pyruvate carboxylase, a key metabolic enzyme	Homo sapiens

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Release 2023.1 (January 2023)