Literature summary for 3.4.24.64 extracted from

Janata, J.; Hola, K.; Kubala, M.; Gakh, O.; Parkhomenko, N.; Matuskova, A.; Kutejova, E.; Amler, E.
Substrate evokes translocation of both domains in the mitochondrial processing peptidase alpha-subunit during which the C-terminus acts as a stabilizing element (2004), Biochem. Biophys. Res. Commun., 316, 211-217.

Search for more literature for 3.4.24.64

Protein Variants

Protein Variants	Comment	Organism
delW481-F482	mutation has no effect on protein solubility, slightly unstable during long-term storage	Saccharomyces cerevisiae
W223F	mutation leads to a nearly entirely insoluble protein	Saccharomyces cerevisiae
W223M	mutation leads to an entirely insoluble protein	Saccharomyces cerevisiae
W481F	mutation has no effect on protein solubility	Saccharomyces cerevisiae
W481H	mutation has no effect on protein solubility	Saccharomyces cerevisiae
W481Y	mutation has no effect on protein solubility	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
mitochondrial malate dehydrogenase precursor + H2O	the extreme C-terminus of the alpha-subunit of mitochondrial processing peptidase provides mechanical support to the C-terminal domain of the protein during its extensive conformational change accompanying the substrate recognition site	Saccharomyces cerevisiae	mitochondrial malate dehydrogenase + mitochondrial malate dehydrogenase transit peptide	-	?

Synonyms

Synonyms	Comment	Organism
MPP	-	Saccharomyces cerevisiae

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)