Literature summary for 5.2.1.8 extracted from

Hennig, L.; Christner, C.; Kipping, M.; Schelbert, B.; Rucknagel, K.P.; Grabley, S.; Kullertz, G.; Fischer, G.
Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone (1998), Biochemistry, 37, 5953-5960.

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Cloned(Commentary)

Cloned (Comment)	Organism
mutant enzyme C69A	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
C69A	about one equivalent of 5-hydroxy-1,4-naphthoquinone results in complete inactivation of the mutant enzyme compared to two equivalent for the wild-type enzyme	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
5-hydroxy-1,4-naphthoquinone	i.e. juglone, 0.0057 mM, complete inhibition of wild-type and mutant C69A within 30 min, irreversible inhibition of the parvulin family of peptidyl-prolyl cis/trans isomerases, specific inhibition allows selective inactivation of these enzymes in presence of other peptidylprolyl isomerases, the inactivated parvulin contains two juglone molecules that are covalently bound to the side chains of Cys41 and Cys69, partial unfolding of the active site of the parvulins is thought to be the cause of the deterioration of peptidylprolyl isomerase activity	Escherichia coli
5-hydroxy-1,4-naphthoquinone	i.e. juglone, 0.0057 mM, complete inactivation within 150 min, irreversible inhibition of the parvulin family of peptidyl-prolyl cis/trans isomerases, specific inhibition allows selective inactivation of these enzymes in presence of other peptidylprolyl isomerases, the inactivated parvulin contains two juglone molecules that are covalently bound to the side chains of Cys41 and Cys69, partial unfolding of the active site of the parvulins is thought to be the cause of the deterioration of peptidylprolyl isomerase activity	Homo sapiens
5-hydroxy-1,4-naphthoquinone	i.e. juglone, 0.0057 mM, complete inactivation within 150 min, irreversible inhibition of the parvulin family of peptidyl-prolyl cis/trans isomerases, specific inhibition allows selective inactivation of these enzymes in presence of other peptidylprolyl isomerases, the inactivated parvulin contains two juglone molecules that are covalently bound to the side chains of Cys41 and Cys69, partial unfolding of the active site of the parvulins is thought to be the cause of the deterioration of peptidylprolyl isomerase activity	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-
Homo sapiens	-	-	-
Saccharomyces cerevisiae	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide	-	Homo sapiens	succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide	-	?
succinyl-Ala-Glu-(trans)-Pro-Phe-4-nitroanilide	-	Saccharomyces cerevisiae	succinyl-Ala-Glu-(cis)-Pro-Phe-4-nitroanilide	-	?
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide	-	Escherichia coli	succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide	-	?

Synonyms

Synonyms	Comment	Organism
Parvulin	-	Escherichia coli
Ptf1/Ess1	-	Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.0000559	-	5-hydroxy-1,4-naphthoquinone	mutant enzyme C69A	Escherichia coli

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Release 2023.1 (January 2023)