Literature summary for 3.6.1.7 extracted from

Parrini, C.; Bemporad, F.; Baroncelli, A.; Gianni, S.; Travaglini-Allocatelli, C.; Kohn, J.E.; Ramazzotti, M.; Chiti, F.; Taddei, N.
The folding process of acylphosphatase from Escherichia coli is remarkably accelerated by the presence of a disulfide bond (2008), J. Mol. Biol., 379, 1107-1118.

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Protein Variants

Protein Variants	Comment	Organism
C5A/C49A	site-directed mutagenesis, the folding of the mutant lacking the disulfide bond is impaired and conformational stability is decreased compared to the wild-type enzyme, mutEcoAcP folds about 1500fold slower and a partially folded species accumulates int he mutant expressing strain	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics and thermodynamics of wild-type and mutant enzymes,overview	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AB65	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
folding and unfolding kinetics of wild-type and mutant enzymes at 28°C and pH 5.5 as a function of GdnHCl concentration, overview	Escherichia coli

Subunits

Subunits	Comment	Organism
More	structure determination and protein folding analysis of wild-type and mutant enzymes by far-UV and near-UV circular dichroism and dynamic light-scattering measurements, the protein folding of AcP is enhanced by disulfide bonds, overview	Escherichia coli

Synonyms

Synonyms	Comment	Organism
ACP	-	Escherichia coli

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Release 2023.1 (January 2023)