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Literature summary for 5.2.1.8 extracted from

  • Wang, P.; Li, X.Z.; Cui, H.R.; Feng, Y.G.; Wang, X.Y.
    Identification and functional analysis of a novel parvulin-type peptidyl-prolyl isomerase from Gossypium hirsutum (2014), Plant Physiol. Biochem., 76, 58-66.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene PPI, phylogenetic analysis, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), expression of GhPPI-GFP fusion enzyme in onion epidermal cell nuclei from pBI121-GFP using Agrobacterium tumefaciens strain LBA4404 for transfection Gossypium hirsutum

Protein Variants

Protein Variants Comment Organism
C138A site-directed mutagenesis, the mutant shows 93% of wild-type activity Gossypium hirsutum
C41A site-directed mutagenesis, the mutant shows 104% of wild-type activity Gossypium hirsutum
C51A site-directed mutagenesis, the mutant shows 93% of wild-type activity Gossypium hirsutum
C90A site-directed mutagenesis, the mutant shows 35% of wild-type activity Gossypium hirsutum
F111A site-directed mutagenesis, the mutant shows 30% of wild-type activity Gossypium hirsutum
F111Y site-directed mutagenesis, the mutant shows 20% of wild-type activity Gossypium hirsutum
H131A site-directed mutagenesis, the mutant shows 19% of wild-type activity Gossypium hirsutum
H134A site-directed mutagenesis, the mutant shows 30% of wild-type activity Gossypium hirsutum
H48A site-directed mutagenesis, the mutant shows 7.8% of wild-type activity Gossypium hirsutum
M107A site-directed mutagenesis, the mutant shows 73% of wild-type activity Gossypium hirsutum
T130A site-directed mutagenesis, the mutant shows 68% of wild-type activity Gossypium hirsutum

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus
-
Gossypium hirsutum 5634
-

Organism

Organism UniProt Comment Textmining
Gossypium hirsutum Q4KNC9
-
-
Gossypium hirsutum ZM3 Q4KNC9
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Gossypium hirsutum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information purified recombinant GhPPI accelerates the initial velocity of the cis-trans conversion of peptidyl-prolyl bonds of a tetrapeptide in a GhPPI concentration-dependent manner. Recombinant GhPPI also suppresses protein aggregation under denaturing conditions using guanidine hydrochloride, suggesting an additional chaperone activity Gossypium hirsutum ?
-
?
additional information purified recombinant GhPPI accelerates the initial velocity of the cis-trans conversion of peptidyl-prolyl bonds of a tetrapeptide in a GhPPI concentration-dependent manner. Recombinant GhPPI also suppresses protein aggregation under denaturing conditions using guanidine hydrochloride, suggesting an additional chaperone activity Gossypium hirsutum ZM3 ?
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
Gossypium hirsutum ?
-
?
N-succinyl-Ala-Ala-Pro-Phe-4-nitroanilide
-
Gossypium hirsutum ZM3 ?
-
?

Subunits

Subunits Comment Organism
More three-dimensional structure of GhPPI by homology modeling, molecular docking, structure of the substrate binding site of GhPPI, overview Gossypium hirsutum

Synonyms

Synonyms Comment Organism
parvulin-type peptidyl-prolyl isomerase
-
Gossypium hirsutum
peptidyl-prolyl cis/trans isomerase
-
Gossypium hirsutum
PPIase
-
Gossypium hirsutum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Gossypium hirsutum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Gossypium hirsutum

Expression

Organism Comment Expression
Gossypium hirsutum mRNA accumulation of GhPPI is induced by salt stress up

General Information

General Information Comment Organism
evolution the enzyme belongs to the parvulin family of peptidyl-prolyl cis/trans isomerases, PPIases Gossypium hirsutum
additional information three-dimensional structure of GhPPI by homology modeling, molecular docking, structure of the substrate binding site of GhPPI, overview Gossypium hirsutum