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Information on EC 5.2.1.8 - peptidylprolyl isomerase and Organism(s) Escherichia coli and UniProt Accession P0A9L5
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5.2.1.8 peptidylprolyl isomeraseIUBMB Comments
The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.
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Word Map
- 5.2.1.8
-
cyclosporine
-
immunophilins
-
isomerization
- calcineurin
- isomerases
- necrosis
- cardiac
- lymphocyte
- immunodeficiency
- capsid
-
ryanodine
- t-cells
- steroid
- glucocorticoid
- alzheimer
-
tetratricopeptide
- tacrolimus
-
refolding
- hsp70
- mtor
- interactor
- virion
- imperfecta
- gapdh
-
co-chaperone
-
genorm
- dnak
-
anti-hcv
- ptp
- groel
- legionella
-
osteogenesis
-
sarcoplasmic
- translocase
-
heterocomplexes
- pneumophila
-
voltage-dependent
-
phosphorylation-dependent
- ns5a
- analysis
-
ca2+-induced
-
direct-acting
- sirolimus
-
csa-induced
-
proline-directed
-
bestkeeper
-
excitation-contraction
- medicine
- ribavirin
-
emmprin
-
normfinder
-
ribosome-associated
- agriculture
- pharmacology
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
cyclophilin, cyclophilin a, fkbp12, ppiase, fkbp51, trigger factor, fkbp52, fk506-binding protein, peptidyl-prolyl isomerase, cyclophilin b, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
12 kDa FKBP
-
-
-
-
12.6 kDa FKBP
-
-
-
-
13 kDa FKBP
-
-
-
-
15 kDa FKBP
-
-
-
-
19 kDa FK506-binding protein
-
-
-
-
22 kDa FK506-binding protein
-
-
-
-
25 kDa FKBP
-
-
-
-
27 kDa membrane protein
-
-
-
-
36 kDa FK506 binding protein
-
-
-
-
40 kDa thylakoid lumen PPIase
-
-
-
-
40 kDa thylakoid lumen rotamase
-
-
-
-
51 kDa FK506-binding protein
-
-
-
-
52 kDa FK506 binding protein
-
-
-
-
54 kDa progesterone receptor-associated immunophilin
-
-
-
-
65 kDa FK506-binding protein
-
-
-
-
CGI-124
-
-
-
-
Chl-Mip
-
-
-
-
CPH
-
-
-
-
Cyclophilin
-
-
-
-
Cyclophilin 18
-
-
-
-
Cyclophilin 33
-
-
-
-
Cyclophilin A
-
-
-
-
Cyclophilin B
-
-
-
-
Cyclophilin C
-
-
-
-
Cyclophilin cyp2
-
-
-
-
Cyclophilin homolog
-
-
-
-
Cyclophilin ScCypA
-
-
-
-
Cyclophilin ScCypB
-
-
-
-
Cyclophilin-10
-
-
-
-
Cyclophilin-11
-
-
-
-
Cyclophilin-40
-
-
-
-
Cyclophilin-60
-
-
-
-
Cyclophilin-like protein Cyp-60
-
-
-
-
Cyclophilin-related protein
-
-
-
-
Cyclosporin A-binding protein
-
-
-
-
CYP-40
-
-
-
-
CYP-S1
-
-
-
-
Cyp3 PPIase
-
-
-
-
CyPA
-
-
-
-
CyPB
-
-
-
-
Estrogen receptor binding cyclophilin
-
-
-
-
FF1 antigen
-
-
-
-
FKBP
-
-
-
-
FKBP-12
-
-
-
-
FKBP-12.6
-
-
-
-
FKBP-13
-
-
-
-
FKBP-15
-
-
-
-
FKBP-19
-
-
-
-
FKBP-21
-
-
-
-
FKBP-22
-
-
-
-
FKBP-23
-
-
-
-
FKBP-25
-
-
-
-
FKBP-36
-
-
-
-
FKBP-51
-
-
-
-
FKBP-70
-
-
-
-
FKBP22
FKBP52 protein
-
-
-
-
FKBP54
-
-
-
-
FKBP59
-
-
-
-
FKBP65
-
-
-
-
FKBP65RS
-
-
-
-
FkpA
HBI
-
-
-
-
Histidine rich protein
-
-
-
-
hPar14
-
-
-
-
HSP binding immunophilin
-
-
-
-
HSP90-binding immunophilin
-
-
-
-
Immunophilin FKBP12
-
-
-
-
Immunophilin FKBP12.6
-
-
-
-
Immunophilin FKBP36
-
-
-
-
Immunophilin FKBP65
-
-
-
-
Isomerase, peptidylprolyl cis-trans
-
-
-
-
Macrolide binding protein
-
-
-
-
Macrophage infectivity potentiator
-
-
-
-
MtFK
-
-
-
-
Nucleolar proline isomerase
-
-
-
-
p17.7
-
-
-
-
P31
-
-
-
-
P54
-
-
-
-
p59 protein
-
-
-
-
Par14
-
-
-
-
Parvulin
Parvulin 14
-
-
-
-
Peptide bond isomerase
-
-
-
-
Peptidyl-prolyl cis-trans isomerase
Peptidyl-prolyl cis-trans isomerase plp
-
-
-
-
Peptidyl-prolyl cis-trans isomerase surA
-
-
-
-
Peptidyl-prolyl cis/trans isomerase EPVH
-
-
-
-
Peptidylprolyl cis-trans isomerase
-
-
-
-
PfCyP
-
-
-
-
Planta-induced rust protein 28
-
-
-
-
PPIase
PPIase Pin1
-
-
-
-
PPIase Pin4
-
-
-
-
Proline rotamase
-
-
-
-
Proteins, cyclophilins
-
-
-
-
Proteins, specific or class, cyclophilins
-
-
-
-
Rapamycin-binding protein
-
-
-
-
Rapamycin-selective 25 kDa immunophilin
-
-
-
-
Rotamase
-
-
-
-
Rotamase Pin1
-
-
-
-
Rotamase Pin4
-
-
-
-
Rotamase plp
-
-
-
-
S-cyclophilin
-
-
-
-
S1205-06
-
-
-
-
SCYLP
-
-
-
-
SmCYP A
-
-
-
-
SmCYP B
-
-
-
-
Smp17.7
-
-
-
-
SP18
-
-
-
-
WHP
-
-
-
-
FKBP22
-
-
-
-
Parvulin
-
-
-
-
Peptidyl-prolyl cis-trans isomerase
-
-
-
-
PPIase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
peptidylproline (omega=180) = peptidylproline (omega=0)
the refolding mechanism is similar in the presence and absence of the enzyme
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
Peptidylproline cis-trans-isomerase
The first type of this enzyme found [1] proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.
CAS REGISTRY NUMBER
COMMENTARY
95076-93-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Ala-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Lys-(cis)-Pro-Ala-Cys-(NO2)-Tyr-NH2
-
-
-
-
?
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Gly-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Lys-(cis)-Pro-Gly-Cys-(NO2)-Tyr-NH2
-
-
-
-
?
4-aminobenzoyl-Cys-Phe-(trans)-Pro-Val-Cys-(NO2)-Tyr-NH2
4-aminobenzoyl-Cys-Phe-(cis)-Pro-Val-Cys-(NO2)-Tyr-NH2
-
-
-
-
?
reduced carboxymethylated bovine alpha-lactalbumin
reduced carboxymethylated bovine alpha-lactalbumin
-
-
-
?
RNase A S-protein
RNase A S-protein
partially folded
action of enzyme greatly reduces the population of aggregated oligomeric species
-
?
succinyl-Ala-Ala-(cis)-Pro-Phe 4-methylcoumarin 7-amide
succinyl-Ala-Ala-(trans)-Pro-Phe + 7-amino-4-methylcoumarin
-
-
-
-
?
succinyl-Ala-Ala-Pro-Phe 4-nitroanilide
succinyl-Ala-Ala-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Glu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Glu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Gly-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Gly-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-His-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-His-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Leu-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Leu-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Lys-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Lys-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
Succinyl-Ala-Phe-(cis)-Pro-Phe 4-nitroanilide
Succinyl-Ala-Phe-(trans)-Pro-Phe 4-nitroanilide
-
-
-
-
?
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
RNAse T1
?
-
reduced and carboxymethylated RNAse T1, refolding by trans to cis isomerization of peptidyl-prolyl bonds at Pro39 and Pro55
-
?
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
succinyl-Ala-Phe-(trans)-Pro-Phe-4-nitroanilide
succinyl-Ala-Phe-(cis)-Pro-Phe-4-nitroanilide
-
-
-
?
additional information
?
-
-
increases the refolding of type IV procollagen
-
-
?
additional information
?
-
-
catalyzes the refolding of thermally denatured type III collagen
-
-
?
additional information
?
-
the enzyme has peptidylprolyl isomerase activity and chaperone activity
-
?
additional information
?
-
-
the enzyme has peptidylprolyl isomerase activity and chaperone activity
-
?
additional information
?
-
-
the folding of some exported proteins may be catalyzed by the periplasmic proline isomerase
-
-
?
additional information
?
-
-
trigger factor's peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins
-
?
additional information
?
-
-
PpiD interacts with misfolded proteins such as scrambled ribonuclease A or with D-somatostatin, with the amino acid sequence AGSKNFFWKTFTSS, and derived model peptides. Substrate specificity of PpiD is less specific than that for isoform SurA. The substrate specificity of PpiD is determined more by the hydrophobicity of residues in the model peptides than the presence of aromatic residues
-
-
?
additional information
?
-
-
peptidyl-prolyl cis-trans isomerase FKBP22 binds FK506 and rapamycin, that are both immunosuppressive drugs
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the folding of some exported proteins may be catalyzed by the periplasmic proline isomerase
-
-
?
additional information
?
-
-
trigger factor's peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(6,8aR)-6-N,N-monophenylimino-8a-carboxyindolizidin-5-one methyl ester
-
dissociation constant: above 0.2 mM
(6R,8a,R)-6-(2-methylnaphthyl)-N-tert-butoxycarbonyl-6-amino-8a-carboxyindolizidin-5-one methyl ester
-
dissociation constant: 0.017 mM
(6R,8aR)-6-(2-methylnaphthyl)-N-acetyl-6-amino-8a-carboxyindolizidin-5-one methyl ester
-
dissociation constant: 0.0015 mM
(6R,8aR)-6-(2-methylnaphthyl)-N-benzyloxycarbonyl-6-amino-8a-carboxyindolizidin-5-one methyl ester
-
dissociation constant: 0.047 mM
(6R,8aR)-6-(2-methylnaphthyl)-N-tert-butoxycarbonyl-6-amino-8a-indolizidine methyl ester
-
dissociation constant: 0.077 mM
(6R,8aR)-6-benzyl-6-N-tert-butoxycarbonylamino-8a-carboxyindolizidin-5-one methyl ester
-
dissociation constant: 0.14 mM
(6R,8aR)-6-benzyl-N-benzyloxycarbonyl-6-amino-8a-carboxyindolizidin-5-one methyl ester
-
dissociation constant: 0.124 mM
(6R,8aR)-6-N-tert-butoxycarbonylamino-8a-carboxyindolizidine methyl ester
-
dissociation constant: 0.2 mM
(6S,8aR)-6-N-tert-butoxycarbonylamino-8a-carboxyindolizidine methyl ester
-
dissociation constant: above 0.2 mM
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
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
96.9
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Gly-Cys-(NO2)-Tyr-NH2
-
wild type enzyme, with 50 mM dithiothreitol in 35 mM HEPES, pH 7.8, at 10°C
5.11
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Ala-Cys-(NO2)-Tyr-NH2
-
mutant enzyme, with 50 mM dithiothreitol in 35 mM HEPES, pH 7.8, at 10°C
115
4-aminobenzoyl-Cys-Lys-(trans)-Pro-Ala-Cys-(NO2)-Tyr-NH2
-
wild type enzyme, with 50 mM dithiothreitol in 35 mM HEPES, pH 7.8, at 10°C
3.45
4-aminobenzoyl-Cys-Phe-(trans)-Pro-Val-Cys-(NO2)-Tyr-NH2
-
mutant enzyme G148D, with 50 mM dithiothreitol in 35 mM HEPES, pH 7.8, at 10°C
1380
4-aminobenzoyl-Cys-Phe-(trans)-Pro-Val-Cys-(NO2)-Tyr-NH2
-
wild type enzyme, with 50 mM dithiothreitol in 35 mM HEPES, pH 7.8, at 10°C
30
RNase T1
mutant Y15A, pH not specified in the publication, temperature not specified in the publication
-
46
RNase T1
mutant I65P, pH not specified in the publication, temperature not specified in the publication
-
338
RNase T1
mutant A82P, pH not specified in the publication, temperature not specified in the publication
-
491
RNase T1
mutant V72P, pH not specified in the publication, temperature not specified in the publication
-
760
RNase T1
wild-type, pH not specified in the publication, temperature not specified in the publication
-
818
RNase T1
wild-type, pH not specified in the publication, temperature not specified in the publication
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
anionic enzyme form. Antibodies against the periplasmic enzyme form do not recognize the cytoplasmic enzyme, indicating significant differences in epitopes between the two forms
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
-
length of helix alpha3 contributes significantly to the preservation of the structure, function, and stability of Escherichia coli FKBP22. Homology modeling of the three-dimensional enzyme structure, overview
physiological function
-
colicin M unfolds during transfer across the outer or cytoplasmic membrane and refolds to the active form in the periplasm assisted by prolyl cis-trans isomerase/chaperone FkpA
physiological function
-
peptidyl-prolyl isomerase SLyD controls the recombinant folding of bacteriophage T4 long tail fiber fragments
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22960
-
2 * 23300, about, recombinant wild-type enzyme, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D5, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D30, sequence calculation, 2 * 23650, about, recombinant mutant rFKBP22I3, sequence calculation, 2 * 24140, about, recombinant mutant rFKBP22I6, sequence calculation
23300
-
2 * 23300, about, recombinant wild-type enzyme, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D5, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D30, sequence calculation, 2 * 23650, about, recombinant mutant rFKBP22I3, sequence calculation, 2 * 24140, about, recombinant mutant rFKBP22I6, sequence calculation
23650
-
2 * 23300, about, recombinant wild-type enzyme, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D5, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D30, sequence calculation, 2 * 23650, about, recombinant mutant rFKBP22I3, sequence calculation, 2 * 24140, about, recombinant mutant rFKBP22I6, sequence calculation
24140
-
2 * 23300, about, recombinant wild-type enzyme, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D5, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D30, sequence calculation, 2 * 23650, about, recombinant mutant rFKBP22I3, sequence calculation, 2 * 24140, about, recombinant mutant rFKBP22I6, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
dimer
245-residue subunit is divided into two domains, the overall form of the dimer is V-shaped, and the two C-terminal domains are located at the extremities of the V
dimer
-
2 * 23300, about, recombinant wild-type enzyme, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D5, sequence calculation, 2 * 22960, about, recombinant mutant rFKBP22D30, sequence calculation, 2 * 23650, about, recombinant mutant rFKBP22I3, sequence calculation, 2 * 24140, about, recombinant mutant rFKBP22I6, sequence calculation
additional information
structure analysis by multidimensional solution-state NMR spectroscopy, model of substrate binding pocket, comparison with human and plant proteins
additional information
-
structure analysis by multidimensional solution-state NMR spectroscopy, model of substrate binding pocket, comparison with human and plant proteins
additional information
-
PpiD interacts with misfolded proteins such as scrambled ribonuclease A or with D-somatostatin, with the amino acid sequence AGSKNFFWKTFTSS and derived model peptides
additional information
-
homology modeling of the three-dimensional enzyme structure, structures of the helix alpha3 mutants, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
NMR-study of enzyme and its complexes with substrates RNase A and reduced carboxymethylated bovine alpha-lactalbumin in solution. Molecular model of chaperone activity of enzyme
three different forms: 1. crystals of the full length native molecule are obtained by sitting drop vapour diffusion method, 2. crystals of the truncated form lacking the last 21 residues are obtained by hanging drop vapour diffusion method 3. crystals of the truncated form lacking the last 21 residues in complex with the immunosuppressant ligand, FK506, are obtained by hanging drop vapour diffusion method
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A82P
mutation in hinge region, 41% of wild-type activity. Unlike wild-type, the mutant unfolds by a non-two state mechanism in the presence of urea. Mutation affects both the shape and size of the protein significantly
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
E178V
-
slightly more active than wild-type enzyme with succinyl-Ala-Phe-Pro-Phe-4-nitroanilide, as active as wild-type enzyme in refolding of reduced and carboxymethylated RNAse T1, chaperone activity comparable with wild-type, not impaired in association with nascent proteins
F198A
-
inactive with succinyl-Ala-Phe-Pro-Phe-4-nitroanilide, inactive in refolding of reduced and carboxymethylated RNAse T1, chaperone activity comparable with wild-type, not impaired in association with nascent proteins
F233L
-
inactive with succinyl-Ala-Phe-Pro-Phe-4-nitroanilide, less active than wild-type enzyme in refolding of reduced and carboxymethylated RNAse T1, chaperone activity comparable with wild-type, not impaired in association with nascent proteins
G148D
-
the FkpA313 mutant protein, which contains a G148D replacement in the PPIase domain, shows only a very low in vitro PPIase activity with both peptides (the activity amounts to 0.4 and 0.2% that of wild type enzyme)
I42S
-
about 50% of wild-type peptidylprolyl isomerase activity, cells show moderate deficiency in nickel uptake under anaerobic conditions
I42S/F132Y
-
almost complete loss of peptidylprolyl isomerase activity, retains most of hydrogenase activity and cells show moderate deficiency in nickel uptake under anaerobic conditions
I65P
mutation in hinge region, 6% of wild-type activity. Unlike wild-type, the mutant unfolds by a non-two state mechanism in the presence of urea. Mutation affects both the shape and size of the protein significantly
V72P
mutation in hinge region, 60% of wild-type activity. Unlike wild-type, the mutant unfolds by a non-two state mechanism in the presence of urea
Y15A
residue Tyr 15 is indispensable for dimerization ability, catalytic activity, and structure but contributes little to its inhibitor binding ability and stability
Y221F
-
mutant enzyme shows 15% of the activity of the wild-type enzyme with succinyl-Ala-Phe-Pro-Phe-4-nitroanilide as substrate, less active than wild-type enzyme in refolding of reduced and carboxymethylated RNAse T1, chaperone activity comparable with wild-type, not impaired in association with nascent proteins
additional information
additional information
the deletion mutant comprising the N-terminal domain only, exists in solution as a mixture of monomeric and dimeric species, and exhibits chaperone activity. The deletion mutant comprising the C-terminal domain only is monomeric, and although it shows peptidylprolyl isomerase activity, it is devoid of chaperone function
additional information
-
the deletion mutant comprising the N-terminal domain only, exists in solution as a mixture of monomeric and dimeric species, and exhibits chaperone activity. The deletion mutant comprising the C-terminal domain only is monomeric, and although it shows peptidylprolyl isomerase activity, it is devoid of chaperone function
additional information
-
genetic inactivation of isoforms FkpA, PpiA, PpiD, SurA results in a viable strain with decreased growth rate and increased susceptibility to certain antibodies. Expression of P and type 1 pili is severely diminished in the quadruple mutant as well as in absence of SurA alone
additional information
-
the temperature-sensitive mutant FkpA43 confers 10% activity to colicin M at 30°C and no activity at 42°C, displays a 2fold lower PPIase activity than wild type FkpA for Phe-Pro-176-Val and a 5fold lower activity for Leu-Pro-260-Gly than for Phe-Pro-176-Val (measured at 10°C)
additional information
-
construction of FKBP22 four helix alpha3 mutant variants by various in vitro probes, rFKBP22D5 and rFKBP22D30 are deletion mutants, while rFKBP22I3 and rFKBP22I6 are insertion mutants. The molecular dimensions, dimerization efficiencies, secondary structures, tertiary structures, stabilities, and protein folding abilities of all mutant proteins differ from those of wild-type rFKBP22, but the rapamycin binding affinities of the mutant proteins are affected very little
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type rFKBP22, and mutants rFKBP22D5, rFKBPP22D30, rFKBP22I3, and rFKBP22I6 from Escherichia coli strain BL21(DE3) derivatives SAU1289, SAU1290, SAU1291, SAU1292, and SAU1293, respectively, by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged wild-type rFKBP22, and of mutants rFKBP22D5, rFKBPP22D30, rFKBP22I3, and rFKBP22I6 in Escherichia coli strains SAU1289, SAU1290, SAU1291, SAU1292, and SAU1293, respectively
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the N-terminal domain of peptidyl-prolyl isomerase SlyD (residues 1-165) is expressed in Escherichia coli BL21(DE3) cells
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes, urea-induced unfolding of wild-type and mutant enzymes follows a two-state mechanism and is reversible in nature, mechanism, overview
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Davis, J.M.; Boswell, B.A.; Bchinger, H.P.
Thermal stability and folding of type IV procollagen and effect of peptidyl-prolyl cis-trans-isomerase on the folding of the triple helix
J. Biol. Chem.
264
8956-8962
1989
Escherichia coli, Escherichia coli B / ATCC 11303
Compton, L.A.; Davis, J.M.; MacDonald, J.R.; Bchinger, H.P.
Structural and functional characterization of Escherichia coli peptidyl-prolyl cis-trans isomerases
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206
927-934
1992
Escherichia coli
Liu, J.; Walsh, C.T.
Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: A periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A
Proc. Natl. Acad. Sci. USA
87
4028-4032
1990
Escherichia coli
Hayano, T.; Takahashi, N.; Kato, S.; Maki, N.; Suzuki, M.
Two distinct forms of peptidylprolyl-cis-trans-isomerase are expressed separately in periplasmic and cytoplasmic compartments of Escherichia coli cells
Biochemistry
30
3041-3048
1991
Escherichia coli
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
Biochemistry
37
5953-5960
1998
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens
Kramer, G.; Patzelt, H.; Rauch, T.; Kurz, T.A.; Vorderwulbecke, S.; Bukau, B.; Deuerling, E.
Trigger factor's peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli
J. Biol. Chem.
279
14165-14179
2004
Escherichia coli
Wang, H.C.; Kim, K.; Bakhtiar, R.; Germanas, J.P.
Structure-activity studies of ground- and transition-State analogue inhibitors of cyclophilin
J. Med. Chem.
44
2593-2600
2001
Escherichia coli
Saul, F.A.; Arie, J.P.; Vulliez-le Normand, B.; Kahn, R.; Betton, J.M.; Bentley, G.A.
Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity
J. Mol. Biol.
335
595-608
2004
Escherichia coli (P45523), Escherichia coli
Justice, S.S.; Hunstad, D.A.; Harper, J.R.; Duguay, A.R.; Pinkner, J.S.; Bann, J.; Frieden, C.; Silhavy, T.J.; Hultgren, S.J.
Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli
J. Bacteriol.
187
7680-7686
2005
Escherichia coli
Kuehlewein, A.; Voll, G.; Alvarez, B.H.; Kessler, H.; Fischer, G.; Rahfeld, J.U.; Gemmecker, G.
Solution structure of Escherichia coli Par10: The prototypic member of the Parvulin family of peptidyl-prolyl cis/trans isomerases
Protein Sci.
13
2378-2387
2004
Escherichia coli (P0A9L5), Escherichia coli
Hu, K.; Galius, V.; Pervushin, K.
Structural plasticity of peptidyl-prolyl isomerase sFkpA is a key to its chaperone function as revealed by solution NMR
Biochemistry
45
11983-11991
2006
Escherichia coli (P45523)
Zhang, J.W.; Leach, M.R.; Zamble, D.B.
The peptidyl-prolyl isomerase activity of SlyD is not required for maturation of Escherichia coli hydrogenase
J. Bacteriol.
189
7942-7944
2007
Escherichia coli
Stymest, K.H.; Klappa, P.
The periplasmic peptidyl prolyl cis-trans isomerases PpiD and SurA have partially overlapping substrate specificities
FEBS J.
275
3470-3479
2008
Escherichia coli
Helbig, S.; Patzer, S.I.; Schiene-Fischer, C.; Zeth, K.; Braun, V.
Activation of colicin M by the FkpA prolyl cis-trans isomerase/chaperone
J. Biol. Chem.
286
6280-6290
2011
Escherichia coli, Escherichia coli AB2847
Chuprov-Netochin, R.; Amarantov, S.; Shneider, M.; Sykilinda, N.; Filchikov, M.; Ivanova, M.; Mesyanzhinov, V.; Miroshnikov, K.
Peptidyl-prolyl isomerase SLyD controls the recombinant folding of bacteriophage T4 long tail fiber fragments
Russ. J. Biopharm.
3
30-36
2011
Escherichia coli, Escherichia coli B/E1
-
Jana, B.; Sau, S.
The helix located between the two domains of a mip-like peptidyl-prolyl cis-trans isomerase is crucial for its structure, stability, and protein folding ability
Biochemistry
51
7930-7939
2012
Escherichia coli
Polley, S.; Chakravarty, D.; Chakrabarti, G.; Chattopadhyaya, R.; Sau, S.
Proline substitutions in a Mip-like peptidyl-prolyl cis-trans isomerase severely affect its structure, stability, shape and activity
Biochim. Open
1
28-39
2015
Escherichia coli (P0A9L3)
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