An enzyme that catalyzes the isomerization of proline residues within proteins. EC 5.2.1.8.
A family of immunophilin proteins that bind to the immunosuppressive drugs TACROLIMUS (also known as FK506) and SIROLIMUS. EC 5.2.1.-
Enzymes that catalyze the interconversion of aldose and ketose compounds.
Enzymes that catalyze either the racemization or epimerization of chiral centers within amino acids or derivatives. EC 5.1.1.
A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.
Enzymes that catalyze the shifting of a carbon-carbon double bond from one position to another within the same molecule. EC 5.3.3.
A family of peptidyl-prolyl cis-trans isomerases that bind to CYCLOSPORINS and regulate the IMMUNE SYSTEM. EC 5.2.1.-
Members of a family of highly conserved proteins which are all cis-trans peptidyl-prolyl isomerases (PEPTIDYLPROLYL ISOMERASE). They bind the immunosuppressant drugs CYCLOSPORINE; TACROLIMUS and SIROLIMUS. They possess rotamase activity, which is inhibited by the immunosuppressant drugs that bind to them.
A 17-KDa cytoplasmic PEPTIDYLPROLYL ISOMERASE involved in immunoregulation. It is a member of the cyclophilin family of proteins that binds to CYCLOSPORINE.
The phenomenon whereby certain chemical compounds have structures that are different although the compounds possess the same elemental composition. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
Enzymes that catalyze the epimerization of chiral centers within carbohydrates or their derivatives. EC 5.1.3.
A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.
Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Enzymes that catalyze the transposition of double bond(s) in a steroid molecule. EC 5.3.3.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
UNSATURATED FATTY ACIDS that contain at least one double bond in the trans configuration, which results in a greater bond angle than the cis configuration. This results in a more extended fatty acid chain similar to SATURATED FATTY ACIDS, with closer packing and reduced fluidity. HYDROGENATION of unsaturated fatty acids increases the trans content.
The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)

Preferential release of 11-cis-retinol from retinal pigment epithelial cells in the presence of cellular retinaldehyde-binding protein. (1/278)

In photoreceptor cells of the retina, photoisomerization of 11-cis-retinal to all-trans-retinal triggers phototransduction. Regeneration of 11-cis-retinal proceeds via a complex set of reactions in photoreceptors and in adjacent retinal pigment epithelial cells where all-trans-retinol is isomerized to 11-cis-retinol. Our results show that isomerization in vitro only occurs in the presence of apo-cellular retinaldehyde-binding protein. This retinoid-binding protein may drive the reaction by mass action, overcoming the thermodynamically unfavorable isomerization. Furthermore, this 11-cis-retinol/11-cis-retinal-specific binding protein potently stimulates hydrolysis of endogenous 11-cis-retinyl esters but has no effect on hydrolysis of all-trans-retinyl esters. Apo-cellular retinaldehyde-binding protein probably exerts its effect by trapping the 11-cis-retinol product. When retinoid-depleted retinal pigment epithelial microsomes were preincubated with different amounts of all-trans-retinol to form all-trans-retinyl esters and then [3H]all-trans-retinol was added, as predicted, the specific radioactivity of [3H]all-trans-retinyl esters increased during subsequent reaction. However, the specific radioactivity of newly formed 11-cis-retinol stayed constant during the course of the reaction, and it was largely unaffected by expansion of the all-trans-retinyl ester pool during the preincubation. The absence of dilution establishes that most of the ester pool does not participate in isomerization, which in turn suggests that a retinoid intermediate other than all-trans-retinyl ester is on the isomerization reaction pathway.  (+info)

Identification of a novel nutrient-deprivation-induced Sinorhizobium meliloti gene (hmgA) involved in the degradation of tyrosine. (2/278)

Sinorhizobium meliloti strain N4 carries a Tn5luxAB insertion in a gene which is induced by nitrogen and carbon deprivation as well as in the presence of tyrosine. The Tn5luxAB-tagged locus was found to share significant similarity with the human hmgA gene and the corresponding Aspergillus nidulans gene, encoding the enzyme homogentisate dioxygenase, which is involved in the degradation of tyrosine. Extended DNA sequence analysis of the tagged locus revealed the presence of several ORFs, including one encoding a polypeptide sharing a high degree of similarity with human and fungal maleylacetoacetate isomerases. Strain N4 was found to be unable to use tyrosine as carbon source, to lack homogentisate dioxygenase activity, to produce a melanin-like pigment and to be affected in stationary-phase survival. This is believed to be the first report of a hmgA-homologous gene in bacteria.  (+info)

Isolation and characterization of the cis-trans-unsaturated fatty acid isomerase of Pseudomonas oleovorans GPo12. (3/278)

Pseudomonas oleovorans contains an isomerase which catalyzes the cis-trans conversion of the abundant unsaturated membrane fatty acids 9-cis-hexadecenoic acid (palmitoleic acid) and 11-cis-octadecenoic acid (vaccenic acid). We purified the isomerase from the periplasmic fraction of Pseudomonas oleovorans. The molecular mass of the enzyme was estimated to be 80 kDa under denaturing conditions and 70 kDa under native conditions, suggesting a monomeric structure of the active enzyme. N-terminal sequencing showed that the isomerase derives from a precursor with a signal sequence which is cleaved from the primary translation product in accord with the periplasmic localization of the enzyme. The purified isomerase acted only on free unsaturated fatty acids and not on esterified fatty acids. In contrast to the in vivo cis-trans conversion of lipids, this in vitro isomerization of free fatty acids did not require the addition of organic solvents. Pure phospholipids, even in the presence of organic solvents, could not serve as substrate for the isomerase. However, when crude membranes from Pseudomonas or Escherichia coli cells were used as phospholipid sources, a cis-trans isomerization was detectable which occurred only in the presence of organic solvents. These results indicate that isolated membranes from Pseudomonas or E. coli cells must contain factors which, activated by the addition of organic solvents, enable and control the cis-trans conversion of unsaturated acyl chains of membrane phospholipids by the periplasmic isomerase.  (+info)

cis/trans isomerase of unsaturated fatty acids of Pseudomonas putida P8: evidence for a heme protein of the cytochrome c type. (4/278)

From a pool of 600 temperature-sensitive transposon mutants of Pseudomonas putida P8, 1 strain was isolated that carries a mini-Tn5 insertion within the cytochrome c operon. As a result, genes involved in the attachment of heme to cytochrome c-type proteins are turned off. Accordingly, cytochrome c could not be detected spectrophotometrically. The mutant also exhibited a remarkable reduction of cis-trans isomerization capability for unsaturated fatty acids. Consistent with the genetic and physiological data is the detection of a cytochrome c-type heme-binding motif close to the N terminus of the predicted polypeptide of the cis/trans isomerase (cti) gene (CVACH; conserved amino acids in italics). The functional significance of this motif was proven by site-directed mutagenesis. A possible mechanism of heme-catalyzed cis-trans isomerization of unsaturated fatty acids is discussed.  (+info)

Identification of RPE65 in transformed kidney cells. (5/278)

The protein RPE65 has an important role in retinoid processing and/or retinoid transport in the eye. Retinoids are involved in cell differentiation, embryogenesis and carcinogenesis. Since the kidney is known as an important site for retinoid metabolism, the expression of RPE65 in normal kidney and transformed kidney cells has been examined. The RPE65 mRNA was detected in transformed kidney cell lines including the human embryonic kidney cell line HEK293 and the African green monkey kidney cell lines COS-1 and COS-7 by reverse transcription PCR. In contrast, it was not detected in human primary kidney cells or monkey kidney tissues under the same PCR conditions. The RPE65 protein was also identified in COS-7 and HEK293 cells by Western blot analysis using a monoclonal antibody to RPE65, but not in the primary kidney cells or kidney tissues. The RPE65 cDNA containing the full-length encoding region was amplified from HEK293 and COS-7 cells. DNA sequencing showed that the RPE65 cDNA from HEK293 cells is identical to the RPE65 cDNA from the human retinal pigment epithelium. The RPE65 from COS-7 cells shares 98 and 99% sequence identity with human RPE65 at the nucleotide and amino acid levels, respectively. Moreover, the RPE65 mRNA was detected in three out of four renal tumor cultures analyzed including congenital mesoblastic nephroma and clear cell sarcoma of the kidney. These results demonstrated that transformed kidney cells express this retinoid processing protein, suggesting that these transformed cells may have an alternative retinoid metabolism not present in normal kidney cells.  (+info)

Involvement of the cis/trans isomerase Cti in solvent resistance of Pseudomonas putida DOT-T1E. (6/278)

Pseudomonas putida DOT-T1E is a solvent-resistant strain that is able to grow in the presence of high concentrations of toluene. We have cloned and sequenced the cti gene of this strain, which encodes the cis/trans isomerase, termed Cti, that catalyzes the cis-trans isomerization of esterified fatty acids in phospholipids, mainly cis-oleic acid (C(16:1,9)) and cis-vaccenic acid (C(18:1,11)), in response to solvents. To determine the importance of this cis/trans isomerase for solvent resistance a Cti-null mutant was generated and characterized. This mutant showed a longer lag phase when grown with toluene in the vapor phase; however, after the lag phase the growth rate of the mutant strain was similar to that of the wild type. The mutant also showed a significantly lower survival rate when shocked with 0.08% (vol/vol) toluene. In contrast to the wild-type strain, which grew in liquid culture medium at temperatures up to 38.5 degrees C, the Cti-null mutant strain grew significantly slower at temperatures above 37 degrees C. An in-frame fusion of the Cti protein with the periplasmic alkaline phosphatase suggests that this constitutively expressed enzyme is located in the periplasm. Primer extension studies confirmed the constitutive expression of Cti. Southern blot analysis of total DNA from various pseudomonads showed that the cti gene is present in all the tested P. putida strains, including non-solvent-resistant ones, and in some other Pseudomonas species.  (+info)

Molecular analysis of maleate cis-trans isomerase from thermophilic bacteria. (7/278)

Several strains of thermophilic bacteria containing maleate cis-trans isomerase were isolated from soil samples and identified as Bacillus stearothermophilus, Bacillus circulans, Bacillus brevis, and Deleya halophila. The maleate cis-trans isomerase was purified and characterized from one of the isolated strains, B. stearothermophilus MI-102. The purified enzyme of strain MI-102 showed higher thermal stability than the enzyme of a mesophile, Alcaligenes faecalis IFO13111. The seven maleate cis-trans isomerase genes (maiA) of thermophile were cloned and sequenced. B. stearothemophilus MI-102 MaiA has 67% amino acid identity with A. faecalis MaiA. All eight amino acid sequences of maiA gene products had significant conserved regions containing cysteine residues, which were previously suggested to be involved in an active site of the enzyme. To probe the catalytic mechanism, three cysteine residues in the conserved regions of A. faecalis MaiA were replaced with serine by site-directed mutagenesis. The results suggest that Cys80 and Cys198 play important roles in the enzyme activity.  (+info)

Rapid restoration of visual pigment and function with oral retinoid in a mouse model of childhood blindness. (8/278)

Mutations in the retinal pigment epithelium gene encoding RPE65 are a cause of the incurable early-onset recessive human retinal degenerations known as Leber congenital amaurosis. Rpe65-deficient mice, a model of Leber congenital amaurosis, have no rod photopigment and severely impaired rod physiology. We analyzed retinoid flow in this model and then intervened by using oral 9-cis-retinal, attempting to bypass the biochemical block caused by the genetic abnormality. Within 48 h, there was formation of rod photopigment and dramatic improvement in rod physiology, thus demonstrating that mechanism-based pharmacological intervention has the potential to restore vision in otherwise incurable genetic retinal degenerations.  (+info)

cis-trans-Isomerases at the US National Library of Medicine Medical Subject Headings (MeSH) v t e (Isomerases, All stub ... In biochemistry, cis-trans isomerase is a type of isomerase which catalyzes the isomerization of geometric isomers. Examples ...
... may refer to: Dodecenoyl-CoA isomerase, an enzyme Vinylacetyl-CoA Delta-isomerase, ...
... is an enzyme that in humans is encoded by the PIN4 gene. GRCh38: Ensembl ... 2000). "NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic ... 2001). "Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14". J. Mol. Biol. 305 (4): 917- ... "Entrez Gene: PIN4 protein (peptidylprolyl cis/trans isomerase) NIMA-interacting, 4 (parvulin)". Uchida T, Fujimori F, Tradler T ...
Galat A (September 1993). "Peptidylproline cis-trans-isomerases: immunophilins". Eur. J. Biochem. 216 (3): 689-707. doi:10.1111 ... two ubiquitous families of peptidyl-prolyl cis-trans isomerases". FASEB J. 6 (15): 3410-20. doi:10.1096/fasebj.6.15.1464374. ... These proteins have peptidyl prolyl isomerase activity, which catalyzes the isomerization of peptide bonds from trans form to ... also known as peptidylprolyl isomerase A (PPIA), which is found in the cytosol, has a beta barrel structure with two alpha ...
This cis-trans-isomerase contains glutathione as a coenzyme. Fumarylacetoacetate is finally split by the enzyme ... Fumarylacetoacetate is created by maleylacetoacetate cis-trans-isomerase through rotation of the carboxyl group created from ...
ISBN 978-3-527-30673-2. Otsuka K (January 1961). "Cis-trans Isomerase Isomerisation from Maleic Acid to Fumaric Acid". ... Purification and Properties of Maleate cis-trans Isomerase Induced by Malonate". Journal Agricultural and Biological Chemistry ... In enzymology, a maleate isomerase (EC 5.2.1.1), or maleate cis-tran isomerase, is a member of the Asp/Glu racemase superfamily ... "Analysis of oxidation sensitivity of maleate cis-trans isomerase from Serratia marcescens". Bioscience, Biotechnology, and ...
As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of ... PPIB is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of ... Peptidyl-prolyl cis-trans isomerase B is an enzyme that is encoded by the PPIB gene. ... Overview of all the structural information available in the PDB for UniProt: P23284 (Peptidyl-prolyl cis-trans isomerase B) at ...
... specifically cis-trans isomerases. The systematic name of this enzyme class is 3-maleylpyruvate cis-trans-isomerase. This ... Lack L (November 1961). "Enzymic cis-trans isomerization of maleylpyruvic acid". The Journal of Biological Chemistry. 236: 2835 ... In enzymology, a maleylpyruvate isomerase (EC 5.2.1.4) is an enzyme that catalyzes the chemical reaction 3-maleylpyruvate ⇌ {\ ... This enzyme belongs to the family of isomerases, ...
... specifically cis-trans isomerases. The systematic name of this enzyme class is all-trans-retinol 11-cis-trans-isomerase. This ... all-trans-retinol, and one product, 11-cis-retinol. These enzymes are alternatively referred to as retinoid isomerases. This ... Bernstein PS, Law WC, Rando RR (1987). "Isomerization of all-trans-retinoids to 11-cis-retinoids in vitro". Proc. Natl. Acad. ... Bridges CD, Alvarez RA (1987). "The visual cycle operates via an isomerase acting on all-trans retinol in the pigment ...
1999). Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts. Cell Mol Life Sci 55(3):423-36. ... 1994). A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli. FEBS Lett 343:65. Balbach J, Schmid FX. (2000). ... which catalyzes the cis-trans isomerization of proline peptide bonds. Although parvulin has no homology with larger prolyl ... 2006). The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production. Nature 440(7083): ...
This enzyme belongs to the family of isomerases, specifically cis-trans isomerases. The systematic name of this enzyme class is ... 4-olide cis-trans-isomerase. Other names in common use include 2-chlorocarboxymethylenebutenolide isomerase, and ... trans-2-chloro-4-carboxymethylenebut-2-en-1,4-olide Hence, this enzyme has one substrate, cis-2-chloro-4-carboxymethylenebut-2- ... In enzymology, a 2-chloro-4-carboxymethylenebut-2-en-1,4-olide isomerase (EC 5.2.1.10) is an enzyme that catalyzes the chemical ...
... acrylamide cis-trans-isomerase. It has 2 cofactors: NAD+, and NADH. Tomoeda M, Kitamura R (1977). "A cis-trans isomerising ... This enzyme belongs to the family of isomerases, specifically cis-trans isomerases. The systematic name of this enzyme class is ... Isomerization from 2-(2-furyl)-3-cis-(5-nitro-2-furyl) acrylamide (furylfuramide) to its trans isomer". Biochim. Biophys. Acta ... Portal: Biology v t e (EC 5.2.1, NADH-dependent enzymes, Enzymes of unknown structure, All stub articles, Isomerase stubs). ...
... specifically cis-trans isomerases. The systematic name of this enzyme class is 4-maleylacetoacetate cis-trans-isomerase. 4- ... In the phenylalanine degradation pathway, 4-maleylacetoacetate isomerase catalyzes a cis-trans isomerization of 4- ... 4-maleylacetoacetate isomerase has 3 isoforms The most common isoform has two domains, the N-terminal domain (4-87) the C ... Maleylacetoacetate isomerase deficiency is a disease caused by a mutation in the gene GSTZ1. This is an autosomal recessive ...
"A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase". Nature. 341 (6244): 758-60. Bibcode: ...
It is converted to fumarylacetoacetate by the enzyme 4-maleylacetoacetate cis-trans-isomerase. Gluthathione coenzymatically ...
Peptidyl-prolyl cis-trans isomerase FKBP1A is an enzyme that in humans is encoded by the FKBP1A gene. The protein encoded by ... This encoded protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 (tacrolimus) and rapamycin ( ... a peptidylprolyl cis-trans isomerase distinct from cyclophilin". Proceedings of the National Academy of Sciences of the United ... the functional role of peptidyl prolyl cis/trans isomerases". FEBS Letters. 495 (1-2): 1-6. doi:10.1016/S0014-5793(01)02326-2. ...
2011). "Parvulin 17 promotes microtubule assembly by its peptidyl-prolyl cis/trans isomerase activity". Journal of Molecular ...
This encoded protein is a cis-trans prolyl isomerase that binds to the immunosuppressants FK506 and rapamycin. It has high ... the functional role of peptidyl prolyl cis/trans isomerases". FEBS Letters. 495 (1-2): 1-6. doi:10.1016/S0014-5793(01)02326-2. ... Galigniana MD, Radanyi C, Renoir JM, Housley PR, Pratt WB (May 2001). "Evidence that the peptidylprolyl isomerase domain of the ... "The emerging role of peptidyl-prolyl isomerase chaperones in tau oligomerization, amyloid processing, and Alzheimer's disease ...
Pirkl F, Buchner J (May 2001). "Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, ... This encoded protein is a cis-trans prolyl isomerase that binds to the immunosuppressants tacrolimus (FK506) and sirolimus ( ... the functional role of peptidyl prolyl cis/trans isomerases". FEBS Letters. 495 (1-2): 1-6. doi:10.1016/S0014-5793(01)02326-2. ...
This gene encodes a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans ... As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of ... a novel domain of peptidyl-prolyl cis-trans isomerase". Biochemical and Biophysical Research Communications. 333 (3): 845-9. ... Agarwal, PK (Aug 2004). "Cis/trans isomerization in HIV-1 capsid protein catalyzed by cyclophilin A: insights from ...
Peptidyl-prolyl cis-trans isomerase FKBP1B is an enzyme that in humans is encoded by the FKBP1B gene. The protein encoded by ... This encoded protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 (tacrolimus) and rapamycin ( ... the functional role of peptidyl prolyl cis/trans isomerases". FEBS Letters. 495 (1-2): 1-6. doi:10.1016/S0014-5793(01)02326-2. ...
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 is an enzyme that in humans is encoded by the PIN1 gene. Pin 1, or ... Campbell HD, Webb GC, Fountain S, Young IG (Sep 1997). "The human PIN1 peptidyl-prolyl cis/trans isomerase gene maps to human ... Kim G, Bhattarai PY, Choi HS (February 2019). "Peptidyl-prolyl cis/trans isomerase NIMA-interacting 1 as a molecular target in ... Overview of all the structural information available in the PDB for UniProt: Q13526 (Peptidyl-prolyl cis-trans isomerase NIMA- ...
"Control of carotenoid biosynthesis through a heme-based cis-trans isomerase". Nature Chemical Biology. 11 (8): 598-605. doi: ...
"Biosynthesis of cyclosporins and other natural peptidyl prolyl cis/trans isomerase inhibitors". Biochimica et Biophysica Acta ( ...
Lawen A (October 2015). "Biosynthesis of cyclosporins and other natural peptidyl prolyl cis/trans isomerase inhibitors". ... Clinical trial number NCT01287078 for "Cyclosporine Inhalation Solution (CIS) in Lung Transplant and Hematopoietic Stem Cell ...
crtH catalyzes the isomerization of cis-carotenes into trans-carotenes through carotenoid isomerase. crtG encodes for ...
Par14 (eukaryotic homolog of parvulin, EHPF) is a member of the parvulin family of peptidyl-prolyl-cis/trans-isomerases ( ... Saningong, Akuma D.; Bayer, Peter (2015). "Human DNA-binding peptidyl-prolyl cis/Trans isomerase Par14 is cell cycle ... Reimer T (2003), Cellular localization and function of peptidyl-prolyl cis-trans isomerase hPar14. PhD thesis Sekerina, Elena; ... "Identification and characterization of a 14 k Da human protein as a novel parvulin-like peptidyl prolyl cis /Trans isomerase". ...
... belongs to the FKBP-type peptidyl-prolyl cis/trans isomerase (PPIase) family. Members of this family exhibit PPIase ...
Par17, a member of the parvulin family of peptidyl-prolyl-cis/trans-isomerases (PPIases), is an isoform of parvulin 14 (Par14) ... "Parvulin 17 Promotes Microtubule Assembly by Its Peptidyl-Prolyl Cis/Trans Isomerase Activity". Journal of Molecular Biology. ...
The protein encoded by this gene belongs to the FKBP-type peptidyl-prolyl cis/trans isomerase family. It is located in ...
... for the trans isomer (antiperiplanar conformation). Amide groups can isomerize about the C'-N bond between the cis and trans ... Both of these mechanisms for lowering the activation energy have been observed in peptidyl prolyl isomerases (PPIases), which ... The trans form is preferred overwhelmingly in most peptide bonds (roughly 1000:1 ratio in trans:cis populations). However, X- ... The partial double bond renders the amide group planar, occurring in either the cis or trans isomers. In the unfolded state of ...
It is also rarer than the PPII conformation because the cis isomer is higher in energy than the trans. Its typical dihedral ... this interconversion may be catalyzed by specific isomerases known as prolyl isomerases or PPIases. The interconversion between ... due to the high activation energy of X-Pro cis-trans isomerization (Ea ≈ 20 kcal/mol); however, ... The rotation angle Ω per residue of any polypeptide helix with trans isomers is given by the equation 3 cos ⁡ Ω = 1 − 4 cos 2 ...
Oligomerization and trans-phosphorylation of Ire1p (Ern1p) are required for kinase activation". The Journal of Biological ... Yoshida H, Haze K, Yanagi H, Yura T, Mori K (December 1998). "Identification of the cis-acting endoplasmic reticulum stress ... protein disulfide isomerases facilitate formation of disulfide bonds, which confer structural stability to the protein in order ...
This encoded protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin. It has a higher ... provides an overview of all the structure information available in the PDB for Human Peptidyl-prolyl cis-trans isomerase FKBP3 ... provides an overview of all the structure information available in the PDB for Mouse Peptidyl-prolyl cis-trans isomerase FKBP3 ...
Peptidyl-prolyl cis-trans isomerase-like 2 is an enzyme that in humans is encoded by the PPIL2 gene. This gene is a member of ... "Entrez Gene: PPIL2 peptidylprolyl isomerase (cyclophilin)-like 2". Wang BB, Hayenga KJ, Payan DG, Fisher JM (1996). " ... 2010). "Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases". PLOS Biol. ... the cyclophilin family of peptidylprolyl isomerases. The cyclophilins are a highly conserved ubiquitous family, members of ...
15-cis-zeta-carotene isomerase) is an enzyme with systematic name 9,15,9'-tricis-zeta-carotene cis-trans-isomerase. This enzyme ... Zeta-carotene+isomerase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 5.2.1). ... Li F, Murillo C, Wurtzel ET (June 2007). "Maize Y9 encodes a product essential for 15-cis-zeta-carotene isomerization". Plant ... ζ-Carotene isomerase (EC 5.2.1.12, Z-ISO, ...
11-cis-3-hydroxyretinal + (3R)-all-trans-3-hydroxyretinal The enzyme from the moth Galleria mellonella and the fruit fly ... "NinaB combines carotenoid oxygenase and retinoid isomerase activity in a single polypeptide". Proceedings of the National ... cis-isomerizing). This enzyme catalyses the following chemical reaction zeaxanthin + O2 ⇌ {\displaystyle \rightleftharpoons } ( ...
... both drugs act via an effect on an intranuclear isomerase, topoisomerase II, and peptide cis-trans-isomerase, respectively; ... Schabel FM, Trader MW, Laster WR, Corbett TH, Griswold DP (1979). "cis-Dichlorodiammineplatinum(II): combination chemotherapy ...
... (EC 5.2.1.14, DWARF27 (gene)) is an enzyme with systematic name beta-carotene 9-cis-all-trans isomerase ... This enzyme catalyses the following chemical reaction all-trans-beta-carotene ⇌ {\displaystyle \rightleftharpoons } 9-cis-beta- ... Beta-carotene+isomerase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (Articles with ...
The loops being with Thr132 in the active site and ends with a cis-peptide bond to Pro138. A Met137 residue plugs a hole in the ... Through FLIM FRET, it was shown that CHS interacts with chalcone isomerase (CHI), a consecutive step enzyme, as well as other ... of a Chimeric Chalcone Synthase Gene into Petunia Results in Reversible Co-Suppression of Homologous Genes in trans". Plant ... Cain CC, Saslowsky DE, Walker RA, Shirley BW (October 1997). "Expression of chalcone synthase and chalcone isomerase proteins ...
These observed phenomena are due to the trans-cis isomerization of the vinyl trans double bond in the p-coumaric acid. ... "Structural Coupling Throughout the Active Site Hydrogen Bond Networks of Ketosteroid Isomerase and Photoactive Yellow Protein ... Oxyanion holes exist in enzymes to stabilize transitions states of reaction intermediates, thus stabilizing the trans-cis ... Upon transitioning to the cis-isomeric form of p-coumaric acid the favorable hydrogen bonds are no longer in close interaction ...
If the acyl CoA contains a cis-Δ3 bond, then cis-Δ3-Enoyl CoA isomerase will convert the bond to a trans-Δ2 bond, which is a ... β-Oxidation of unsaturated fatty acids poses a problem since the location of a cis bond can prevent the formation of a trans-Δ2 ... Trans-delta2-enoyl CoA is hydrated at the double bond to produce L-3-hydroxyacyl CoA by enoyl-CoA hydratase. L-3-hydroxyacyl ... This is catalyzed by acyl CoA dehydrogenase to produce trans-delta 2-enoyl CoA. It uses FAD as an electron acceptor and it is ...
The cis-Pro formation is associated with an increase in Ssu72. Scp1 on recognizes trans-Pro formations, and is not affected by ... Peptidyl-prolyl isomerase, or PPIase, is an enzyme very commonly associated with proline isomerization due to their ability to ... Similar to aspartic acid, the amino acid proline has the rare property of being able to occupy both cis and trans isomers of ... In epigenetics, proline isomerization is the effect that cis-trans isomerization of the amino acid proline has on the ...
When it absorbs a photon, 11-cis-retinal undergoes photoisomerization to all-trans-retinal, which changes the conformation of ... and then converted to 11-cis-retinol by the isomerohydrolase RPE65. The isomerase activity of RPE65 has been shown; it is ... The retinal undergoes isomerisation, changing from the 11-cis-retinal to the all-trans-retinal configuration. Opsin therefore ... Following photoisomerization, all-trans-retinal is released from the opsin protein and reduced to all-trans-retinol, which ...
... homologous ninaB enzyme in Drosophila has both retinal-forming carotenoid-oxygenase activity and all-trans to 11-cis isomerase ... all-trans-retinal; all-trans-retinal + NADPH + H+ → all-trans-retinol + NADP+; all-trans-retinol dehydrogenases; all-trans- ... 11-cis-retinol + fatty acid; RPE65 isomerohydrolases; 11-cis-retinol + NAD+ → 11-cis-retinal + NADH + H+; 11-cis-retinol ... In these molecules, light causes the all-trans-retinal to become 13-cis retinal, which then cycles back to all-trans-retinal in ...
... zeta-carotene desaturase and carotene cis-trans isomerase) called the poly-cis pathway and leads to the red colored lycopene. ... PDS converts 15-cis-phytoene into 9,15,9'-tri-cis-ζ-carotene through reduction of the enzymes non-covalently bound FAD cofactor ... 15-cis-phytoene desaturases (PDS, plant-type phytoene desaturases) (EC 1.3.5.5, 15-cis-phytoene:plastoquinone oxidoreductase), ... Breitenbach J, Sandmann G (March 2005). "zeta-Carotene cis isomers as products and substrates in the plant poly-cis carotenoid ...
... trans-Isomerase (HP0175)-Mediated Induction of IL-6 Release from Macrophages". The Journal of Immunology. 195 (4): 1902. doi: ... and Stress-Activated Protein Kinase 1-Triggered Phosphorylation Events Are Central to Helicobacter pylori Peptidyl Prolyl cis ... trans-Isomerase (HP0175)-Mediated Induction of IL-6 Release from Macrophages". Retrieved 2 May 2018. {{cite journal}}: Cite ... and Stress-Activated Protein Kinase 1-Triggered Phosphorylation Events Are Central to Helicobacter pylori Peptidyl Prolyl cis ...
... trans-2-cis-3-decenoyl-ACP isomerase, trans-2,cis-3-decenoyl-ACP isomerase, trans-2-decenoyl-ACP isomerase, and FabM. Brock DJ ... The systematic name of this enzyme class is decenoyl-[acyl-carrier-protein] Delta2-trans-Delta3-cis-isomerase. Other names in ... In enzymology, a trans-2-decenoyl-[acyl-carrier protein] isomerase (EC 5.3.3.14) is an enzyme that catalyzes the chemical ... cis-dec-3-enoyl-[acyl-carrier-protein] Hence, this enzyme has one substrate, [[trans-dec-2-enoyl-[acyl-carrier-protein]]], and ...
"Periplasmic Peptidyl Prolyl cis-trans Isomerases Are Not Essential for Viability, but SurA Is Required for Pilus Biogenesis in ...
4.4 cis-trans prolyl isomerases. 4. 4.5 Related to spliceosome. 48. V. Possible splicing related Proteins. 51. ...
peptidyl-prolyl cis-trans isomerase FKBP10. *peptidyl-prolyl cis-trans isomerase FKBP10 precursor ...
5.2 cis-trans-Isomerases. 5.2.1 cis-trans Isomerases (only sub-subclass identified to date). 5.2.1.8 peptidylprolyl isomerase. ... Peptidyl prolyl isomerase. Cyclophilin. 4331972. Ubiquitin system [BR:osa04121]. Ubiquitin ligases (E3). U-box type E3. 4331972 ...
FKBP-type peptidyl-prolyl cis-trans isomerase -related …. swissprot. blastx. No significant hits ( or none blast was used over ... immunophilin-related / FKBP-type peptidyl-prolyl cis-trans isomerase-related [Arabidopsis thali…. ... IPR001179 Peptidylprolyl isomerase, FKBP-type. Prediction based on longest six frame method >SGN-P153652 (100 Aa). ... Peptidylprolyl isomerase. FKBP-type. - Biological Process: protein folding (GO:0006457). 4. *i value: controls inflation, a ...
... tularensis peptidyl-propyl cis-trans isomerase gene (GenBank accession no. CP003048). Babesia spp.-specific DNA was amplified ...
142 Phosphorylation of PKM2 on Ser37 leads to recruitment of peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), ... Several succinate receptor ligands have been described, including the succinate receptor agonizts cis-epoxysuccinic acid (cESA ... Mitochondrial citrate is converted into isocitrate via cis-aconitate by the enzyme aconitase of the TCA cycle (Fig. 2). ... Itaconate is generated through decarboxylation of cis-aconitate by immunoresponsive gene 1 (IRG-1) in the mitochondrial matrix ...
Finally, Pin1 peptidyl-prolyl cis/trans isomerase was proposed to restore the capacity of CDK-phosphorylated Tau to bind to the ... Lu, P. J., Wulf, G., Zhou, X. Z., Davies, P., and Lu, K. P. (1999). The prolyl isomerase Pin1 restores the function of ...
Isomerase, Proline Isomerase, Prolyl PPIase Peptidyl Prolyl cis trans Isomerase Peptidyl-Prolyl cis-trans-Isomerase Proline ... Isomerase, Prolyl. PPIase. Peptidyl Prolyl cis trans Isomerase. Peptidyl-Prolyl cis-trans-Isomerase. Proline Isomerase. Proline ... Peptidyl-Prolyl Cis-Trans Isomerase NIMA-Interacting 4 [D08.811.399.325.500.850] Peptidyl-Prolyl Cis-Trans Isomerase NIMA- ... Isomerase Proline Rotamase Prolyl Isomerase Rotamase, Proline cis-trans-Isomerase, Peptidyl-Prolyl ...
cis-trans-Isomerases. Enzymes that catalyze the rearrangement of geometry about double bonds. EC 5.2.. ... Cyclic-GMP PhosphodiesterasesPeripherinsGuanylate Cyclase-Activating Proteinscis-trans-IsomerasesPhotoreceptors, MicrobialCone ... Cyclic-GMP PhosphodiesterasesPeripherinsGuanylate Cyclase-Activating Proteinscis-trans-IsomerasesOcular Physiological Phenomena ... In the vertebrate photoreceptor cells, all-trans-retinal is released and replaced by a newly synthesized 11-cis-retinal ... ...
peptidyl-prolyl cis-trans isomerase activity. IEP. Enrichment. MF. GO:0004109. coproporphyrinogen oxidase activity. IEP. ... ribose-5-phosphate isomerase activity. IEP. Enrichment. MF. GO:0004852. uroporphyrinogen-III synthase activity. IEP. Enrichment ... isomerase activity. IEP. Enrichment. MF. GO:0016859. cis-trans isomerase activity. IEP. Enrichment. ...
peptidyl-prolyl cis-trans isomerase activity. IEP. Neighborhood. MF. GO:0005338. nucleotide-sugar transmembrane transporter ... cis-trans isomerase activity. IEP. Neighborhood. BP. GO:0017186. peptidyl-pyroglutamic acid biosynthetic process, using ...
Cis-trans-Isomerases (3) * Nanopartículas (3) * Neovascularização Retiniana (2) * Inibidores da Angiogênese (2) ...
Peptidyl-prolyl cis/trans isomerases C. *Phosphatases *Class I classical (Cys-based) phosphatases*Dual specificity phosphatases ...
FKBP-like peptidyl-prolyl cis-trans isomerase family protein. External link. http://www.arabidopsis.org/servlets/TairObject? ...
Peptidyl-Prolyl Cis-Trans Isomerase D; PPIase D; 40 kDa Peptidyl-Prolyl Cis-Trans Isomerase; Cyclophilin-40; CYP-40; ...
FKBP-type peptidyl-prolyl cis-trans isomerase. 1.0E-23. 17. 115. ... FKBP-type peptidyl-prolyl cis-trans isomerase. Proteins with at ... FKBP-type peptidyl-prolyl cis-trans isomerase. 3.5E-33. 31. 122. ... FKBP-type peptidyl-prolyl cis-trans isomerase. 6.2E-32. 393. ... FKBP-type peptidyl-prolyl cis-trans isomerase. 6.5E-28. 15. 114. ...
peptidyl-prolyl cis-trans isomerase domain-containing protein 12, 229. DVU2092. thiamine biosynthesis protein ThiF 161, 304. ...
... "peptidyl-prolyl cis-trans isomerase, cyclophilin-type [Ensembl]. Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain [ ... ","Protein-disulfide isomerase [Ensembl]. Thioredoxin [Interproscan].","protein_coding" "CRN76961","No alias","Pseudomonas ... ","arsenical resistance operon trans-acting repressor ArsD [Ensembl].","protein_coding" "AGT26848","N559_5274","Klebsiella ... ","periplasmic protein disulfide isomerase I [Ensembl]. DSBA-like thioredoxin domain [Interproscan].","protein_coding" " ...
Analysis of peptidyl-propyl-cis/trans isomerase 1 (PIN1) gene -842(G , C) and -667(T , C) polymorphic variants in relation to ...
This gene encodes a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans ...
AP71477 Recombinant human Peptidyl-prolyl cis-trans isomerase-like 4 11055 6930 4125 2508 1452 0 1012 E.coli HUMAN His-SUMO-tag ... AP71533 Recombinant human Peptidyl-prolyl cis-trans isomerase FKBP14 11055 6930 4125 2508 1452 0 1012 E.coli HUMAN His-SUMO-tag ... AP71102 Recombinant Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) FKBP-type peptidyl-prolyl cis-trans isomerase ... AP71216 Recombinant Aeromonas hydrophila FKBP-type peptidyl-prolyl cis-trans isomerase FkpA? 16280 10230 7678 4664 2706 0 1903 ...
A family of peptidyl-prolyl cis-trans isomerases that bind to CYCLOSPORINS and regulate the IMMUNE SYSTEM. EC 5.2.1.-. ...
Similar to Peptidyl-prolyl cis-trans isomerase 1 (EC 5.2.1.8) (Rotamase Pin1) (PPIase Pin1) (MdPin1).. LOC_Os04g02830. ...
... cis-trans isomerase activity;0.000170637445429301!GO:0004004;ATP-dependent RNA helicase activity;0.000173844930796994!GO: ... peptidyl-prolyl cis-trans isomerase activity;0.000187481562655478!GO:0045941;positive regulation of transcription; ... isomerase activity;1.25753060146472e-05!GO:0000139;Golgi membrane;1.39985588889505e-05!GO:0006950;response to stress; ... protein disulfide isomerase activity;0.0466005939079284!GO:0016864;intramolecular oxidoreductase activity, transposing S-S ...
Synonyms: PPIE, CYP-33, CYP33, peptidylprolyl isomerase E, peptidyl-prolyl cis-trans isomerase E, PPIase E, cyclophilin-33, ...
Pin1: une peptidyl-prolyl cis/trans isomérase aux rôles insoupçonnés Sébastien B. Lavoie, Alexandra L. Albert and Michel ... Peptidyl-prolyl isomerases (PPIases) are chaperone enzymes which alter the peptide bond between a given amino acid and a ... Pin1 est une peptidyl-prolyl isomérase (PPIase) catalysant lisomérisation cis/trans de certains liens peptidiques précédant ... changing it from the cis to the trans conformation and vice versa. This modification can cause dramatic structural ...
Peptidyl-Prolyl Cis-Trans Isomerase NIMA-Interacting 4. *POU Domain Factors. *Proto-Oncogene Proteins c-bcl-6 ...
  • Macrophage infectivity potentiator (Mip) proteins catalyse the folding of proline -containing proteins through their peptidyl prolyl cis-trans isomerase ( PPIase ) activity and have been shown to play an important role in the virulence of several pathogenic bacteria . (bvsalud.org)
  • FKB1_XENLA FK506-binding protein 1A (Peptidyl-prolyl cis-trans isomerase) (PPiase) (Rotamase) (1. (cornell.edu)
  • FKB1_DROME 12 kDa FK506-binding protein (FKBP) (Peptidyl-prolyl cis-trans isomerase) (PPiase) (M. (cornell.edu)
  • 17. Introduction to Peptidyl-Prolyl cis/trans Isomerase (PPIase) Series. (nih.gov)
  • 16. Peptidyl-Proline Isomerases (PPIases): Targets for Natural Products and Natural Product-Inspired Compounds. (nih.gov)
  • 19. Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets. (nih.gov)
  • Peptidyl-prolyl cis/trans isomerases (PPIases) are evolutionarily conserved enzymes that catalyze cis/trans isomerization of peptidyl-prolyl peptide bonds. (nih.gov)
  • From NCBI Gene: FKBP11 belongs to the FKBP family of peptidyl-prolyl cis/trans isomerases, which catalyze the folding of proline-containing polypeptides. (nih.gov)
  • The peptidyl-prolyl isomerase activity of FKBP proteins is inhibited by the immunosuppressant compounds FK506 and rapamycin (Rulten et al. (nih.gov)
  • 3. Roles of peptidyl-prolyl isomerase Pin1 in disease pathogenesis. (nih.gov)
  • 20. [Unexpected roles of the peptidyl-prolyl cis/trans isomerase Pin1]. (nih.gov)
  • 7. Prolyl isomerase Pin1 promotes extracellular matrix production in hepatic stellate cells through regulating formation of the Smad3-TAZ complex. (nih.gov)
  • 16. The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production. (nih.gov)
  • Glutathione S-transferases act as isomerases in isomerization of 13-cis-retinoic acid to all-trans-retinoic acid in vitro. (nih.gov)
  • Rates of cis-trans isomerization were determined quantitatively by HPLC. (nih.gov)
  • The same heat treatment did not significantly inhibit isomerization catalysed by GSH and apoferritin, indicating that the observed decrease in isomerase activity by heat inactivation was not primarily due to oxidation of protein thiol groups in the GSTs. (nih.gov)
  • It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. (nih.gov)
  • Dr. Redmond and his colleagues demonstrated the essential role of RPE65 in vision, that mutations in the human RPE65 gene cause Leber congenital amaurosis (LCA), that RPE65 is necessary for the all-trans to 11-cis isomerization of vitamin A in the retina, and that RPE65 is the crucial retinol isomerase enzyme of the vitamin A visual cycle. (nih.gov)
  • 1. The Role of Peptidyl Prolyl Isomerases in Aging and Vascular Diseases. (nih.gov)
  • 2. Peptidyl-prolyl isomerases: functionality and potential therapeutic targets in cardiovascular disease. (nih.gov)
  • 4. Peptidyl-prolyl isomerases: a full cast of critical actors in cardiovascular diseases. (nih.gov)
  • 11. Prolyl isomerases in a minimal cell. (nih.gov)
  • 14. The Multiple Roles of Peptidyl Prolyl Isomerases in Brain Cancer. (nih.gov)
  • Macrophage infectivity potentiator protein, a peptidyl prolyl cis-trans isomerase, essential for Coxiella burnetii growth and pathogenesis. (bvsalud.org)
  • 13. Pharmacological targeting of catalyzed protein folding: the example of peptide bond cis/trans isomerases. (nih.gov)
  • This encoded protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin. (nih.gov)
  • 15. Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases. (nih.gov)
  • RPE65 retinol isomerase is an indispensable player in the visual cycle between the vertebrate retina and RPE. (nih.gov)
  • All 4 sequences were identical and shared 99% similarity with the F. tularensis peptidyl-propyl cis - trans isomerase gene (GenBank accession no. (cdc.gov)
  • 27 May 2009 determined by the fraction of cis X-Pro peptide bonds in this region. (nih.gov)
  • DEB025 binds to CypA, a peptidyl-prolyl cis-trans isomerase which is a crucial cofactor for HCV replication. (unl.pt)
  • 10. Functional analysis of the Hsp90-associated human peptidyl prolyl cis/trans isomerases FKBP51, FKBP52 and Cyp40. (nih.gov)
  • RPE65 is a carotenoid oxygenase that has specifically evolved into an enzyme that is capable of hydrolyzing and isomerizing all-trans retinyl ester into 11-cis retinol but that is specialized to the extreme. (nih.gov)
  • FK506 binding / peptidyl-prolyl cis-trans isomerase [Arabidopsis thaliana] >gi7391936. (cornell.edu)
  • It is a complex consisting of a molecule of ROD OPSIN and a molecule of 11-cis retinal (RETINALDEHYDE). (lookformedical.com)
  • The RPE-specific mechanism of major interest to us is the visual cycle, the cyclical process by which vitamin A (all-trans retinol) is converted to the form (11-cis retinal) required for vision. (nih.gov)
  • In the process of light absorption by retinal photoreceptors, the 11-cis retinal chromophore bound to visual pigment is photo-isomerized to the all-trans isomer. (nih.gov)
  • This in turn is oxidized to 11-cis retinal and then secreted to the photoreceptors to regenerate the visual pigment. (nih.gov)
  • 12. Wheat FKBP73 functions in vitro as a molecular chaperone independently of its peptidyl prolyl cis-trans isomerase activity. (nih.gov)
  • 23- and 340-fold those of GSH and apoferritin respectively when comparisons were made on the basis of free thiol concentrations, indicating that free thiol in GSTs cannot account for the majority of observed isomerase activities and suggesting that specific conformations of GSTs are important for such activities. (nih.gov)
  • The unique chemical properties of Pro allow for the adoption of two distinct amide bond conformations (cis and trans). (nih.gov)
  • A family of peptidyl-prolyl cis-trans isomerases that bind to CYCLOSPORINS and regulate the IMMUNE SYSTEM. (illumina.com)
  • It is assumed that all members are peptidyl-prolyl cis-trans isomerases with the enzymatic function attributed to the FKBP domain. (nih.gov)
  • 17. Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts. (nih.gov)
  • From NCBI Gene: FKBP11 belongs to the FKBP family of peptidyl-prolyl cis/trans isomerases, which catalyze the folding of proline-containing polypeptides. (nih.gov)
  • Peptidyl-prolyl cis/trans isomerases (PPIases) are evolutionarily conserved enzymes that catalyze cis/trans isomerization of peptidyl-prolyl peptide bonds. (nih.gov)
  • Members of a family of highly conserved proteins which are all cis-trans peptidyl-prolyl isomerases ( PEPTIDYLPROLYL ISOMERASE ). (bvsalud.org)
  • 12. Proline isomerases at the crossroads of protein folding, signal transduction, and immunosuppression. (nih.gov)
  • Incubation with guanidine (7-8 M) or heat-inactivation of GSTs (100 degrees C for 3 min) decreased isomerase activities by approx. (nih.gov)
  • 6. NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein. (nih.gov)

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