Substrates: the reaction is completely bi-directional. The specific activity with cis-4-hydroxy-D-proline is 160% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. The catalytic efficiency (kcat/Km) values for L-proline and trans-4-hydroxy-D-proline are similar, whereas a preference for D-proline over cis-4-hydroxy-D-proline (45fold) is identified and is caused by a 75fold lower Km for D-proline. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site Products: -
Substrates: the reaction is completely bi-directional. The specific activity with trans-4-hydroxy-D-proline is 97% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site Products: -
Substrates: a mutant lacking the 4-hydroxyproline epimerase, the first enzyme of the pathway, is still equally active as an inducer of the remaining three enzymes, suggesting that each epimer has intrinsic inducer activity Products: -
Substrates: the reaction is completely bi-directional. The specific activity with trans-4-hydroxy-D-proline is 97% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site Products: -
Substrates: the reaction is completely bi-directional. The specific activity with trans-4-hydroxy-D-proline is 97% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site Products: -
Substrates: kcat/Km value for trans-4-hydroxy-L-proline is about 3fold lower than that for L-proline, which is attributed to a 17fold lower kcat value. The kinetic parameters of the epimerization of cis-4-hydroxy-D-proline can not be determined Products: -
Substrates: the reaction is completely bi-directional. The specific activity with cis-4-hydroxy-D-proline is 160% compared to the L-enantiomer. The bifunctional enzyme reversibly catalyzes the racemization of proline and the epimerization of 4-hydroxyproline and 3-hydroxyproline with similar kinetic constants. The catalytic efficiency (kcat/Km) values for L-proline and trans-4-hydroxy-D-proline are similar, whereas a preference for D-proline over cis-4-hydroxy-D-proline (45fold) is identified and is caused by a 75fold lower Km for D-proline. Catalysis is based on the same 1,1-proton transfer mechanism using two general acidic/basic cysteine residues located on opposite faces of the active site Products: -
Substrates: a mutant lacking the 4-hydroxyproline epimerase, the first enzyme of the pathway, is still equally active as an inducer of the remaining three enzymes, suggesting that each epimer has intrinsic inducer activity Products: -
a hypRE mutant grows with cis-4-hydroxy-D-proline but not with trans-4-hydroxy-L-proline, and it exhibits wild-type growth on succinate and proline, mutant complementation with the native smb20268 gene
the enzyme performs the first step of hydroxyproline catabolism, regulation, hyp cluster promoters are regulated by HypR, overview. cis-4-Hydroxy-D-proline is the effector that interacts with HypR and the results suggest a role of positive feedback in the regulation of hyp catabolism, as cis-4-hydroxy-D-proline (or a downstream catabolite) is a stronger inducer than the initial substrate trans-4-hydroxy-L-proline
the enzyme 4-hydroxyproline 2-epimerase reversibly catalyse the interconversion of trans-4-hydroxy-L-proline and cis-4-hydroxy-D-proline. The Brucella proline racemase (PrpA) or hydroxyproline epimerase (BaHyPRE) also exhibit B-cell mitogenic properties thereby causing B-lymphocytes polyclonal activation and increase secretion of interleukin (IL)-10. Importance of PrpA in brucellosis
the enzyme 4-hydroxyproline 2-epimerase reversibly catalyse the interconversion of trans-4-hydroxy-L-proline and cis-4-hydroxy-D-proline. The Brucella proline racemase (PrpA) or hydroxyproline epimerase (BaHyPRE) also exhibit B-cell mitogenic properties thereby causing B-lymphocytes polyclonal activation and increase secretion of interleukin (IL)-10. Importance of PrpA in brucellosis
almost complete loss of epimerization of trans-4-hydroxy-L-Pro, some residual activity on trans-4-hydroxy-D-Pro. V60 residue accounts for OH-Pro ligand specificity
shows 5.3fold, 430fold, and 5.8fold lower kcat/Km values for trans-4-hydroxy-L-proline, trans-3-hydroxy-L-proline, and cis-4-hydroxy-D-proline respectively, mainly due to a marked decrease in kcat values, whereas no significant effects were found in the kinetic constants of proline, suggesting that this (hydrophobic and bulky) tryptophan residue plays an importance role in the recognition of hydroxyproline (more hydrophilic and bulky than proline)
shows 5.3fold, 430fold, and 5.8fold lower kcat/Km values for trans-4-hydroxy-L-proline, trans-3-hydroxy-L-proline, and cis-4-hydroxy-D-proline respectively, mainly due to a marked decrease in kcat values, whereas no significant effects were found in the kinetic constants of proline, suggesting that this (hydrophobic and bulky) tryptophan residue plays an importance role in the recognition of hydroxyproline (more hydrophilic and bulky than proline)
gene hypRE, encoded in the Hyp catabolism locus, DNA and amino acid sequence determination and analysis, expression of the C-terminally His-tagged enzyme in Escherichia coli strain BL21/DE3/pET28 from the T7 promoter
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
live attenuated Salmonella typhimurium (ST) vector constitutively expressing heterologous Brucella abortus S19 PrpA protein (ST-PrpA) is inoculated in BALB/c mice. No aggravation of morbidity is observed upon mice inoculation of ST-PrpA. Immunized mice show significantly quicker anti-Salmonella IgG responses as compared to ST only immunization, and an increase interleukin-4 production evident in in vitro pulsed mice splenocytes, splenocytes proliferative profiles and lymphocyte population evaluation, overview
live attenuated Salmonella typhimurium (ST) vector constitutively expressing heterologous Brucella abortus S19 PrpA protein (ST-PrpA) is inoculated in BALB/c mice. No aggravation of morbidity is observed upon mice inoculation of ST-PrpA. Immunized mice show significantly quicker anti-Salmonella IgG responses as compared to ST only immunization, and an increase interleukin-4 production evident in in vitro pulsed mice splenocytes, splenocytes proliferative profiles and lymphocyte population evaluation, overview
live attenuated Salmonella typhimurium (ST) vector constitutively expressing heterologous Brucella abortus S19 PrpA protein (ST-PrpA) is inoculated in BALB/c mice. No aggravation of morbidity is observed upon mice inoculation of ST-PrpA. Immunized mice show significantly quicker anti-Salmonella IgG responses as compared to ST only immunization, and an increase interleukin-4 production evident in in vitro pulsed mice splenocytes, splenocytes proliferative profiles and lymphocyte population evaluation, overview
spectrophotometric assay for hydroxyproline in collagenous tissue hydrolysates, with an enzymatic method using 4-hydroxyproline 2-epimerase,EC 5.1.1.8, D-amino acid oxidase, EC 1.4.3.3, and a colorimetric reagent of the mixture of Ti(IV) and 4-(2-pyridylazo)-resorcinol
estimation of the content of L-hydroxyprolines using coupling systems with metabolic enzymes of the trans-4-hydroxy-L-proline pathway (hydroxyproline 2-epimerase (HypE) and cis-4-hydroxy-D-proline dehydrogenase (HypDH)) and the trans-3-hydroxy-L-proline pathway (trans-3-hydroxy-L-proline dehydratase (T3LHypD) and DELTA1-pyrroline-2-carboxylate reductase (Pyr2CR)) from microorganisms. A functional expression system of recombinant HypDH with a heterooligomeric structure is constructed in Escherichia coli cells. Enzymological characterization reveals that the beta-subunit acts as a catalytic subunit, and also that assembly with other subunit(s) improves the kinetics for cis-4-hydroxy-D-proline and thermostability. By using a spectrophotometric assay with different wavelengths, the contents of trans-4-hydroxy-L-proline and trans-3-hydroxy-L-proline are successfully estimated within the ranges of 0.004-1 mM and 0.05-1 mM, respectively, and are consistent with the contents determined by HPLC. This enzymatic method is used to measure the content of trans-4-hydroxy-L-proline in the acid-hydrolysate of collagen, and blood plasma
PrpA can be used as a protein adjuvant in a live Salmonella delivery system, in order to increase humoral responses effectively without major interference on the cell mediated immunity
PrpA can be used as a protein adjuvant in a live Salmonella delivery system, in order to increase humoral responses effectively without major interference on the cell mediated immunity
PrpA can be used as a protein adjuvant in a live Salmonella delivery system, in order to increase humoral responses effectively without major interference on the cell mediated immunity
PrpA can be used as a protein adjuvant in a live Salmonella delivery system, in order to increase humoral responses effectively without major interference on the cell mediated immunity
Gavina, J.M.; White, C.E.; Finan, T.M.; Britz-McKibbin, P.
Determination of 4-hydroxyproline-2-epimerase activity by capillary electrophoresis: A stereoselective platform for inhibitor screening of amino acid isomerases
Watanabe, S.; Tanimoto, Y.; Nishiwaki, H.; Watanabe, Y.
Identification and characterization of bifunctional proline racemase/hydroxyproline epimerase from archaea: discrimination of substrates and molecular evolution