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Showing 1 to 11 of 11 entries
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Pseudomonas aeruginosa porphobilinogen synthase assembly state regulators: hit discovery and initial SAR studies.

ARKIVOC : free online journal of organic chemistry

Reitz AB, Ramirez UD, Stith L, Du Y, Smith GR, Jaffe EK.
PMID: 21643541
ARKIVOC. 2010 Jun;2010:175-188.

Porphobilinogen synthase (PBGS) catalyzes the first common step in the biosynthesis of the essential heme, chlorophyll and vitamin B(12) heme pigments. PBGS activity is regulated by assembly state, with certain oligomers exhibiting biological activity and others either partially or...

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Reitz AB, Ramirez UD, Stith L, et al. Pseudomonas aeruginosa porphobilinogen synthase assembly state regulators: hit discovery and initial SAR studies. ARKIVOC. 2010;2010:175-188
Reitz, A. B., Ramirez, U. D., Stith, L., Du, Y., Smith, G. R., & Jaffe, E. K. (2010). Pseudomonas aeruginosa porphobilinogen synthase assembly state regulators: hit discovery and initial SAR studies. ARKIVOC : free online journal of organic chemistry, 2010175-188.
Reitz, Allen B, et al. "Pseudomonas aeruginosa porphobilinogen synthase assembly state regulators: hit discovery and initial SAR studies." ARKIVOC : free online journal of organic chemistry vol. 2010 (2010): 175-188.
Reitz AB, Ramirez UD, Stith L, Du Y, Smith GR, Jaffe EK. Pseudomonas aeruginosa porphobilinogen synthase assembly state regulators: hit discovery and initial SAR studies. ARKIVOC. 2010 Jun;2010:175-188. PMID: 21643541; PMCID: PMC3106444.
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The Se.

Computational toxicology (Amsterdam, Netherlands)

Nogara PA, Orian L, Rocha JBT.
PMID: 32572387
Comput Toxicol. 2020 Aug;15:100127. doi: 10.1016/j.comtox.2020.100127. Epub 2020 Jun 09.

Organoselenium compounds present many pharmacological properties and are promising drugs. However, toxicological effects associated with inhibition of thiol-containing enzymes, such as the δ-aminolevulinic acid dehydratase (δ-AlaD), have been described. The molecular mechanism(s) by which they inhibit thiol-containing enzymes at...

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Nogara PA, Orian L, Rocha JBT. The Se. Comput Toxicol. 2020;15:100127doi: 10.1016/j.comtox.2020.100127.
Nogara, P. A., Orian, L., & Rocha, J. B. T. (2020). The Se. Computational toxicology (Amsterdam, Netherlands), 15100127. https://doi.org/10.1016/j.comtox.2020.100127
Nogara, Pablo Andrei, et al. "The Se." Computational toxicology (Amsterdam, Netherlands) vol. 15 (2020): 100127. doi: https://doi.org/10.1016/j.comtox.2020.100127
Nogara PA, Orian L, Rocha JBT. The Se. Comput Toxicol. 2020 Aug;15:100127. doi: 10.1016/j.comtox.2020.100127. Epub 2020 Jun 09. PMID: 32572387; PMCID: PMC7280828.
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Revealing the promoting effect of betaine on vitamin B12 biosynthetic pathway of Pseudomonas denitrificans by using a proteomics analysis.

Current pharmaceutical biotechnology

Li KT, Yang Y, Cheng X.
PMID: 34061014
Curr Pharm Biotechnol. 2021 May 31; doi: 10.2174/1389201022666210531120935. Epub 2021 May 31.

BACKGROUND: Our previous comparative metabolomics research revealed that betaine (N,N,N-trimethylglycine, a typically essential methyl-group donor for vitamin B12 biosynthesis) had a powerful promoting effect on the generation of vitamin B12 precursors and intermediates in vitamin B12-producing Pseudomonas denitrificans. However,...

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Li KT, Yang Y, Cheng X. Revealing the promoting effect of betaine on vitamin B12 biosynthetic pathway of Pseudomonas denitrificans by using a proteomics analysis. Curr Pharm Biotechnol. 2021;doi: 10.2174/1389201022666210531120935.
Li, K. T., Yang, Y., & Cheng, X. (2021). Revealing the promoting effect of betaine on vitamin B12 biosynthetic pathway of Pseudomonas denitrificans by using a proteomics analysis. Current pharmaceutical biotechnology, . https://doi.org/10.2174/1389201022666210531120935
Li, Kun-Tai, et al. "Revealing the promoting effect of betaine on vitamin B12 biosynthetic pathway of Pseudomonas denitrificans by using a proteomics analysis." Current pharmaceutical biotechnology vol. (2021). doi: https://doi.org/10.2174/1389201022666210531120935
Li KT, Yang Y, Cheng X. Revealing the promoting effect of betaine on vitamin B12 biosynthetic pathway of Pseudomonas denitrificans by using a proteomics analysis. Curr Pharm Biotechnol. 2021 May 31; doi: 10.2174/1389201022666210531120935. Epub 2021 May 31. PMID: 34061014.
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Crystallization and preliminary X-ray diffraction studies of 5-chlorolevulinate-modified bovine porphobilinogen synthase and the Pb(II)-complexed enzyme.

Acta crystallographica. Section D, Biological crystallography

Carrell HL, Glusker JP, Shimoni L, Keefe LJ, Afshar C, Volin M, Jaffe EK.
PMID: 15299718
Acta Crystallogr D Biol Crystallogr. 1996 Mar 01;52:419-21. doi: 10.1107/S0907444995013163.

Bovine porphobilinogen synthase (PBGS) is an homo-octameric enzyme with four active sites. Each active site binds two Zn(II) atoms whose ligands differ and two molecules of 5-aminolevulinate whose chemical fates differ. The asymmetric binding of two Zn(II) atoms and...

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Carrell HL, Glusker JP, Shimoni L, et al. Crystallization and preliminary X-ray diffraction studies of 5-chlorolevulinate-modified bovine porphobilinogen synthase and the Pb(II)-complexed enzyme. Acta Crystallogr D Biol Crystallogr. 1996;52:419-21doi: 10.1107/S0907444995013163.
Carrell, H. L., Glusker, J. P., Shimoni, L., Keefe, L. J., Afshar, C., Volin, M., & Jaffe, E. K. (1996). Crystallization and preliminary X-ray diffraction studies of 5-chlorolevulinate-modified bovine porphobilinogen synthase and the Pb(II)-complexed enzyme. Acta crystallographica. Section D, Biological crystallography, 52419-21. https://doi.org/10.1107/S0907444995013163
Carrell, H L, et al. "Crystallization and preliminary X-ray diffraction studies of 5-chlorolevulinate-modified bovine porphobilinogen synthase and the Pb(II)-complexed enzyme." Acta crystallographica. Section D, Biological crystallography vol. 52 (1996): 419-21. doi: https://doi.org/10.1107/S0907444995013163
Carrell HL, Glusker JP, Shimoni L, Keefe LJ, Afshar C, Volin M, Jaffe EK. Crystallization and preliminary X-ray diffraction studies of 5-chlorolevulinate-modified bovine porphobilinogen synthase and the Pb(II)-complexed enzyme. Acta Crystallogr D Biol Crystallogr. 1996 Mar 01;52:419-21. doi: 10.1107/S0907444995013163. PMID: 15299718.
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MORPHEEINS - A NEW PATHWAY FOR ALLOSTERIC DRUG DISCOVERY.

The open conference proceedings journal

Jaffe EK.
PMID: 21643557
Open Conf Proc J. 2010;1:1-6. doi: 10.2174/2210289201001010001.

The morpheein model of allosteric regulation can be applied as a novel approach to the discovery of small molecule allosteric modulators of protein function. Morpheeins are homo-oligomeric proteins where, under physiological conditions, the oligomer can dissociate, the dissociated units...

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Jaffe EK. MORPHEEINS - A NEW PATHWAY FOR ALLOSTERIC DRUG DISCOVERY. Open Conf Proc J. 2010;1:1-6doi: 10.2174/2210289201001010001.
Jaffe, E. K. (2010). MORPHEEINS - A NEW PATHWAY FOR ALLOSTERIC DRUG DISCOVERY. The open conference proceedings journal, 11-6. https://doi.org/10.2174/2210289201001010001
Jaffe, Eileen K. "MORPHEEINS - A NEW PATHWAY FOR ALLOSTERIC DRUG DISCOVERY." The open conference proceedings journal vol. 1 (2010): 1-6. doi: https://doi.org/10.2174/2210289201001010001
Jaffe EK. MORPHEEINS - A NEW PATHWAY FOR ALLOSTERIC DRUG DISCOVERY. Open Conf Proc J. 2010;1:1-6. doi: 10.2174/2210289201001010001. PMID: 21643557; PMCID: PMC3107518.
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In silico designing and molecular docking of a potent analog against Staphylococcus aureus porphobilinogen synthase.

Journal of pharmacy & bioallied sciences

Kumar PS, Kumar YN, Prasad UV, Yeswanth S, Swarupa V, Sowjenya G, Venkatesh K, Srikanth L, Rao VK, Sarma PV.
PMID: 25035635
J Pharm Bioallied Sci. 2014 Jul;6(3):158-66. doi: 10.4103/0975-7406.135246.

BACKGROUND: The emergence of multidrug-resistant strains of Staphylococcus aureus, there is an urgent need for the development of new antimicrobials which are narrow and pathogen specific.AIM: In this context, the present study is aimed to have a control on...

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Kumar PS, Kumar YN, Prasad UV, et al. In silico designing and molecular docking of a potent analog against Staphylococcus aureus porphobilinogen synthase. J Pharm Bioallied Sci. 2014;6(3):158-66doi: 10.4103/0975-7406.135246.
Kumar, P. S., Kumar, Y. N., Prasad, U. V., Yeswanth, S., Swarupa, V., Sowjenya, G., Venkatesh, K., Srikanth, L., Rao, V. K., & Sarma, P. V. (2014). In silico designing and molecular docking of a potent analog against Staphylococcus aureus porphobilinogen synthase. Journal of pharmacy & bioallied sciences, 6(3), 158-66. https://doi.org/10.4103/0975-7406.135246
Kumar, Pasupuleti Santhosh, et al. "In silico designing and molecular docking of a potent analog against Staphylococcus aureus porphobilinogen synthase." Journal of pharmacy & bioallied sciences vol. 6,3 (2014): 158-66. doi: https://doi.org/10.4103/0975-7406.135246
Kumar PS, Kumar YN, Prasad UV, Yeswanth S, Swarupa V, Sowjenya G, Venkatesh K, Srikanth L, Rao VK, Sarma PV. In silico designing and molecular docking of a potent analog against Staphylococcus aureus porphobilinogen synthase. J Pharm Bioallied Sci. 2014 Jul;6(3):158-66. doi: 10.4103/0975-7406.135246. PMID: 25035635; PMCID: PMC4097929.
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Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis.

Acta crystallographica. Section D, Structural biology

Mills-Davies N, Butler D, Norton E, Thompson D, Sarwar M, Guo J, Gill R, Azim N, Coker A, Wood SP, Erskine PT, Coates L, Cooper JB, Rashid N, Akhtar M, Shoolingin-Jordan PM.
PMID: 28045381
Acta Crystallogr D Struct Biol. 2017 Jan 01;73:9-21. doi: 10.1107/S2059798316019525. Epub 2017 Jan 01.

A number of X-ray analyses of an enzyme involved in a key early stage of tetrapyrrole biosynthesis are reported. Two structures of human 5-aminolaevulinate dehydratase (ALAD), native and recombinant, have been determined at 2.8 Å resolution, showing that the...

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Mills-Davies N, Butler D, Norton E, et al. Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis. Acta Crystallogr D Struct Biol. 2017;73:9-21doi: 10.1107/S2059798316019525.
Mills-Davies, N., Butler, D., Norton, E., Thompson, D., Sarwar, M., Guo, J., Gill, R., Azim, N., Coker, A., Wood, S. P., Erskine, P. T., Coates, L., Cooper, J. B., Rashid, N., Akhtar, M., & Shoolingin-Jordan, P. M. (2017). Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis. Acta crystallographica. Section D, Structural biology, 739-21. https://doi.org/10.1107/S2059798316019525
Mills-Davies, N, et al. "Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis." Acta crystallographica. Section D, Structural biology vol. 73 (2017): 9-21. doi: https://doi.org/10.1107/S2059798316019525
Mills-Davies N, Butler D, Norton E, Thompson D, Sarwar M, Guo J, Gill R, Azim N, Coker A, Wood SP, Erskine PT, Coates L, Cooper JB, Rashid N, Akhtar M, Shoolingin-Jordan PM. Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis. Acta Crystallogr D Struct Biol. 2017 Jan 01;73:9-21. doi: 10.1107/S2059798316019525. Epub 2017 Jan 01. PMID: 28045381.
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Environmental contaminants perturb fragile protein assemblies and inhibit normal protein function.

Current chemical biology

Lawrence SH, Selwood T, Jaffe EK.
PMID: 25045409
Curr Chem Biol. 2013;7(2):196-206. doi: 10.2174/2212796811307020011.

The molecular mechanisms whereby small molecules that contaminate our environment cause physiological effects are largely unknown, in terms of both targets and mechanisms. The essential human enzyme porphobilinogen synthase (

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Lawrence SH, Selwood T, Jaffe EK. Environmental contaminants perturb fragile protein assemblies and inhibit normal protein function. Curr Chem Biol. 2013;7(2):196-206doi: 10.2174/2212796811307020011.
Lawrence, S. H., Selwood, T., & Jaffe, E. K. (2013). Environmental contaminants perturb fragile protein assemblies and inhibit normal protein function. Current chemical biology, 7(2), 196-206. https://doi.org/10.2174/2212796811307020011
Lawrence, Sarah H, et al. "Environmental contaminants perturb fragile protein assemblies and inhibit normal protein function." Current chemical biology vol. 7,2 (2013): 196-206. doi: https://doi.org/10.2174/2212796811307020011
Lawrence SH, Selwood T, Jaffe EK. Environmental contaminants perturb fragile protein assemblies and inhibit normal protein function. Curr Chem Biol. 2013;7(2):196-206. doi: 10.2174/2212796811307020011. PMID: 25045409; PMCID: PMC4102012.
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Expanding the Concepts in Protein Structure-Function Relationships and Enzyme Kinetics: Teaching using Morpheeins.

Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology

Lawrence SH, Jaffe EK.
PMID: 19578473
Biochem Mol Biol Educ. 2008;36(4):274-283. doi: 10.1002/bmb.20211.

A morpheein is a homo-oligomeric protein that can exist as an ensemble of physiologically significant and functionally different alternate quaternary assemblies. Morpheeins exist in nature and utilize conformational equilibria between different tertiary structures to form distinct oligomers as a...

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Lawrence SH, Jaffe EK. Expanding the Concepts in Protein Structure-Function Relationships and Enzyme Kinetics: Teaching using Morpheeins. Biochem Mol Biol Educ. 2008;36(4):274-283doi: 10.1002/bmb.20211.
Lawrence, S. H., & Jaffe, E. K. (2008). Expanding the Concepts in Protein Structure-Function Relationships and Enzyme Kinetics: Teaching using Morpheeins. Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology, 36(4), 274-283. https://doi.org/10.1002/bmb.20211
Lawrence, Sarah H, and Jaffe, Eileen K. "Expanding the Concepts in Protein Structure-Function Relationships and Enzyme Kinetics: Teaching using Morpheeins." Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology vol. 36,4 (2008): 274-283. doi: https://doi.org/10.1002/bmb.20211
Lawrence SH, Jaffe EK. Expanding the Concepts in Protein Structure-Function Relationships and Enzyme Kinetics: Teaching using Morpheeins. Biochem Mol Biol Educ. 2008;36(4):274-283. doi: 10.1002/bmb.20211. PMID: 19578473; PMCID: PMC2575429.
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Revealing the promoting effect of betaine on vitamin B12 biosynthetic pathway of Pseudomonas denitrificans by using a proteomics analysis.

Current pharmaceutical biotechnology

Li KT, Yang Y, Cheng X.
PMID: 34061014
Curr Pharm Biotechnol. 2021 May 31; doi: 10.2174/1389201022666210531120935. Epub 2021 May 31.

BACKGROUND: Our previous comparative metabolomics research revealed that betaine (N,N,N-trimethylglycine, a typically essential methyl-group donor for vitamin B12 biosynthesis) had a powerful promoting effect on the generation of vitamin B12 precursors and intermediates in vitamin B12-producing Pseudomonas denitrificans. However,...

Cite
Li KT, Yang Y, Cheng X. Revealing the promoting effect of betaine on vitamin B12 biosynthetic pathway of Pseudomonas denitrificans by using a proteomics analysis. Curr Pharm Biotechnol. 2021;doi: 10.2174/1389201022666210531120935.
Li, K. T., Yang, Y., & Cheng, X. (2021). Revealing the promoting effect of betaine on vitamin B12 biosynthetic pathway of Pseudomonas denitrificans by using a proteomics analysis. Current pharmaceutical biotechnology, . https://doi.org/10.2174/1389201022666210531120935
Li, Kun-Tai, et al. "Revealing the promoting effect of betaine on vitamin B12 biosynthetic pathway of Pseudomonas denitrificans by using a proteomics analysis." Current pharmaceutical biotechnology vol. (2021). doi: https://doi.org/10.2174/1389201022666210531120935
Li KT, Yang Y, Cheng X. Revealing the promoting effect of betaine on vitamin B12 biosynthetic pathway of Pseudomonas denitrificans by using a proteomics analysis. Curr Pharm Biotechnol. 2021 May 31; doi: 10.2174/1389201022666210531120935. Epub 2021 May 31. PMID: 34061014.
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[No title available]

Microbiology (Reading, England)

Scott AF, Deery E, Lawrence AD, Warren MJ.
PMID: 34661520
Microbiology (Reading). 2021 Oct;167(10). doi: 10.1099/mic.0.001095.

Uroporphyrinogen III, the universal progenitor of macrocyclic, modified tetrapyrroles, is produced from aminolaevulinic acid (ALA) by a conserved pathway involving three enzymes: porphobilinogen synthase (PBGS), hydroxymethylbilane synthase (HmbS) and uroporphyrinogen III synthase (UroS). The gene encoding uroporphyrinogen III synthase...

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Scott AF, Deery E, Lawrence AD, et al. . Microbiology (Reading). 2021;167(10)doi: 10.1099/mic.0.001095.
Scott, A. F., Deery, E., Lawrence, A. D., & Warren, M. J. (2021). . Microbiology (Reading, England), 167(10), . https://doi.org/10.1099/mic.0.001095
Scott, Alan F, et al. "." Microbiology (Reading, England) vol. 167,10 (2021). doi: https://doi.org/10.1099/mic.0.001095
Scott AF, Deery E, Lawrence AD, Warren MJ. . Microbiology (Reading). 2021 Oct;167(10). doi: 10.1099/mic.0.001095. PMID: 34661520.
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Showing 1 to 11 of 11 entries