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Article ; Online: Repurposing of rabeprazole as an anti-

García-Torres, Itzhel / De la Mora-De la Mora, Ignacio / López-Velázquez, Gabriel / Cabrera, Nallely / Flores-López, Luis Antonio / Becker, Ingeborg / Herrera-López, Juliana / Hernández, Roberto / Pérez-Montfort, Ruy / Enríquez-Flores, Sergio

Journal of enzyme inhibition and medicinal chemistry

2023 Volume 38, Issue 1, Page(s) 2231169

Abstract: Trypanosoma ... ...

Abstract	Trypanosoma cruzi
MeSH term(s)	Humans ; Trypanosoma cruzi ; Triose-Phosphate Isomerase/chemistry ; Triose-Phosphate Isomerase/pharmacology ; Rabeprazole/pharmacology ; Rabeprazole/therapeutic use ; Drug Repositioning ; Chagas Disease/drug therapy ; Trypanocidal Agents/pharmacology
Chemical Substances	benzonidazole (YC42NRJ1ZD) ; Triose-Phosphate Isomerase (EC 5.3.1.1) ; Rabeprazole (32828355LL) ; Trypanocidal Agents
Language	English
Publishing date	2023-07-03
Publishing country	England
Document type	Journal Article
ZDB-ID	2082578-X
ISSN	1475-6374 ; 1475-6366
ISSN (online)	1475-6374
ISSN	1475-6366
DOI	10.1080/14756366.2023.2231169
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Article ; Online: Human Triosephosphate Isomerase Is a Potential Target in Cancer Due to Commonly Occurring Post-Translational Modifications.

Enríquez-Flores, Sergio / De la Mora-De la Mora, Ignacio / García-Torres, Itzhel / Flores-López, Luis A / Martínez-Pérez, Yoalli / López-Velázquez, Gabriel

Molecules (Basel, Switzerland)

2023 Volume 28, Issue 16

Abstract: Cancer involves a series of diseases where cellular growth is not controlled. Cancer is a leading cause of death worldwide, and the burden of cancer incidence and mortality is rapidly growing, mainly in developing countries. Many drugs are currently used, ...

Abstract	Cancer involves a series of diseases where cellular growth is not controlled. Cancer is a leading cause of death worldwide, and the burden of cancer incidence and mortality is rapidly growing, mainly in developing countries. Many drugs are currently used, from chemotherapeutic agents to immunotherapy, among others, along with organ transplantation. Treatments can cause severe side effects, including remission and progression of the disease with serious consequences. Increased glycolytic activity is characteristic of cancer cells. Triosephosphate isomerase is essential for net ATP production in the glycolytic pathway. Notably, some post-translational events have been described that occur in human triosephosphate isomerase in which functional and structural alterations are provoked. This is considered a window of opportunity, given the differences that may exist between cancer cells and their counterpart in normal cells concerning the glycolytic enzymes. Here, we provide elements that bring out the potential of triosephosphate isomerase, under post-translational modifications, to be considered an efficacious target for treating cancer.
MeSH term(s)	Humans ; Triose-Phosphate Isomerase/genetics ; Neoplasms/drug therapy ; Protein Processing, Post-Translational ; Cell Cycle ; Cell Proliferation
Chemical Substances	Triose-Phosphate Isomerase (EC 5.3.1.1)
Language	English
Publishing date	2023-08-21
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	1413402-0
ISSN	1420-3049 ; 1431-5165 ; 1420-3049
ISSN (online)	1420-3049
ISSN	1431-5165 ; 1420-3049
DOI	10.3390/molecules28166163
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Article ; Online: Testing New Peptides From

Xicoténcatl-García, Lizbeth / Enriquez-Flores, Sergio / Correa, Dolores

Frontiers in cellular and infection microbiology

2019 Volume 9, Page(s) 368

Abstract: Toxoplasma ... ...

Abstract	Toxoplasma gondii
MeSH term(s)	Adolescent ; Adult ; Amino Acid Sequence ; Antigens, Protozoan/immunology ; Computational Biology/methods ; Conserved Sequence ; Enzyme-Linked Immunosorbent Assay ; Female ; Humans ; Infant, Newborn ; Infectious Disease Transmission, Vertical ; Male ; Mexico/epidemiology ; Peptides/immunology ; Protein Conformation ; Protozoan Proteins/chemistry ; Protozoan Proteins/immunology ; Risk Assessment ; Serotyping/methods ; Structure-Activity Relationship ; Toxoplasma/classification ; Toxoplasma/immunology ; Toxoplasmosis/diagnosis ; Toxoplasmosis/epidemiology ; Toxoplasmosis/parasitology ; Toxoplasmosis/transmission ; Young Adult
Chemical Substances	Antigens, Protozoan ; Peptides ; Protozoan Proteins
Language	English
Publishing date	2019-10-23
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2619676-1
ISSN	2235-2988 ; 2235-2988
ISSN (online)	2235-2988
ISSN	2235-2988
DOI	10.3389/fcimb.2019.00368
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Article ; Online: The Giardial Arginine Deiminase Participates in

Fernández-Lainez, Cynthia / de la Mora-de la Mora, Ignacio / Enríquez-Flores, Sergio / García-Torres, Itzhel / Flores-López, Luis A / Gutiérrez-Castrellón, Pedro / de Vos, Paul / López-Velázquez, Gabriel

International journal of molecular sciences

2022 Volume 23, Issue 19

Abstract: Beyond the problem in public health that protist-generated diseases represent, understanding the variety of mechanisms used by these parasites to interact with the human immune system is of biological and medical relevance. ...

Abstract	Beyond the problem in public health that protist-generated diseases represent, understanding the variety of mechanisms used by these parasites to interact with the human immune system is of biological and medical relevance.
MeSH term(s)	Animals ; Giardia ; Giardiasis ; Humans ; Hydrolases ; Immunity ; Immunomodulation ; Molecular Docking Simulation ; Toll-Like Receptors
Chemical Substances	Toll-Like Receptors ; Hydrolases (EC 3.-) ; arginine deiminase (EC 3.5.3.6)
Language	English
Publishing date	2022-09-30
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms231911552
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Article ; Online: Improved yield, stability, and cleavage reaction of a novel tobacco etch virus protease mutant.

Enríquez-Flores, Sergio / De la Mora-De la Mora, José Ignacio / Flores-López, Luis Antonio / Cabrera, Nallely / Fernández-Lainez, Cynthia / Hernández-Alcántara, Gloria / Guerrero-Beltrán, Carlos Enrique / López-Velázquez, Gabriel / García-Torres, Itzhel

Applied microbiology and biotechnology

2022 Volume 106, Issue 4, Page(s) 1475–1492

Abstract: The protease catalytic subunit of the nuclear inclusion protein A from tobacco etch virus (TEVp) is widely used to remove tags and fusion proteins from recombinant proteins. Some intrinsic drawbacks to its recombinant production have been studied for ... ...

Abstract	The protease catalytic subunit of the nuclear inclusion protein A from tobacco etch virus (TEVp) is widely used to remove tags and fusion proteins from recombinant proteins. Some intrinsic drawbacks to its recombinant production have been studied for many years, such as low solubility, auto-proteolysis, and instability. Some point mutations have been incorporated in the amino acid protease sequence to improve its production. Here, a comprehensive review of each mutation reported so far has been made to incorporate them into a mutant called TEVp7M with a total of seven changes. This mutant with a His
MeSH term(s)	Chromatography, Affinity ; Endopeptidases/genetics ; Endopeptidases/metabolism ; Proteolysis ; Recombinant Fusion Proteins/metabolism
Chemical Substances	Recombinant Fusion Proteins ; Endopeptidases (EC 3.4.-) ; TEV protease (EC 3.4.-)
Language	English
Publishing date	2022-01-29
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	392453-1
ISSN	1432-0614 ; 0171-1741 ; 0175-7598
ISSN (online)	1432-0614
ISSN	0171-1741 ; 0175-7598
DOI	10.1007/s00253-022-11786-5
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Article: Improved yield, stability, and cleavage reaction of a novel tobacco etch virus protease mutant

Applied microbiology and biotechnology. 2022 Feb., v. 106, no. 4

2022

Abstract	The protease catalytic subunit of the nuclear inclusion protein A from tobacco etch virus (TEVp) is widely used to remove tags and fusion proteins from recombinant proteins. Some intrinsic drawbacks to its recombinant production have been studied for many years, such as low solubility, auto-proteolysis, and instability. Some point mutations have been incorporated in the amino acid protease sequence to improve its production. Here, a comprehensive review of each mutation reported so far has been made to incorporate them into a mutant called TEVp7M with a total of seven changes. This mutant with a His₇tag at N-terminus was produced with remarkable purification yields (55 mg/L of culture) from the soluble fraction in a single step affinity purification. The stability of His₇-TEVp7M was analyzed and compared with the single mutant TEVp S219V, making evident that His₇-TEVp7M shows very constant thermal stability against pH variation, whereas TEVp S219V is highly sensitive to this change. The cleavage reaction was optimized by determining the amount of protease that could cleave a 100-fold excess substrate in the shortest possible time at 30 °C. Under these conditions, His₇-TEVp7M was able to cleave His-tag in the buffers commonly used for affinity purification. Finally, a structural analysis of the mutations showed that four of them increased the polarity of the residues involved and, consequently, showed increased solubility of TEVp and fewer hydrophobic regions exposed to the solvent. Taken together, the seven changes studied in this work improved stability, solubility, and activity of TEVp producing enough protease to digest large amounts of tags or fusion proteins. KEY POINTS: • Production of excellent yields of a TEVp (TEVp7M) by incorporation of seven changes. • His-tag removal in an excess substrate in the common buffers used for purification. • Incorporated mutations improve polarity, stability, and activity of TEVp7M.
Keywords	Tobacco etch virus ; amino acids ; biotechnology ; hydrophobicity ; microbiology ; mutants ; pH ; protein subunits ; proteinases ; solubility ; solvents ; thermal stability
Language	English
Dates of publication	2022-02
Size	p. 1475-1492.
Publishing place	Springer Berlin Heidelberg
Document type	Article
ZDB-ID	392453-1
ISSN	1432-0614 ; 0171-1741 ; 0175-7598
ISSN (online)	1432-0614
ISSN	0171-1741 ; 0175-7598
DOI	10.1007/s00253-022-11786-5
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Article: Differential effects on enzyme stability and kinetic parameters of mutants related to human triosephosphate isomerase deficiency.

Cabrera, Nallely / Torres-Larios, Alfredo / García-Torres, Itzhel / Enríquez-Flores, Sergio / Perez-Montfort, Ruy

Biochimica et biophysica acta. General subjects

2018 Volume 1862, Issue 6, Page(s) 1401–1409

Abstract: Human triosephosphate isomerase (TIM) deficiency is a very rare disease, but there are several mutations reported to be causing the illness. In this work, we produced nine recombinant human triosephosphate isomerases which have the mutations reported to ... ...

Abstract	Human triosephosphate isomerase (TIM) deficiency is a very rare disease, but there are several mutations reported to be causing the illness. In this work, we produced nine recombinant human triosephosphate isomerases which have the mutations reported to produce TIM deficiency. These enzymes were characterized biophysically and biochemically to determine their kinetic and stability parameters, and also to substitute TIM activity in supporting the growth of an Escherichia coli strain lacking the tim gene. Our results allowed us to rate the deleteriousness of the human TIM mutants based on the type and severity of the alterations observed, to classify four "unknown severity mutants" with altered residues in positions 62, 72, 122 and 154 and to explain in structural terms the mutation V231M, the most affected mutant from the kinetic point of view and the only homozygous mutation reported besides E104D.
MeSH term(s)	Anemia, Hemolytic, Congenital Nonspherocytic/enzymology ; Anemia, Hemolytic, Congenital Nonspherocytic/genetics ; Carbohydrate Metabolism, Inborn Errors/enzymology ; Carbohydrate Metabolism, Inborn Errors/genetics ; Enzyme Stability ; Humans ; Kinetics ; Models, Molecular ; Mutagenesis, Site-Directed ; Mutation ; Protein Conformation ; Triose-Phosphate Isomerase/chemistry ; Triose-Phosphate Isomerase/deficiency ; Triose-Phosphate Isomerase/genetics ; Triose-Phosphate Isomerase/metabolism
Chemical Substances	Triose-Phosphate Isomerase (EC 5.3.1.1)
Language	English
Publishing date	2018-03-20
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0304-4165 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0304-4165 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagen.2018.03.019
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Article ; Online: Naturally occurring deamidated triosephosphate isomerase is a promising target for cell-selective therapy in cancer.

Enríquez-Flores, Sergio / Flores-López, Luis A / De la Mora-De la Mora, Ignacio / García-Torres, Itzhel / Gracia-Mora, Isabel / Gutiérrez-Castrellón, Pedro / Fernández-Lainez, Cynthia / Martínez-Pérez, Yoalli / Olaya-Vargas, Alberto / de Vos, Paul / López-Velázquez, Gabriel

Scientific reports

2022 Volume 12, Issue 1, Page(s) 4028

Abstract: Human triosephosphate isomerase (HsTIM) is a central glycolytic enzyme and is overexpressed in cancer cells with accelerated glycolysis. Triple-negative breast cancer is highly dependent on glycolysis and is typically treated with a combination of ... ...

Abstract	Human triosephosphate isomerase (HsTIM) is a central glycolytic enzyme and is overexpressed in cancer cells with accelerated glycolysis. Triple-negative breast cancer is highly dependent on glycolysis and is typically treated with a combination of surgery, radiation therapy, and chemotherapy. Deamidated HsTIM was recently proposed as a druggable target. Although thiol-reactive drugs affect cell growth in deamidated HsTIM-complemented cells, the role of this protein as a selective target has not been demonstrated. To delve into the usefulness of deamidated HsTIM as a selective target, we assessed its natural accumulation in breast cancer cells. We found that deamidated HsTIM accumulates in breast cancer cells but not in noncancerous cells. The cancer cells are selectively programmed to undergo cell death with thiol-reactive drugs that induced the production of methylglyoxal (MGO) and advanced glycation-end products (AGEs). In vivo, a thiol-reactive drug effectively inhibits the growth of xenograft tumors with an underlying mechanism involving deamidated HsTIM. Our findings demonstrate the usefulness of deamidated HsTIM as target to develop new therapeutic strategies for the treatment of cancers and other pathologies in which this post translationally modified protein accumulates.
MeSH term(s)	Breast Neoplasms ; Female ; Glycolysis ; Humans ; Proteins/metabolism ; Pyruvaldehyde/metabolism ; Sulfhydryl Compounds ; Triose-Phosphate Isomerase/metabolism
Chemical Substances	Proteins ; Sulfhydryl Compounds ; Pyruvaldehyde (722KLD7415) ; Triose-Phosphate Isomerase (EC 5.3.1.1)
Language	English
Publishing date	2022-03-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-022-08051-0
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Article: Further Evidence That Defects in Main Thyroid Dysgenesis-Related Genes Are an Uncommon Etiology for Primary Congenital Hypothyroidism in Mexican Patients: Report of Rare Variants in

Alcántara-Ortigoza, Miguel Angel / Sánchez-Verdiguel, Iraís / Fernández-Hernández, Liliana / Enríquez-Flores, Sergio / González-Núñez, Aidy / Hernández-Martínez, Nancy Leticia / Sánchez, Carmen / González-Del Angel, Ariadna

Children (Basel, Switzerland)

2021 Volume 8, Issue 6

Abstract: Mexico shows a high birth prevalence of congenital hypothyroidism (CH) due to thyroid dysgenesis (TD). ...

Abstract	Mexico shows a high birth prevalence of congenital hypothyroidism (CH) due to thyroid dysgenesis (TD).
Language	English
Publishing date	2021-05-30
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2732685-8
ISSN	2227-9067
ISSN	2227-9067
DOI	10.3390/children8060457
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Article ; Online: Cloning, purification, and characterization of the 6-phosphogluconate dehydrogenase (6 PGDH) from Giardia lamblia.

Morales-Luna, Laura / Hernández-Ochoa, Beatriz / Martínez-Rosas, Víctor / González-Valdez, Abigail / Cárdenas-Rodríguez, Noemi / Enríquez-Flores, Sergio / Marcial-Quino, Jaime / Gómez-Manzo, Saúl

Molecular and biochemical parasitology

2021 Volume 244, Page(s) 111383

Abstract: Giardia lamblia, due to the habitat in which it develops, requires a continuous supply of intermediate compounds that allow it to survive in the host. The pentose phosphate pathway (PPP) provides essential molecules such as NADPH and ribulose-5-phosphate ...

Abstract	Giardia lamblia, due to the habitat in which it develops, requires a continuous supply of intermediate compounds that allow it to survive in the host. The pentose phosphate pathway (PPP) provides essential molecules such as NADPH and ribulose-5-phosphate during the oxidative phase of the pathway. One of the key enzymes during this stage is 6-phosphogluconate dehydrogenase (6 PGDH) for generating NADPH. Given the relevance of the enzyme, in the present work, the 6pgdh gene from G. lamblia was amplified and cloned to produce the recombinant protein (Gl-6 PGDH) and characterize it functionally and structurally after the purification of Gl-6 PGDH by affinity chromatography. The results of the characterization showed that the protein has a molecular mass of 54 kDa, with an optimal pH of 7.0 and a temperature of 36-42 °C. The kinetic parameters of Gl-6 PGDH were K
MeSH term(s)	Amino Acid Motifs ; Binding Sites ; Cloning, Molecular/methods ; Gene Expression ; Geobacillus stearothermophilus/chemistry ; Geobacillus stearothermophilus/enzymology ; Giardia lamblia/enzymology ; Giardia lamblia/genetics ; Gluconates/chemistry ; Gluconates/metabolism ; Humans ; Kinetics ; Models, Molecular ; NADP/chemistry ; NADP/metabolism ; Pentose Phosphate Pathway/genetics ; Phosphogluconate Dehydrogenase/chemistry ; Phosphogluconate Dehydrogenase/genetics ; Phosphogluconate Dehydrogenase/metabolism ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Protozoan Proteins/chemistry ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Ribulosephosphates/chemistry ; Ribulosephosphates/metabolism ; Structural Homology, Protein ; Substrate Specificity ; Thermodynamics
Chemical Substances	Gluconates ; Protozoan Proteins ; Recombinant Proteins ; Ribulosephosphates ; ribulose 5-phosphate (4151-19-3) ; NADP (53-59-8) ; Phosphogluconate Dehydrogenase (EC 1.1.1.43) ; 6-phosphogluconic acid (W31WK7B8U0)
Language	English
Publishing date	2021-05-25
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	756166-0
ISSN	1872-9428 ; 0166-6851
ISSN (online)	1872-9428
ISSN	0166-6851
DOI	10.1016/j.molbiopara.2021.111383
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