Rosario A. Muñoz‐Clares

ORCID: 0000-0002-0115-3565
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About
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Research Areas
  • Enzyme Structure and Function
  • Metabolomics and Mass Spectrometry Studies
  • Metabolism and Genetic Disorders
  • Microbial Metabolic Engineering and Bioproduction
  • Biotin and Related Studies
  • Amino Acid Enzymes and Metabolism
  • Mitochondrial Function and Pathology
  • Biochemical Acid Research Studies
  • Photosynthetic Processes and Mechanisms
  • Alcoholism and Thiamine Deficiency
  • Diet and metabolism studies
  • Alcohol Consumption and Health Effects
  • Protein Structure and Dynamics
  • Folate and B Vitamins Research
  • Plant Stress Responses and Tolerance
  • Vitamin C and Antioxidants Research
  • GABA and Rice Research
  • Biochemical and biochemical processes
  • Polyamine Metabolism and Applications
  • Biochemical effects in animals
  • Muscle metabolism and nutrition
  • Tryptophan and brain disorders
  • Aldose Reductase and Taurine
  • Biochemical and Molecular Research
  • Metabolism, Diabetes, and Cancer

Universidad Nacional Autónoma de México
2014-2024

Universidad Autónoma de la Ciudad de México
2018-2019

University of Manchester
1980-1981

Universidad de Granada
1979-1980

The renal-specific Na + -K -2Cl − cotransporter NKCC2 belongs to the SLC12 gene family; it is target for loop diuretics and cause of type I Bartter's syndrome. Because sequence contains two putative N-linked glycosylation sites, one which conserved with renal -Cl in affects thiazide affinity, we assessed role on functional properties. One (N442Q or N452Q) both (N442,452Q) N-glycosylation sites were eliminated by site-directed mutagenesis. Wild-type mutant clones expressed Xenopus laevis...

10.1152/ajprenal.00071.2005 article EN AJP Renal Physiology 2005-11-16

Abstract Plant Aldehyde Dehydrogenase10 (ALDH10) enzymes catalyze the oxidation of ω-primary or ω-quaternary aminoaldehydes, but, intriguingly, only some them, such as spinach (Spinacia oleracea) betaine aldehyde dehydrogenase (SoBADH), efficiently oxidize (BAL) forming osmoprotectant glycine (GB), which confers tolerance to osmotic stress. The crystal structure SoBADH reported here shows tyrosine (Tyr)-160, tryptophan (Trp)-167, Trp-285, and Trp-456 in an arrangement suitable for cation-π...

10.1104/pp.112.194514 article EN cc-by PLANT PHYSIOLOGY 2012-02-16

Betaine aldehyde dehydrogenase (BADH) (EC 1.2.1.8) catalyzes the last, irreversible step in synthesis of osmoprotectant glycine betaine from choline. In Pseudomonas aeruginosa this reaction is also an obligatory assimilation carbon and nitrogen when bacteria are growing choline or precursors. We present here a method for rapid purification to homogeneity enzyme by use ion-exchange affinity chromatographies on 2',5'-ADP-Sepharose, which results high yield pure with specific activity at 30...

10.1128/jb.181.4.1292-1300.1999 article EN Journal of Bacteriology 1999-02-15

Betaine aldehyde dehydrogenase (BADH) catalyses the irreversible oxidation of betaine to glycine with concomitant reduction NAD(P)(+) NADP(H). In Pseudomonas aeruginosa this reaction is a compulsory step in assimilation carbon and nitrogen when bacteria are growing choline or precursors. The kinetic mechanisms NAD(+)- NADP(+)-dependent reactions were examined by steady-state methods dinucleotide binding experiments. double-reciprocal patterns obtained for initial velocity product dead-end...

10.1042/bj3520675 article EN Biochemical Journal 2000-12-08

Plant ALDH10 enzymes are aminoaldehyde dehydrogenases (AMADHs) that oxidize different ω-amino or trimethylammonium aldehydes, but only some of them have betaine aldehyde dehydrogenase (BADH) activity and produce the osmoprotectant glycine (GB). The latter possess alanine cysteine at position 441 (numbering spinach enzyme, SoBADH), while those ALDH10s cannot (BAL) isoleucine this position. Only plants contain A441- C441-type isoenzymes accumulate GB in response to osmotic stress. In work we...

10.1186/1471-2229-14-149 article EN cc-by BMC Plant Biology 2014-01-01

Abstract It has been a common practice to assay phosphoenolpyruvate carboxylase (PEPC) under high, nonphysiological concentrations of Mg2+ and bicarbonate. We have performed kinetic studies on the enzyme from maize (Zea mays) leaves at near physiological levels free (0.4 mm) bicarbonate (0.1 mm), found that both nonphosphorylated phosphorylated enzymes exhibited high degree cooperativity in binding phosphoenolpyruvate, much lower affinity for this substrate activators, greater malate than...

10.1104/pp.123.1.149 article EN PLANT PHYSIOLOGY 2000-05-01

The purpose of the present study was to determine major functional, pharmacological, and regulatory properties flounder thiazide-sensitive Na-Cl cotransporter (flTSC) make a direct comparison with our recent characterization rat TSC (rTSC; Monroy A, Plata C, Hebert SC, Gamba G. Am J Physiol Renal 279: F161–F169, 2000). When expressed in Xenopus laevis oocytes, flTSC exhibits lower affinity for Na + than Cl − , apparent Michaelis-Menten constant ( K m ) values 58.2 ± 7.1 22.1 4.2 mM,...

10.1152/ajprenal.00284.2001 article EN AJP Renal Physiology 2002-04-01

PaBADH (Pseudomonas aeruginosa betaine aldehyde dehydrogenase) catalyses the irreversible NAD(P)+-dependent oxidation of to its corresponding acid, osmoprotector glycine betaine. This reaction is involved in catabolism choline and response this important pathogen osmotic oxidative stresses prevalent infection sites. The crystal structure complex with NADPH showed a novel covalent adduct between C2N pyridine ring sulfur atom catalytic cysteine residue, Cys286. kind has not been reported...

10.1042/bj20110376 article EN Biochemical Journal 2011-07-12

The kinetics of the oxidation betaine aldehyde catalyzed by NAD+-betaine-aldehyde dehydrogenase, purified from amaranth leaves subjected to water deficit, were analyzed steady state initial velocity and product dead-end inhibition studies at low substrate concentrations.Only one product, NADH, gives inhibition.The other reaction, glycine betaine, does not inhibit enzyme even concentrations as high 10 m.In experiments, AMP choline used analogs NAD+ aldehyde, respectively.The families...

10.1016/s0021-9258(20)80458-x article EN cc-by Journal of Biological Chemistry 1993-11-01
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