Inactivation of Malonate Semialdehyde Decarboxylase by 3-Halopropiolates:  Evidence for Hydratase Activity†

Biochemistry ◽  
2005 ◽  
Vol 44 (26) ◽  
pp. 9375-9381 ◽  
Author(s):  
Gerrit J. Poelarends ◽  
Hector Serrano ◽  
William H. Johnson ◽  
Christian P. Whitman
Keyword(s):  
Hydratase Activity ◽  
Malonate Semialdehyde Decarboxylase

The Hydratase Activity of Malonate Semialdehyde Decarboxylase:  Mechanistic and Evolutionary Implications

2004 ◽  
Vol 126 (48) ◽  
pp. 15658-15659 ◽  
Author(s):  
Gerrit J. Poelarends ◽  
Hector Serrano ◽  
William H. Johnson ◽  
David W. Hoffman ◽  
Christian P. Whitman
Keyword(s):  
Hydratase Activity ◽  
Malonate Semialdehyde Decarboxylase

scholarly journals AUH, a gene encoding an AU-specific RNA binding protein with intrinsic enoyl-CoA hydratase activity.

1995 ◽  
Vol 92 (6) ◽  
pp. 2051-2055 ◽  
Author(s):  
J. Nakagawa ◽  
H. Waldner ◽  
S. Meyer-Monard ◽  
J. Hofsteenge ◽  
P. Jeno ◽  
...  
Keyword(s):  
Rna Binding ◽  
Binding Protein ◽  
Rna Binding Protein ◽  
Gene Encoding ◽  
Hydratase Activity ◽  
Enoyl Coa Hydratase

scholarly journals Fluorocitrate inhibition of aconitate hydratase and the tricarboxylate carrier of rat liver mitochondria

1973 ◽  
Vol 134 (1) ◽  
pp. 217-224 ◽  
Author(s):  
M. D. Brand ◽  
Susan M. Evans ◽  
J. Mendes-Mourão ◽  
J. B. Chappell
Keyword(s):  
Rat Liver ◽  
Inhibitory Action ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Exchange Reactions ◽  
Aconitate Hydratase ◽  
Isolated Rat Liver ◽  
Tricarboxylate Carrier ◽  
Hydratase Activity ◽  
Isolated Rat

1. The effect of biologically synthesized and purified fluorocitrate on the metabolism of tricarboxylate anions by isolated rat liver mitochondria was investigated, in relation to the claim by Eanes et al. (1972) that this fluoro compound inhibits the tricarboxylate carrier at concentrations at which it has little effect on the aconitate hydratase activity. 2. That the inhibitory action of fluorocitrate is at the level of the aconitate hydratase and not at the level of the tricarboxylate carrier is indicated by the following findings. Although the oxidation of citrate and cis-aconitate, but not that of isocitrate, was inhibited by fluorocitrate, the exchange of internal citrate for external citrate or l-malate was not. Had the tricarboxylate carrier been affected, these latter exchange reactions would have been inhibited. 3. By using aconitate hydratase solubilized from mitochondria it was found that with citrate as substrate the inhibition by fluorocitrate was partially competitive (Ki=3.4×10−8m), whereas with cis-aconitate as substrate the inhibition was partially non-competitive (Ki=3.0×10−8m).

Carbonic anhydrase XII mRNA encodes a hydratase that is differentially expressed along the rabbit nephron

2003 ◽  
Vol 284 (2) ◽  
pp. F399-F410 ◽  
Author(s):  
George J. Schwartz ◽  
Anne M. Kittelberger ◽  
Richard H. Watkins ◽  
Michael A. O'Reilly
Keyword(s):  
Carbonic Anhydrase ◽  
Transmembrane Protein ◽  
Proximal Tubules ◽  
Rabbit Kidney ◽  
Kidney Cortex ◽  
Thick Ascending Limb ◽  
Basolateral Membranes ◽  
Collecting Ducts ◽  
Straight Tubules ◽  
Hydratase Activity

Membrane-bound carbonic anhydrase (CA) facilitates acidification in the kidney. Although most hydratase activity is considered due to CA IV, some in the basolateral membranes could be attributed to CA XII. Indeed, CA IV is glycosylphosphatidylinositol anchored, connoting apical polarization, but CA IV immunoreactivity has been detected on basolateral membranes of proximal tubules. Herein, we determined whether CA XII mRNA was expressed in acidifying segments of the rabbit nephron. The open reading frame of CA XII was sequenced from a rabbit kidney cortex cDNA library; it was 83% identical to human CA XII and coded for a 355-amino acid single-pass transmembrane protein. Northern blot analysis revealed an abundant 4.5-kb message in kidney cortex, medulla, and colon. By in situ hybridization, CA XII mRNA was expressed by proximal convoluted and straight tubules, cortical and medullary collecting ducts, and papillary epithelium. By RT-PCR, CA XII mRNA was abundantly expressed in cortical and medullary collecting ducts and thick ascending limb of Henle's loop; it was also expressed in proximal convoluted and straight tubules but not in glomeruli or S3 segments. FLAG-CA XII of ∼40 kDa expressed in Escherichia coli showed hydratase activity that was inhibited by 0.1 mM acetazolamide. Unlike CA IV, expressed CA XII activity was inhibited by 1% SDS, suggesting insufficient disulfide linkages to stabilize the molecule. Western blotting of expressed CA XII with two anti-rabbit CA IV peptide antibodies showed no cross-reactivity. Our findings indicate that CA XII may contribute to the membrane CA activity of proximal tubules and collecting ducts.

scholarly journals Immunochemical identity of peroxisomal enoyl-CoA hydratase with the peroxisome-proliferation -associated 80,000 mol wt polypeptide in rat liver

1981 ◽  
Vol 89 (3) ◽  
pp. 406-417 ◽  
Author(s):  
MK Reddy ◽  
SA Qreshi ◽  
PF Hollenberg ◽  
JK Reddy
Keyword(s):  
Rat Liver ◽  
Fatty Acyl ◽  
Polyacrylamide Gel ◽  
Lipid Lowering ◽  
Peroxisome Proliferation ◽  
Peroxisome Proliferators ◽  
Heat Labile ◽  
Hydratase Activity ◽  
Oxidation System ◽  
Enoyl Coa Hydratase

Peroxisome proliferators, which induce proliferation of hepatic peroxisomes, have been shown previously to cause a marked increase in an 80,000 mol wt polypeptide predominantly in the light mitochondrial and microsomal fractions of liver of rodents. We now present evidence to show that this hepatic peroxisome-proliferation-associated polypeptide, referred to as polypeptide PPA-80, is immunochemically identical with the multifunctional peroxisome protein displaying heat-labile enoyl-CoA hydratase activity. This conclusion is based on the following observations: (a) the purified polypeptide PPA-80 and the heat- labile enoyl-CoA hydratase from livers of rats treated with the peroxisome proliferators Wy-14,643 {[4-chloro-6(2,3-xylidino)-2-pyrimidinylthio]acetic acid} exhibit identical minimum molecular weights of approximately 80,000 on SDS polyacrylamide gel electrophoresis; (b) these two proteins are immunochemically identical on the basis of ouchterlony double diffusion, immunotitration, rocket immunoelectrophoresis, and crossed immunoelectrophoresis analysis; and (c) the immunoprecipitates formed by antibodies to polypeptide PPA-80 when dissociated on a sephadex G-200 column yield enoyl-CoA hydratase activity. Whether the polypeptide PPA-80 exhibits the activity of other enzyme(s) of the peroxisomal β-oxidation system such as fatty acyl-CoA oxidase activity or displays immunochemical identity with such enzymes remains to be determined. The availability of antibodies to polypeptide PPA-80 and enoyl-CoA hydratase facilitated immunofluorescent and immunocytochemical localization of the polypeptide PPA- 80 and enoyl-CoA hydratase in the rat liver. The indirect immunofluorescent studies with these antibodies provided direct visual evidence for the marked induction of polypeptide PPA-80 and enoyl-CoA hydratase in the livers of rats treated with Wy-14,643. The present studies also provide immunocytochemical evidence for the localization of polypeptide PPA- 80 and the heat-labile enoyl-CoA hydratase in the peroxisome, but not in the mitochondria, of hepatic parenchymal cells. These studies, therefore, provide morphological evidence for the existence of fatty acyl-CoA oxidizing system in peroxisomes. An increase of polypeptide PPA-80 on SDS polyacrylamide gel electrophoretic analysis of the subcellular fractions of liver of rodents treated with lipid-lowering drugs should serve as a reliable and sensitive indicator of enhanced peroxisomal β- oxidation system.

INTERINDIVIDUAL VARIATIONS OF EPOXIDE HYDRATASE ACTIVITY IN HUMAN LIVER AND LUNG BIOPSIES, LYMPHOCYTES AND FIBROBLAST CULTURES

1980 ◽  
pp. 651-654 ◽  
Author(s):  
H.R. Glatt ◽  
J. Lorenz ◽  
R. Fleischmann ◽  
H. Remmer ◽  
E.E. Ohnhaus ◽  
...  
Keyword(s):  
Human Liver ◽  
Interindividual Variations ◽  
Fibroblast Cultures ◽  
Epoxide Hydratase ◽  
Hydratase Activity ◽  
Lung Biopsies

scholarly journals IDDF2019-ABS-0245 Suppression of fumarate hydratase activity increases the efficacy of cisplatin-mediated chemotherapy in gastric cancer

2019 ◽  
Author(s):  
Hong-En Yu ◽  
Feng Wang ◽  
Fang Yu ◽  
Huai-Qiang Ju ◽  
Rui-Hua Xu ◽  
...  
Keyword(s):  
Gastric Cancer ◽  
Fumarate Hydratase ◽  
Hydratase Activity

Changes in soluble carbonic anhydrase activity in response to maturation and NH4Cl loading in the rabbit

1991 ◽  
Vol 261 (5) ◽  
pp. R1204-R1213 ◽  
Author(s):  
L. P. Brion ◽  
B. J. Zavilowitz ◽  
O. Rosen ◽  
G. J. Schwartz
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Activity ◽  
Interindividual Variation ◽  
Kidney Cortex ◽  
Significant Activity ◽  
Outer Medulla ◽  
Two Factors ◽  
Hydratase Activity ◽  
Three Stages ◽  
Acid Loading

Maturation and systemic acidosis are two factors that stimulate urinary acidification. Proton secretion, CO2 handling, and some metabolic processes are facilitated by cytosolic carbonic anhydrase (CA). The activity of this enzyme in kidney, red blood cells (RBCs), and liver could be regulated in response to acid-base perturbations or maturation. Therefore, we investigated the effects of maturation and NH4Cl acid loading on soluble CA hydratase activity in RBCs, kidneys, and livers of female New Zealand White rabbits during three stages of maturation (neonatal, 4 wk, and adult). Total RBC CA activity doubled with maturation but did not increase after NH4Cl loading. There was substantial interindividual variation in the amount of CA I related activity. In the kidney we found intrinsic cortical CA II activity to be more than twice that in the outer medulla, which was more than twice that in the inner medulla. CA activity doubled with maturation in the cortex and increased by 70% in the outer medulla. Twenty hours after an NH4Cl load there was a 50% increase in renal cortical CA activity in 4-wk-old rabbits, but a comparable increase in cortical CA activity was only seen after 3-5 days of NH4Cl loading in adult animals. In the liver a third of cytosolic CA activity was acetazolamide resistant, presumably CA III, which doubled with maturation. Chronic NH4Cl loading in adult animals induced an almost 60% increase in hepatic acetazolamide-sensitive CA activity (mostly CA II). These data show that in the rabbit there is a renal corticomedullary gradient in soluble CA activity (mostly CA II), with significant activity in the inner medulla. Maturation induced total CA activity in the inner medulla. Maturation induced total CA activity in RBCs, CA II activity in kidney cortex and outer medulla, and CA III in the liver. Finally, CA II activity in kidney cortex and liver appeared to be regulated in response to some conditions of NH4Cl loading.

scholarly journals Microbial Production of Conjugated Linoleic Acid and Conjugated Linolenic Acid Relies on a Multienzymatic System

2018 ◽  
Vol 82 (4) ◽  
Author(s):  
Ana S. Salsinha ◽  
Lígia L. Pimentel ◽  
Ana L. Fontes ◽  
Ana M. Gomes ◽  
Luis M. Rodríguez-Alcalá
Keyword(s):  
Fatty Acids ◽  
Production Capacity ◽  
Microbial Production ◽  
Screening Tools ◽  
Analytical Determination ◽  
Enzymatic Reactions ◽  
Content Type ◽  
Hydratase Activity ◽  
Available Information

SUMMARYConjugated linoleic acids (CLAs) and conjugated linolenic acids (CLNAs) have gained significant attention due to their anticarcinogenic and lipid/energy metabolism-modulatory effects. However, their concentration in foodstuffs is insufficient for any therapeutic application to be implemented. From a biotechnological standpoint, microbial production of these conjugated fatty acids (CFAs) has been explored as an alternative, and strains of the generaPropionibacterium,Lactobacillus, andBifidobacteriumhave shown promising producing capacities. Current screening research works are generally based on direct analytical determination of production capacity (e.g., trial and error), representing an important bottleneck in these studies. This review aims to summarize the available information regarding identified genes and proteins involved in CLA/CLNA production by these groups of bacteria and, consequently, the possible enzymatic reactions behind such metabolic processes. Linoleate isomerase (LAI) was the first enzyme to be described to be involved in the microbiological transformation of linoleic acids (LAs) and linolenic acids (LNAs) into CFA isomers. Thus, the availability oflaigene sequences has allowed the development of genetic screening tools. Nevertheless, several studies have reported that LAIs have significant homology with myosin-cross-reactive antigen (MCRA) proteins, which are involved in the synthesis of hydroxy fatty acids, as shown by hydratase activity. Furthermore, it has been suggested that CLA and/or CLNA production results from a stress response performed by the activation of more than one gene in a multiple-step reaction. Studies on CFA biochemical pathways are essential to understand and characterize the metabolic mechanism behind this process, unraveling all the gene products that may be involved. As some of these bacteria have shown modulation of lipid metabolismin vivo, further research to be focused on this topic may help us to understand the role of the gut microbiota in human health.

scholarly journals Kinetic, Mutational, and Structural Analysis of Malonate Semialdehyde Decarboxylase fromCoryneformBacterium Strain FG41: Mechanistic Implications for the Decarboxylase and Hydratase Activities

Biochemistry ◽  
2013 ◽  
Vol 52 (28) ◽  
pp. 4830-4841 ◽  
Author(s):  
Youzhong Guo ◽  
Hector Serrano ◽  
Gerrit J. Poelarends ◽  
William H. Johnson ◽  
Marvin L. Hackert ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Malonate Semialdehyde Decarboxylase
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