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Query: UNIPROT:P06889 (Mol)
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We have isolated a novel nodule-specific cDNA clone, GmN56, from soybean root nodules. The expression of GmN56 was induced almost concomitantly with the onset of nitrogen fixation, together with leghemoglobin and other late nodulin genes. In situ hybridization studies demonstrated the localization of GmN56 mRNA in the bacterial infected cells of mature nodules. The predicted amino acid sequence of the GmN56 protein exhibits significant homology to those of LeuA (isopropylmalate synthase) of several microorganisms and NifV (putative homocitrate synthase) of nitrogen-fixing bacteria, suggesting that GmN56 encodes an enzyme catalyzing a reaction involving acetyl-CoA and alpha-keto acid as substrates.
Mol Plant Microbe Interact
PMID:GmN56, a novel nodule-specific cDNA from soybean root nodules encodes a protein homologous to isopropylmalate synthase and homocitrate synthase. 753 40

In the adipose tissue, besides fatty acid synthesis (FA-S) from glucose, which includes several mitochondrial steps, FA-S from glutamate has been demonstrated. FA-S from glutamate takes place in the cytosol through the backward pathway of Krebs cycle (BPKC) and is due to the sequential action of (1) alanine aminotransferase (ALT, EC 2.6.1.2), which is presence of pyruvate converts glutamate to oxoglutarate; (2) isocitrate dehydrogenase (NADP) (ICDH, EC 1.1.1.42), which converts oxoglutarate to isocitrate; (3) aconitate hydratase (ACO, EC 4.2.1.3), which transforms isocitrate to citrate: and (4) ATP citrate-lyase (ATP-CL, EC 4.1.3.8), which splits citrate to yield the acetyl-CoA needed for FA-S. We studied the enzymes involved in BPKC in homogenates of human adipose tissue. In normal subjects, the cytosolic activity (mumol/min/g protein) was: ALT = 10.3 +/- 1.1, ICDH = 29.5 +/- 2.8, ACO = 2.05 +/- 0.23, and ATP-CL = 1.2 +/- 0.2. Mitochondria contained less or no activity, values being 20, 9, 11, and 0% of total for ATL, ICDH, ACO, and ATP-CL, respectively. BPKC enzymes are more active than the enzymes limiting FA-S from glucose, i.e., phosphofructokinase (EC 2.7.1.11), pyruvate carboxylase (EC 6.4.1.1), and pyruvate dehydrogenase (EC 1.2.4.1). In the obese patients, cytosolic ALT and ATP-CL were increased (12.9 +/- 0.7, P < 0.05, and 2.28 +/- 0.27, P < 0.01, respectively) compared to normal, while ICDH was not changed (ACO could not be studied). Similar changes were obtained by expressing enzyme activity per fat cell number.(ABSTRACT TRUNCATED AT 250 WORDS)
Biochem Mol Med 1995 Feb
PMID:Fatty acid synthesis from glutamate in the adipose tissue of normal subjects and obese patients: an enzyme study. 755 12

In the eukaryotic unicellular organism Trichomonas vaginalis a key step of energy metabolism, the oxidative decarboxylation of pyruvate with the formation of acetyl-CoA, is catalyzed by the iron-sulfur protein pyruvate:ferredoxin oxidoreductase (PFO) and not by the almost-ubiquitous pyruvate dehydrogenase multienzyme complex. This enzyme is localized in the hydrogenosome, an organelle bounded by a double membrane. PFO and its closely related homolog, pyruvate:flavodoxin oxidoreductase, are enzymes found in a number of archaebacteria and eubacteria. The presence of these enzymes in eukaryotes is restricted, however, to a few amitochondriate groups. To gain more insight into the evolutionary relationships of T. vaginalis PFO we determined the primary structure of its two genes (pfoA and pfoB). The deduced amino acid sequences showed 95% positional identity. Motifs implicated in related enzymes in liganding the Fe-S centers and thiamine pyrophosphate were well conserved. The T. vaginalis PFOs were found to be homologous to eubacterial pyruvate:flavodoxin oxidoreductases and showed about 40% amino acid identity to these enzymes over their entire length. Lack of eubacterial PFO sequences precluded a comparison. pfoA and pfoB revealed a greater distance from related enzymes of Archaebacteria. The conceptual translation of the nucleotide sequences predicted an amino-terminal pentapeptide not present in the mature protein. This processed leader sequence was similar to but shorter than leader sequences noted in other hydrogenosomal proteins.(ABSTRACT TRUNCATED AT 250 WORDS)
J Mol Evol 1995 Sep
PMID:Primary structure and eubacterial relationships of the pyruvate:ferredoxin oxidoreductase of the amitochondriate eukaryote Trichomonas vaginalis. 756 25

The active site of pig heart citrate synthase contains a histidine residue (H320) which interacts with the carbonyl oxygen of oxaloacetate and is implicated in substrate activation through carbonyl bond polarization, a major catalytic strategy of the enzyme. We report here the effects on the catalytic mechanism of changing this important residue to glycine. H320G shows modest impairment in substrate Michaelis constants [(7-16)-fold] and a large decrease in catalysis (600-fold). For the native enzyme, the chemical intermediate, citryl-CoA, is both hydrolyzed and converted back to reactants, oxaloacetate and acetyl-CoA. In the mutant, citryl-CoA is only hydrolyzed, indicating a major defect in the condensation reaction. As monitored by the carbonyl carbon's chemical shift, the extent of oxaloacetate carbonyl polarization is decreased in all binary and ternary complexes. As indicated by the lack of rapid H320G--oxaloacetate catalysis of the exchange of the methyl protons of acetyl-CoA or the pro-S-methylene proton of propionyl-CoA, the activation of acetyl-CoA is also faulty. Reflecting this defect in acetyl-CoA activation, the carboxyl chemical shift of H320G-bound carboxymethyl-CoA (a transition-state analog of the neutral enol intermediate) fails to decrease on formation of the H3020G-oxaloacetate-carboxymethyl-CoA ternary complex. Progress curves and steady-state data with H320G using citryl-CoA as substrate show unusual properties: substrate inhibition and accelerating progress curves. Either one of two models with subunit cooperativity [Monod, J., Wyman, J., & Changeux, J.-P. (1965) J. Mol. Biol. 12, 88; Koshland, D. E., Jr., Nemethy, G., & Filmer, D. (1966) Biochemistry 5, 365] quantitatively accounts for both the initial velocity data and the individual progress curves. The concentrations of all enzyme forms and complexes are assumed to rapidly reach their equilibrium values compared to the rate of substrate turnover. The native enzyme also behaves according to models for subunit cooperativity with citryl-CoA as substrate. However, the rates of formation/dissociation and reaction of complexes are kinetically significant. Comparisons of the values of kinetic constants between the native and mutants enzymes lead us to conclude that the mutant less readily undergoes a conformation change required for efficient activation of substrates.
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PMID:Catalytic strategy of citrate synthase: subunit interactions revealed as a consequence of a single amino acid change in the oxaloacetate binding site. 757 12

Activities of acetyl-CoA-carboxylase, malic enzyme and glucose-6-phosphate-dehydrogenase were measured in seven different anatomical sites in the growing pig (20-120 kg weight). The three enzyme activities increased up to 40-60 kg weight and then decreased, malic enzyme becoming the main producer of NADPH, irrespective of the adipose tissue. Subcutaneous adipose tissue of the neck area was much thicker and exhibited much lower lipogenic enzyme activities than backfat. Subcutaneous adipose tissue is heterogeneous in the pig with some areas exhibiting very low lipogenesis and high lipid deposition importing triglycerides from other areas with high lipogenesis. However, these conclusions based on the measurement of enzyme activity potentials need to be confirmed with measurements of actual activities.
Comp Biochem Physiol B Biochem Mol Biol 1995 Jul
PMID:Comparative study of in vitro lipogenesis in various adipose tissues in the growing domestic pig (Sus domesticus). 761 62

The biosynthetic pathway of the CoQ polyisoprenoid side chain, starting from acetyl-CoA and proceeding through mevalonate and isopentenylpyrophosphate, is the same as that of cholesterol. We performed this study to evaluate whether vastatins (hypocholesterolemic drugs that inhibit HMG-CoA reductase) modify blood levels of ubiquinone. Thirty-four unrelated outpatients with hypercholesterolemia (IIa phenotype) were treated with 20 mg of simvastatin for a 6-month period (group S) or with 20 mg of simvastatin plus 100 mg CoQ10 (group US). The following parameters were evaluated at time 0, 45, 90, 135 and 180 days: total plasma cholesterol (TC), HDL-cholesterol, LDL-cholesterol (LDL-C), triglycerides (TG), apo A1, apo B and CoQ10 in plasma and platelets. In the S group, there was a marked decrease in TC and LDL-C (from 290.3 mg/dl to 228.7 mg/dl for TC and from 228.7 mg/dl to 167.6 mg/dl for LDL-C) and in plasma CoQ10 levels from 1.08 mg/dl to 0.80 mg/dl. In contrast, in the US group we observed a significant increase of CoQ10 in plasma (from 1.20 to 1.48 mg/dl) while the hypocholesterolemic effect was similar to that observed in the S group. Platelet CoQ10 also decreased in the S group (from 104 to 90 ng/mg) and increased in the US group (from 95 to 145 ng/mg). This study demonstrates that simvastatin lowers both LDL-C and apo B plasma levels together with the plasma and platelet levels of CoQ10, and that CoQ10 therapy prevents both plasma and platelet CoQ10 decrease, without affecting the cholesterol lowering effect of simvastatin.
Mol Aspects Med 1994
PMID:Exogenous CoQ10 supplementation prevents plasma ubiquinone reduction induced by HMG-CoA reductase inhibitors. 775 30

A cDNA clone encoding a major chloroplast inner envelope membrane protein of 96 kDa (IEP96) was isolated and characterized. The protein is synthesized as a larger-molecular-weight precursor (pIEP96) which contains a cleavable N-terminal transit sequence of 50 amino acids. The transit peptide exhibits typical stromal targeting information. It is cleaved in vitro by the stromal processing peptidase, though the mature protein is clearly localized in the inner envelope membrane. Translocation of pIEP96 into chloroplasts is greatly stimulated in the presence of 80 mM potassium phosphate which results in an import efficiency of about 90%. This effect is specific for potassium and phosphate, but cannot be ascribed to a membrane potential across the inner envelope membrane. Protein sequence analysis reveals five stretches of repeats of 26 amino acids in length. The N-terminal 300 amino acids are 45% identical (76% similarity) to the 35 kDa alpha-subunit of acetyl-CoA carboxyl-transferase from Escherichia coli. The C-terminal 500 amino acids share significant similarity (69%) with USOI, a component of the cytoskeleton in yeast.
Plant Mol Biol 1995 Mar
PMID:Import of a new chloroplast inner envelope protein is greatly stimulated by potassium phosphate. 776 98

Acetyl CoA synthetase (ACS; EC 6.2.1.1) was studied in the mosquito, Aedes togoi, by a novel assay which coupled the acetyl-CoA generated to p-aminosalicylic acid (ASA). The N-acetylated product was determined by an HPLC-fluorimetric procedure. High ACS activity was observed in the newly-pupated pupae of both sexes and in the adult male mosquito whose activity was five times that of the female. Acetyl CoA-dependent N-acetyltransferase (NAT; EC 2.3.1.5) activity toward serotonin (5HT) was also studied using HPLC-electrochemical detection (HPLC-ECD). A progressive increase in the 5HT-NAT activity was observed from the fourth-instar larvae to the adult mosquito with the latter showing 6-fold higher activity in the head compared to the abdomen-thorax region. Kinetic studies on the pupal enzyme extracts showed that the apparent Km values for 5HT and acetyl CoA were 63 and 66 microM respectively. Tryptamine inhibited 5HT-NAT non-competitively with a Ki value of 8 microM.
Insect Biochem Mol Biol 1994 May
PMID:Acetyl CoA generation and N-acetylation of serotonin (5HT) in the mosquito, Aedes togoi. 791 72

We investigated the relationship between Escherichia coli flagellar expression and the regulation of acetyl phosphate synthesis and degradation. Using cells either wild type for acetyl phosphate metabolism or defective for phosphotransacetylase or acetate kinase, or both, we measured flagellar expression and the intracellular concentration of acetyl phosphate relative to growth phase and temperature. Under the conditions tested, we found that elevated levels of acetyl phosphate corresponded to inhibition of flagellar synthesis. To extend these observations, we measured the intracellular concentration of acetyl-CoA, the level of expression from the pta and ackA promoters, and the activities of phosphotransacetylase and acetate kinase derived from cell lysates. Relative to increasing culture density, acetyl-CoA levels and expression from both the pta and ackA promoters decreased. Relative to increasing temperature, expression from the ackA promoter decreased and phosphotransacetylase activity increased. In contrast, temperature had little or no effect on either acetate kinase activity or expression from the pta promoter. We propose that cells regulate intracellular acetyl phosphate concentrations relative to growth phase and temperature by modulating the availability of acetyl-CoA, the expression of ackA, and the activity of phosphotransacetylase.
Mol Microbiol 1994 Jun
PMID:Regulation of acetyl phosphate synthesis and degradation, and the control of flagellar expression in Escherichia coli. 793 4

Entamoeba histolytica ferments glucose to ethanol under the anaerobic conditions of the human colon. There is special interest in this metabolic pathway because it provides an opportunity for parasite-specific chemotherapy. Peptide sequences from a 97-kDa E. histolytica protein, which was originally isolated because of extracellular matrix binding properties, were used to clone and sequence a gene that was found to encode an E. histolytica alcohol dehydrogenase and acetaldehyde dehydrogenase (EhADH2). The EhADH2 cDNA clone had an open reading frame encoding 870 amino acids with a predicted molecular weight of 95,758. The EhADH2 cDNA clone was identical in 48% of its amino acids to the multifunctional enzyme (alcohol dehydrogenase, acetyl-CoA reductase, and pyruvate-formate-lyase-deactivase) encoded by the Escherichia coli adhE gene. The isolation of the EhADH2 protein helps define a new family of ADH enzymes that may be specific to anaerobic and facultatively anaerobic organisms.
Mol Biochem Parasitol 1994 Apr
PMID:Entamoeba histolytica has an alcohol dehydrogenase homologous to the multifunctional adhE gene product of Escherichia coli. 793 3


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