Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A series of dihydroxyacetone-phosphate (DHAP) analogues has been synthesized, differing in their stereochemistry and functionality at C-3. The kinetic effects of these compounds on the enzyme aldolase (EC 4.1.2.13) have been studied and differing modes of action observed. Competitive and time dependent reversible inhibition have been shown to take place both with and without borohydride detected formation of an immonium ion.
Bioorg Med Chem 1995 Sep
PMID:Effects of chirality and substituents at carbon 3 in dihydroxyacetone-phosphate analogues on their binding to rabbit muscle aldolase. 856 17

A 22-year-old man developed transient unconsciousness during running. He developed fever, nausea, vomiting, diarrhea and general fatigue. Next day, he was admitted to National Hospital Nayoro because of high serum CK level of 13,610U/l. Biochemical analyses revealed elevated serum myoglobin, increased CK-MM isozyme, aldolase and lactate dehydrogenase, increased serum osmolality, increased uric acid, and decreased serum potassium levels. Therefore, he was diagnosed as having rhabdomyolysis. In addition, serum CK-MB isozyme, cardiac myosin light chain I and troponin T were increased, suggesting the damage of cardiac muscle. Electrocardiogram showed elevated ST segment and inverted T on V2-4, which were not observed previously. He had no preceding infectious disease, drug ingestion or an underlying metabolic disorder. The rhabdomyolysis may be precipitated by the superimposition of dehydration and loss of potassium due to diarrhea and vomiting. The myocardial injury, probably produced by transient myocardial ischemia, should be paid attention in case of rhabdomyolysis.
Rinsho Shinkeigaku 1995 Sep
PMID:[A case of rhabdomyolysis complicated with myocardial injury]. 856 47

Some cysteine-containing proteins upon sulfitolysis have been found to show anomalously retarded SDS-PAGE mobilities in non-reducing gels. These proteins include bovine serum albumin, ovalbumin, aldolase, ribonuclease and a recombinant fusion protein (XA) consisting of a portion of gamma-interferon linked to the A chain of human insulin. This mobility shift has been employed to determine the stability of the sulfonated products and to study the kinetics of the sulfitolysis reaction. Partially sulfonated products of intermediate shifts were observed at 0.01% beta-ME, while 0.05% beta-ME gave a shift characteristic of the completely reduced protein. The undiluted sulfitolysis reagent reacted with XA to give within 1 min a gel shift characteristic of the fully sulfitolysed protein. Its transition stages could be visualized at 15, 30 and 60 min when the reagent was diluted four-fold. In the presence of 8 M urea, the sulfitolysis of BSA was nearly complete at 30 min when the sulfitolysis reagent was used at a dilution of 1:5. However, under the same conditions BSA was predominantly unsulfitolysed in the absence of urea. In order to elucidate the mechanism of sulfonation shift, several derivatives of XA, e.g. performic acid oxidized, alkylated with (a) iodoacetamide and (b) iodoacetate, have been prepared. While the mobility of XASSO3- was sensitive to the presence of beta-ME, all other derivatives moved in a beta-ME-insensitive fashion. Furthermore, while the nonreducing mobilities of the acidic derivatives (-SSO3-, -SO3- and -SCH2CO2-) were anomalously retarded and identical, the mobility of the iodoacetamide derivative was intermediate between the retarded acidic derivatives above and XA below. These studies have suggested a role of the extended conformation of the A chain of insulin in causing a mobility shift of the acidic derivatives in this series. Similar results were observed in an analogous series of derivatives prepared from BSA. Non-denaturing gel filtration analyses of native vs. sulfitolysed samples of serum albumin, ovalbumin and ribonuclease have indicated that the sulfitolysed proteins elute earlier than their native counterparts and appear to be significantly larger than their true molecular weights. Circular dichroism analysis has indicated significant loss in helicity of sulfitolysed BSA. This suggests that the retarded mobility of sulfitolysed proteins seen on SDS-PAGE is likely to be due to an expansion in the hydrodynamic volumes of these proteins, a phenomenon triggered by cleavage of disulfide bonds and further accentuated by the introduction of strongly negatively charged sulfonates.
Int J Pept Protein Res 1996 Sep
PMID:Anomalous mobility of sulfitolysed proteins in SDS-PAGE. Analysis and applications. 889 91

Among progeny of a hybrid (Rana shqiperica x R. lessonae) x R. lessonae, 14 of 22 loci form four linkage groups (LGs): (1) mitochondrial aspartate aminotransferase, carbonate dehydratase-2, esterase 4, peptidase D; (2) mannosephosphate isomerase, lactate dehydrogenase-B, sex, hexokinase-1, peptidase B; (3) albumin, fructose-biphosphatase-1, guanine deaminase; (4) mitochondrial superoxide dismutase, cytosolic malic enzyme, xanthine oxidase. Fructose-biphosphate aldolase-2 and cytosolic aspartate aminotransferase possibly form a fifth LG. Mitochondrial aconitate hydratase, alpha-glucosidase, glyceraldehyde-3-phosphate dehydrogenase, phosphogluconate dehydrogenase, and phosphoglucomutase-2 are unlinked to other loci. All testable linkages (among eight loci of LGs 1, 2, 3, and 4) are shared with eastern palearctic water frogs. Including published data, 44 protein loci can be assigned to 10 of the 13 chromosomes in Holarctic Rana. Of testable pairs among 18 protein loci, agreement between Palearctic and Nearctic Rana is complete (125 unlinked, 14 linked pairs among 14 loci of five syntenies), and Holarctic Rana and Xenopus laevis are highly concordant (125 shared nonlinkages, 13 shared linkages, three differences). Several Rana syntenies occur in mammals and fish. Many syntenies apparently have persisted for 60-140 x 10(6) years (frogs), some even for 350-400 x 10(6) years (mammals and teleosts).
Genetics 1997 Sep
PMID:Linkage groups of protein-coding genes in western palearctic water frogs reveal extensive evolutionary conservation. 928 85

The electrostatic properties of seven alpha/beta-barrel enzymes selected from different evolutionary families were studied: triose phosphate isomerase, fructose-1,6-bisphosphate aldolase, pyruvate kinase, mandelate racemase, trimethylamine dehydrogenase, glycolate oxidase, and narbonin, a protein without any known enzymatic activity. The backbone of the alpha/beta-barrel has a distinct electrostatic field pattern, which is dipolar along the barrel axis. When the side chains are included in the calculations the general effect is to modulate the electrostatic pattern so that the electrostatic field is generally enhanced and is focused into a specific area near the active site. We use the electrostatic flux through a square surface near the active site to gauge the functionally relevant magnitude of the electrostatic field. The calculations reveal that in six out of the seven cases the backbone itself contributes greater than 45% of the total flux. The substantial electrostatic contribution of the backbone correlates with the known preference of alpha/beta-barrel enzymes for negatively charged substrates.
Protein Sci 1997 Sep
PMID:Backbone makes a significant contribution to the electrostatics of alpha/beta-barrel proteins. 930 Apr 84

Structural relationships between the myofibrillar contractile apparatus and the enzymes that generate ATP for muscle contraction are not well understood. We explored whether glycolytic enzymes are localized in Drosophila flight muscle and whether localization is required for function. We find that glycerol-3-phosphate dehydrogenase (GPDH) is localized at Z-discs and M-lines. The glycolytic enzymes aldolase and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) are also localized along the sarcomere with a periodic pattern that is indistinguishable from that of GPDH localization. Furthermore, localization of aldolase and GAPDH requires simultaneous localization of GPDH, because aldolase and GAPDH are not localized along the sarcomere in muscles of strains that carry Gpdh null alleles. In an attempt to understand the process of glycolytic enzyme colocalization, we have explored in more detail the mechanism of GPDH localization. In flight muscle, there is only one GPDH isoform, GPDH-1, which is distinguished from isoforms found in other tissues by having three C-terminal amino acids: glutamine, asparagine, and leucine. Transgenic flies that can produce only GPDH-1 display enzyme colocalization similar to wild-type flies. However, transgenic flies that synthesize only GPDH-3, lacking the C-terminal tripeptide, do not show the periodic banding pattern of localization at Z-discs and M-lines for GPDH. In addition, neither GAPDH nor aldolase colocalize at Z-discs and M-lines in the sarcomeres of muscles from GPDH-3 transgenic flies. Failure of the glycolytic enzymes to colocalize in the sarcomere results in the inability to fly, even though the full complement of active glycolytic enzymes is present in flight muscles. Therefore, the presence of active enzymes in the cell is not sufficient for muscle function; colocalization of the enzymes is required. These results indicate that the mechanisms by which ATP is supplied to the myosin ATPase, for muscle contraction, requires a highly organized cellular system.
Mol Biol Cell 1997 Sep
PMID:Flight muscle function in Drosophila requires colocalization of glycolytic enzymes. 930 64

It is known that the serum in cancer patients has the characteristics of the heat-stability. The factor produce the heat-stability is known to be due to tumor marker(TM) such as CEA, CA125(glycoprotein), CA19-9, CA15-3, SLX, CA50, CA72-4, DU-PAN-2, ST-439, SPAN-1(mucin) and alpha 1-acid glycoprotein, IAP(acute reactants). CEA belongs to IgG supergene family protein and is not oncofetal protein. CA19-9 is synthesis in subjects with Le(a) or Le(b) type, but negative in Le(a- b-) type. Thus, CA19-9 is not available as TM in Le(a- b-) type. Many TMs can be classified in 3 types because cancer cell has the character of immature cells which composed of immature proteins or glycoproteins. (1) Oncofetal protein: AFP(fetal albumin), PTHrP(fetal PTH) (2) The immature isozyme type: increase of amylase(salivary type), CPK(brain type) and aldolase (muscle and brain type) (3) The immature protein in biosynthesis process: increase of precursor protein(prepro type or pro type) such as PIVKA-II(preprothrombin), ProGRP, TPA or CYFRA 21-1(pro-keratin?) and hormone precursor in hormone producing tumor.
Rinsho Byori 1997 Sep
PMID:[Tumor marker--present and future]. 931 Dec 62

We report a 26-year-old man with eosinophilic fasciitis who presented with progressive joint contractures of all four limbs. In this patient, the serum aldolase concentration was elevated while the serum creatinine kinase concentration was normal. Magnetic resonance imaging showed gadolinium enhancement of fascial structures in the lower limbs. With the clinical improvement by the treatment with oral corticosteroid, the aldolase concentration was decreased, and the fascial hyperintensity on magnetic resonance images was reduced. The phenomenon of increased an aldolase concentration accompanied by a normal creatinine kinase concentration may be characteristic of eosinophilic fasciitis. Serial magnetic resonance images and serum aldolase concentration are useful for monitoring the therapeutic response in this condition.
Intern Med 1997 Sep
PMID:Magnetic resonance imaging and serum aldolase concentration in eosinophilic fasciitis. 931 13

D-Threonine aldolase is an enzyme that catalyzes the cleavage of D-threonine into glycine and acetaldehyde. Its activity was found in several genera of bacteria such as Arthrobacter, Alcaligenes, Xanthomonas, and Pseudomonas, but not in yeasts or fungi. The enzyme was purified to homogeneity from one strain, Arthrobacter sp. DK-38. The enzyme appeared to consist of a single polypeptide chain with an apparent molecular mass of 51 kDa. This enzyme, as well as L-threonine aldolase, requires pyridoxal 5'-phosphate (pyridoxal-P) as a coenzyme. Unlike other pyridoxal-P enzymes, D-threonine aldolase also requires a divalent cation such as Co2+, Ni2+, Mn2+, or Mg2+ for its catalytic activity. The enzyme completely lost its activity in the absence of either pyridoxal-P or a divalent cation. A divalent cation was also essential for the thermal stability of the enzyme. The metal-free enzyme tends to become thermally unstable, resulting in the irreversible loss of its catalytic activity. The enzyme is strictly D-specific for the alpha-position, whereas it cannot distinguish between threo and erythro forms at the beta-position. Thus, D-threonine and D-allothreonine act as substrates of the enzyme, but their kinetic parameters are different; the Km and Vmax values are 3.81 mM and 38.8 micromol x min(-1) x mg(-1) toward D-threonine, and 14.0 mM and 102 micromol x min(-1) x mg(-1) toward D-allothreonine. respectively. The aldolase reaction is reversible, and the enzyme is therefore able to produce nearly equimolar amounts of D-threonine and D-allothreonine through C-C bond formation between glycine and acetaldehyde. The enzyme also acts, in the same manner, on several other D-beta-hydroxy-alpha-amino acids, including D-beta-phenylserine, D-beta-hydroxy-alpha-aminovaleric acid, D-beta-3,4-dihydroxyphenylserine, and D-beta-3,4-methylenedioxyphenylserine.
Eur J Biochem 1997 Sep 01
PMID:Isolation and characterization of D-threonine aldolase, a pyridoxal-5'-phosphate-dependent enzyme from Arthrobacter sp. DK-38. 934 93

The herbal remedy extended by Semecarpus anacardium nut extract against Aflatoxin B1 mediated hepatocellular carcinoma was established by studies on carbohydrate metabolizing enzymes. Since some definite correlation exists between tumour progression and the activities of glycolytic and gluconeogenic enzymes, assessment of alterations in their activity can be used as successful markers of diagnosis and prognosis. The present work compares the activities of glycolytic and gluconeogenic enzymes in hepatocellular carcinoma bearing rats with drug-treated animals. An overall increase in glycolytic enzymes namely hexokinase, phosphoglucoisomerase, and aldolase with a subsequent reduction in gluconeogenic enzymes, glucose-6-phosphatase and fructose-1,6-biphosphatase was observed in plasma and liver homogenates of hepatocellular carcinoma bearing rats. The administration of Semecarpus anacardium nut extract caused a significant decrease in the activity of glycolytic enzymes and an increase in gluconeogenic enzymes' activities to near normal values in drug-treated animals.
Pharmacol Res 1997 Sep
PMID:Modulating effect of Semecarpus anacardium Linn. nut extract on glucose metabolizing enzymes in aflatoxin B1-induced experimental hepatocellular carcinoma. 936 62


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