Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.2.1.13 (glyceraldehyde-3-phosphate dehydrogenase)
 6,511 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of K2PtCl4, cis-Pt(NH3)2Cl2, and trans-Pt(NH3)2Cl2 on the activities of glyceraldehyde-3-phosphate dehydrogenase, glucose-6-phosphate dehydrogenase, dihydrofolate reductase, fructose-1,6-bisphosphate aldolase, catalase, tyrosinase, and peroxidase have been investigated. All of the enzymes which are thought to have essential sulfhydryl groups (glyceraldehyde-3-phosphate dehydrogenase, aldolase, and glucose-6-phosphate dehydrogenase) were significantly inhibited by K2PtCl4. The other four enzymes studied are not known to have essential sulfhydryl groups, and were not significantly affected by the Pt compounds under the conditions employed. Glyceraldehyde-3-phosphate dehydrogenase was the only enzyme inhibited by all three Pt compounds tested, with K2PtCl4 being the most effective and cis-Pt(NH3)2Cl2 the least effective inhibitor. Semilogarithmic plots of residual activity versus inhibition time indicated that the inhibition reactions were not simple first-order processes, except for the inhibition of glucose-6-phosphate dehydrogenase by K2PtCl4 which appeared to be first-order with respect to enzyme concentration.
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PMID:The effects of platinum complexes on seven enzymes. 11 85

The NH2-terminal amino acid sequence of rat skeletal muscle glyceraldehydephosphate dehydrogenase (D-glyceraldehyde-3-phosphate : NAD+ oxidoreductase(physphorylating), EC 1.2.1.12) was determined to be Val-Lys-Val-Gly-Val-Asn-Gly-Phe-Gly-Arg-Ile-Gly-Arg-Leu-Val-Thr-Arg-Ala-Ala-Phe-Ser-Ser-(-)-(-)--Val-Asx-Ile-Val-Ala-Ile. The presence of Asn instead of Asp in position 6 differentiates this enzyme from other glyceraldehyde-3-phosphate dehydrogenases so far sequenced with the exception of the enzymes isolated from liver. The location of Asn in position 6 has been considered as a specific property of liver glyceraldehyde-3-phosphate dehydrogenase (Kulbe, K.D., Jackson, K.W. and Tang, J. (1975) Biochem. Biophys. Res. Commun. 67, 35--42); this suggestion is not sustained by the results of the present investigation. The amino acid composition of the rat skeletal muscle dehydrogenase demonstrates the unusually low histidine content of this enzyme as compared to other mammalian muscle glyceraldehyde-phosphate dehydrogenases.
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PMID:Structural studies on glyceraldehyde-phosphate dehydrogenase from rat skeletal muscle. 62 46

The surface of streptococci presents an array of different proteins, each designed to perform a specific function. In an attempt to understand the early events in group A streptococci infection, we have identified and purified a major surface protein from group A type 6 streptococci that has both an enzymatic activity and a binding capacity for a variety of proteins. Mass spectrometric analysis of the purified molecule revealed a monomer of 35.8 kD. Molecular sieve chromatography and sodium dodecyl sulfate (SDS)-gel electrophoresis suggest that the native conformation of the protein is likely to be a tetramer of 156 kD. NH2-terminal amino acid sequence analysis revealed 83% homology in the first 18 residues and about 56% in the first 39 residues with glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of eukaryotic or bacterial origin. This streptococcal surface GAPDH (SDH) exhibits a dose-dependent dehydrogenase activity on glyceraldehyde-3-phosphate in the presence of beta-nicotinamide adenine dinucleotide both in its pure form and on the streptococcal surface. Its sensitivity to trypsin on whole organism and its inability to be removed with 2 M NaCl or 2% SDS support its surface location and tight attachment to the streptococcal cell. Affinity-purified antibodies to SDH detected the presence of this protein on the surface of all M serotypes of group A streptococcal tested. Purified SDH was found to bind to fibronectin, lysozyme, as well as the cytoskeletal proteins myosin and actin. The binding activity to myosin was found to be localized to the globular heavy meromyosin domain. SDH did not bind to streptococcal M protein, tropomyosin, or the coiled-coil domain of myosin. The multiple binding capacity of the SDH in conjunction with its GAPDH activity may play a role in the colonization, internalization, and the subsequent proliferation of group A streptococci.
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PMID:A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity. 150 Aug 54

Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.2.12) (GAPDH) is a multifunctional protein that associates with the cytoplasmic face of intact human erythrocyte membranes. This association has been postulated to be critically dependent on the interaction of GAPDH with the highly acidic NH2-terminal domain of the principal integral membrane protein of the erythrocyte plasma membrane, the band 3 anion exchanger (AE1). This domain is not conserved in murine erythrocyte AE1 and is fully deleted in the alternatively spliced AE1 isoform that is expressed in the kidney. The lack of conservation of this domain has been proposed to explain the reported absence of GAPDH association with rodent erythrocyte membranes. To determine whether GAPDH could be associated with AE1 proteins in rodent cell membranes, specific rabbit antibodies to peptide sequences of rat GAPDH and mouse AE1 were used to immunolocalize these proteins in sequential semithin sections of rat erythrocytes and kidney medulla. In rat erythrocytes, GAPDH immunoreactivity was predominantly membrane associated and colocalized with AE1. In the kidney medulla, GAPDH was concentrated in the basolateral membrane of type A intercalated cells, where it colocalized with the alternatively spliced kidney form of AE1. GAPDH immunoreactivity was not detected in the plasma membrane of any other cell type in the kidney, indicating its predominant association with AE1-rich membranes. If this membrane interaction occurs via AE1 binding, then GAPDH must have binding sites in addition to those previously described for such binding in human AE1.
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PMID:Colocalization of GAPDH and band 3 (AE1) proteins in rat erythrocytes and kidney intercalated cell membranes. 159 Apr 32

A 37 kDa protein in extracts of bovine aorta and equine platelets was observed on SDS-polyacrylamide gel electrophoretograms to react with polyclonal and monoclonal antibodies to rabbit skeletal troponin-T (TnT) by immunoblotting. Following purification by precipitation at pH 4.6 and several ion-exchange chromatographic steps, it has been identified as glyceraldehyde-3-phosphate dehydrogenase (G3PD) by amino acid analyses and NH2-terminal sequencing. By ELISA, the anti-troponin-T monoclonal antibody reacted with rabbit skeletal G3PD appreciably but 120-fold less specifically than with TnT. A cyanogen bromide fragment (CB2) of TnT (residues 71-151) reacted with the monoclonal antibody nearly as well as intact TnT. This cross-reactivity between G3PD and TnT can be ascribed to a weak homology in the amino acid sequences of the two proteins between residues 72-80 of TnT and residues 157-165 of G3PD. Other regions of limited sequence similarity in the two proteins are also present. We conclude that the identification of diffuse cytoplasmic indirect immunofluorescent staining observed with a monoclonal anti-TnT antibody in chicken gizzard muscle is probably attributable to cross-reactivity with G3PD.
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PMID:Troponin-T and glyceraldehyde-3-phosphate dehydrogenase share a common antigenic determinant. 243 39

Using a cloned cDNA (pGAP30) the nucleotide sequence for chicken glyceraldehyde-3-phosphate dehydrogenase mRNA has been determined. The cDNA insert contains 1051 nucleotides representing the amino acid coding sequence, with the exception of 49 NH2-terminal amino acids, and includes the entire 3'-noncoding region. Sequence information on the missing 5' terminus of the mRNA, not represented in the clone pGAP30, was obtained by extension of the cDNA using an 85-nucleotide-long internal fragment as a primer. Thus the sequence of 310 amino acids of chicken glyceraldehyde-3-phosphate dehydrogenase representing 93% of the complete primary structure could be derived. The coding portion exhibits non-random utilization of synonymous codons with a strong bias for codons with G or C at the third position. The non-coding region contains several octanucleotides which are repeated and shows a potentially stable stem-and-loop structure located towards the end of the mRNA. Hypothetical functional implications of the putative secondary structure are discussed.
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PMID:Sequence analysis of the cloned mRNA coding for glyceraldehyde-3-phosphate dehydrogenase from chicken heart muscle. 683 36

The avian erythrocyte anion exchange protein (band 3), after labeling with [3H2]4,4'-diisothiocyanodihydrostilbene-2, 2'-disulfonic acid appears as a doublet of polypeptide chains with apparent Mr = 105,000 and 100,000 by sodium dodecyl sulfate gel electrophoresis. The structures of the two species are almost identical as determined by partial proteolysis. The copy number of band 3 molecules per chicken erythrocyte was determined to be 800,000 by quantitating the amount of [3H2]4,4'-diisothiocyanodihydrostilbene-2,2'-disulfonic acid covalently bound to the cell surface. A comparison of human and chicken band 3 has revealed differences in their structure. Chicken band 3 differs from the human polypeptide in isoelectric point and proteolytic patterns. Antisera raised against human and chicken band 3 do not cross-react, implying that the two sera do not recognize any common antigenic determinants. There is a 6.5-fold lower activity per cell in the rate of phosphate exchange in the chicken erythrocyte which can be entirely explained by the 1.5-fold decrease in copy number per cell and the increased size of the chicken erythrocyte. This would suggest that there is no difference in the enzyme turnover number between chicken and human band 3. A major functional difference resulting from the structural differences is the inability to bind glyceraldehyde-3-phosphate dehydrogenase, a function associated with the NH2 terminus of human band 3.
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PMID:Characterization of the chicken erythrocyte anion exchange protein. 687 95

An immunoglobulin M kappa-chain murine monoclonal antibody (CAB) reacted in a Western blot (immunoblot) with approximately 30 polypeptides from a whole-cell lysate of several American and European Borrelia burgdorferi strains. The reactive antigen with the highest M(r) was measured at 93 kDa (p93) and had an NH2-terminal sequence identical to the one previously reported for this antigen. The lowest reactive antigen had an M(r) of 16,000. All antigens recognized by CAB had isoelectric points within a narrow acidic range, between 5.4 and 6.2. Thus, the objective of this study was to determine whether the broad reactivity of CAB could be due to degradation of the antigen with the highest M(r), since such spontaneous degradation of p93 has already been reported, and to determine whether CAB could recognize shared epitopes in different antigens. Treatment of B. burgdorferi with protease inhibitors did not result in changes in CAB reactivity, indicating that if such degradation existed, it was most likely not due to the action of endogenous proteases. Likewise, protease treatment of intact organisms and recovery of the antigens in the insoluble fraction of a Triton X-114 partition indicated that they were internal and thus less likely to be degraded by experimental procedures. Amino-terminal sequences of other reactive polypeptides showed one approximately 72-kDa polypeptide to be identical to the DnaK homolog of B. burgdorferi. Two other antigens at approximately 49 and 47 kDa were blocked to Edman degradation. Finally, one sequenced polypeptide with a molecular mass of approximately 38.5 kDa had a strong identity with glyceraldehyde-3-phosphate dehydrogenase of other bacteria and vertebrates. Thus, while it cannot be ruled out that some of the CAB reactivity may be due to fragmentation of p93, there is strong evidence to indicate the presence of a shared epitope in at least three, possibly five, unrelated antigens of B. burgdorferi. A linear epitope within amino acid residues 357 to 371 of p93 was identified. Evidence is presented for a discontinuous epitope in the carboxy-terminal region of the DnaK homolog, which bears strong amino acid identity with the p93 epitope. The conserved amino acid sequences necessary for these shared epitopes indicate possible genetic and/or functional relatedness among these various antigens.
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PMID:Epitopes shared by unrelated antigens of Borrelia burgdorferi. 750 14

Ubiquitin-carrier proteins (E2s, ubiquitin-conjugating enzymes, UBCs) participate in proteolysis by catalyzing transfer of activated ubiquitin to the protein substrates, which are bound to specific ubiquitin-protein ligases (E3s). Yeast UBC2 (RAD6) and the mammalian E2(14kDa) bind to the ligase that recognizes and is involved in the degradation of certain free amino-terminal substrates ("N-end rule" substrates). As such proteins are rather scarce, the role of these E2s in general proteolysis is probably limited. Here, we report the purification and characterization of a novel 18-kDa species of E2 from rabbit reticulocytes. Unlike most members of the E2 family, this enzyme does not adsorb to anion exchange resin in neutral pH, and it is purified from the unadsorbed material (Fraction 1). Thus, it is designated E2-F1. Like all members of the E2 family, it generates a thiol ester with ubiquitin that serves as an intermediate in the conjugation reaction. Sequence analysis revealed a significant homology to many known species of E2s. The enzyme generates multiply ubiquitinated proteins in the presence of an E3 that has not been characterized yet. Most importantly, the ubiquitination via this E2 leads to the degradation of certain non-"N-end rule" substrates such as glyceraldehyde-3-phosphate dehydrogenase (Val at the NH2 terminus) and to the ubiquitination and degradation of certain N-alpha-acetylated proteins such as histone H2A, actin, and alpha-crystallin. The enzyme is also involved in the conjugation and degradation of the tumor suppressor protein p53.
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PMID:Purification and characterization of a novel species of ubiquitin-carrier protein, E2, that is involved in degradation of non-"N-end rule" protein substrates. 814 44

Evidence of in vivo oxidant-induced injury in inflammatory bowel disease (IBD) is largely indirect. Colon epithelial crypt cells (CEC) from paired specimens of histologically normal and inflamed bowel from IBD patients with active disease were examined for altered protein thiol redox status as an indicator of oxidative damage. When CEC preparations from 22 IBD patients were labeled with the reduced-thiol-specific probe [14C]-iodoacetamide (IAM), there was decreased labeling of a number of proteins indicating oxidation of thiol groups in CEC from inflamed mucosa compared to paired normal mucosa, especially the loss of thiol labeling of a 37-kD protein which was almost completely lost. The loss of reduced protein thiol status for the 37-kD band was paralleled by loss of epithelial cell glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.2.1.12) enzyme activity, an enzyme known to contain an essential reduced cysteine (Cys149) at the active site. The identity of the 37-kD protein as GADPH monomer was confirmed by NH2-terminal amino acid sequence analysis. To examine whether this type of in vivo injury could be attributed to biologically relevant oxidants produced by inflammatory cells, CEC prepared from normal mucosa were exposed to H2O2, OCl-, nitric oxide (NO), and a model chloramine molecule chloramine T (ChT) in vitro. Dose-dependent loss of IAM labeling and GAPDH enzyme activity was observed. The efficacy (IC50) against IAM labeling was OCl- >> ChT > H2O2 > NO (52 +/- 3, 250 +/- 17, 420 +/- 12, 779 +/- 120 microM oxidant) and OCl- >> ChT > NO > H2O2 (89 +/- 17, 256 +/- 11, 407 +/- 105, 457 +/- 75 microM oxidant), respectively, for GAPDH enzyme activity. This study provides direct evidence of in vivo oxidant injury in CEC from inflamed mucosa of IBD patients. Oxidation and inhibition of essential protein function by inflammatory cells is a potential mechanism of tissue injury that may contribute to the pathogenesis of the disease and supports the exploration of compounds with antioxidant activity as new therapies for IBD.
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PMID:Evidence of oxidant-induced injury to epithelial cells during inflammatory bowel disease. 869 Jul 84


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