Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: DrugBank:EXPT00572 (Asn)
 11,732 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The NADP-specific glutamate dehydrogenase (EC 1.4.1.4) of Neurospora crassa is inhibited by reaction with 1,2-cyclohexanedione which binds to arginine residues. With the 14C-labeled reagent, a peptide was isolated with the sequence: Gly-Gly-Leu-Arg-Leu-His-Pro-Ser-Val-Asn-Leu, corresponding to residues 78 through 88 in the protein. The arginine, residue 81, was present as N7,N8-(1,2-dihydroxycyclohex-1,2-ylene)-arginyl (or DHCH-arginine). Present evidence indicates that this arginine residue resides at or near the nicotinamide binding domain of the enzyme. Similar sequences are present in the bovine liver enzyme (EC 1.4.1.3) and the NAD-specific glutamate dehydrogenase of Neurospora (EC 1.4.1.2).
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PMID:Identification of a functional arginine residue involved in coenzyme binding by the NADP-specific glutamate dehydrogenase of Neurospora. 0 4

A highly potent heart stimulant, anthopleurin A, from Anthopleura xanthogrammica was shown to exist as a single polypeptide chain consisting of 49 amino acid residues. The sequence of the peptide was shown to be: Gly-Val-Ser-Cys-Leu-Cys-Asp-Ser-Asp-Gly-Pro-Ser-Val-Arg-Gly-Asn-Thr-Leu-Ser-Gly-Thr-Leu-Trp-Leu-Tyr-Pro-Ser-Gly-Cys-Pro-Ser-Gly-Trp-His-Asn-Cys-Lys-Ala-His-Gly-Pro-Thr-Ile-Gly-Trp-Cys-Cys-Lys-Gln as judged by Edman degradation of the carboxymethylcysteine derivative and the tryptic peptides obtained from the derivative. Although six carboxymethylcysteine residues were present in the polypeptide, no cysteine residues were detectable in the native protein, indicating that there are three cystine residues in anthopleurin A.
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PMID:Amino acid sequence of the Anthopleura xanthogrammica heart stimulant, anthopleurin A. 1 6

Glycopeptides containing mainly four amino acid residues in the sequence Asn-Leu-Thr-Ser, with small amounts of additional amino acid residues, were isolated from enzymic hydrolysates of hen's-egg albumin. Heterogeneity of the carbohydrate moiety was confirmed. Acid-base titrations showed that the alpha-amino group has a pKa value of 6.43 at 25 degrees C. The standard free engery and entropy changes associated with the ionization at 25 degrees C were 37.2kJ-mol-1 and -0.014kJ-mol-1- K-1 respectively. The complications arising in the interpretation of titration curves of the glycopeptides, which are heterogeneous with respect to the peptide chain, were considered and discussed in the light of the earlier suggestion that the titration curve of the glycopeptide might be interpreted as being due in part to a structure in which the hydroxyl group of the threonine residue is hydrogen-bonded to the beta-aspartamido oxygen atom [Neuberger & Marshall (1968) in Symposium on Foods - Carbohydrates and their Roles (Schultz, H.W., Cain, R.F. & Wrolstad, R.W., eds.), pp. 115-132, Avi Publishing Co., Westport, CT]. It is concluded that either the glycopeptides do not contain a hydrogen bond of that type, or, if they do, that it cannot be recognized by acid-base-titration studies.
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PMID:Acid dissociation constants of glycopeptides. 1 94

Serial culture of Rhodospirillum rubrum with 2% CO2 in H2 as the exclusive carbon source resulted in a rather large fraction of the soluble protein (greater than 40%) being comprised of ribulosebisphosphate carboxylase (about sixfold higher than the highest value previously reported). Isolation of the enzyme from these cells revealed that it has physical and kinetic properties similar to those previously described for the enzyme derived from cells grown on butyrate. Notably, the small subunit (which is a constituent of the carboxylase from eucaryotes and most procaryotes) was absent in the enzyme from autotrophically grown R. rubrum. Edman degradation of the purified enzyme revealed that the NH2 terminus is free (in contrast to the catalytic subunit of the carboxylase from eucaryotes) and that the NH2-terminal sequence is Met-Asp-Gln-Ser-Ser-Arg-Tyr-Val-Asn-Leu-Ala-Leu-Lys-Glu-Glu-Asp-Leu-Ile-Ala-Gly-Gly-Glx-His-Val-Leu-. Crystals of the enzyme were readily obtained by dialysis against distilled water.
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PMID:Isolation, characterization, and crystallization of ribulosebisphosphate carboxylase from autotrophically grown Rhodospirillum rubrum. 3 52

Two amino acid sequences from the same regions of guinea pig and bovine myelin basic protein which induce experimental allergic encephalomyelitis in Lewis rats were synthesized. The sequences of these two regions may be defined by residues 69 to 84 of the bovine basic protein. The encephalitogenic sequence from guinea pig basic protein (peptide S49), H-Gly-Ser-Leu-Pro-Gln-Lys-Ala-Gin-Arg-Pro-Gin-Asp-Glu-Asn-OH, is a much more potent encephalitogen than that of H-Gly-Ser-Leu-Pro-Gln-Lys-Ala-Gln-Gly-His-Arg-Pro-Gln-Asp-Glu-Asn-OH (peptide S8) found in the bovine protein. The primary structures of the two determinants are similar; however, a Gly-His deletion from the guinea pig sequence is noted. Study of the encephalitogenicity of peptide S49, peptide S8, and the parent proteins suggests that the difference in the encephalitogenic potency of the parent proteins in Lewis rats is due to a natural modification in the primary structure of their respective encephalitogenic determinants.
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PMID:Experimental allergic encephalomyelitis in Lewis rats: chemical synthesis of disease-inducing determinant. 6 39

A glycoprotein has been isolated from the colonic lavages of healthy individuals that is immunologically equivalent to carcinoembryonic antigen purified from tumor tissue. The NH2-terminal sequence of the glycoprotein from normal colon lavages is Lys-Leu-Thr-lle-Glu-Ser-Thr-Pro-Phe-(Asn)-Val-Ala-Glu-Gly-Lys-Glu-Val-(Leu,lle)-(Leu,lle)-(Leu,lle)-Val-(His,Arg?)-?-(Leu,lle). This is homologous to the NH2-terminal sequence of 23 of the first 24 amino acids of carcinoembryonic antigen isolated from tumor tissue.
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PMID:Amino-terminal sequence of a carcinoembryonic antigen-like glycoprotein isolated from the colonic lavages of healthy individuals. 7 56

The complete primary structure of the platelet-specific protein human beta-thromboglobulin has been determined. beta-Thromboglobulin consists of identical subunits of 81 amino acids, each with a molecular weight of 8851. The amino acid sequence of the beta-thromboglobulin subunit is: Gly-Lys-Glu-Glu-Ser-Leu-Asp-Ser-Asp-Leu-Tyr-Ala-Glu-Leu-Arg-Cys-Met-Cys-Ile-Lys-Thr-Thr-Ser-Gly-Ile-His-Pro-Lys-Asn-Ile-Gln-Ser-Leu-Glu-Val-Ile-Gly-Lys-Gly-Thr-His-Cys-Asn-Gln-Val-Glu-Val-Ile-Ala-Thr-Leu-Lys-Asp-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Pro-Asp-Ala-Pro-Arg-Ile-Lys-Lys-Ile-Val-Gln-Lys-Lys-Leu-Ala-Gly-Asp-Glu-Ser-Ala-Asp. Disulfide bridge-18 to half-cystine-58. The amino acid sequence of beta-thromboglobulin shows a marked homology with that of platelet factor 4. When the sequences are aligned for maximum homology, 42 of the 81 residues of beta-thromboglobulin are identical with those of platelet factor 4, including the position of the four half-cystines.
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PMID:Complete covalent structure of human beta-thromboglobulin. 7 77

The use of derived and synthetic peptides has contributed greatly to our understanding of encephalitogenic determinants in the basic protein molecule. Peptides derived from BP by use of trypsin, pepsin, cathepsin D (brain and liver) and BNPS-skatole have proven most useful. Synthetic peptides have served to define the disease-inducing determinants with precision. A remarkable feature of these studies is that different antigenic determinants serve as encephalitogenic sites in different species. The encephalitogenic sites comprise short peptide domains of the BP polypeptide chain, only 8 residues (rat), 9 residues (guinea pig), and 10 residues (rabbit) in length. In view of the requirement for both haptenic and carrier specificity of an immunogenic molecule, it is impressive that these peptides themselves elicit the autoimmune disease, EAE. While less active than BP on a molar basis, they are nonetheless potent encephalitogens, producing clinical signs in rats and guinea pigs at less than 1 microgram dose. The data indicate that for most animal species (guinea pig, rat, monkey) there appears to be only one major encephalitogenic determinant, an unusual finding in view of the number of antigenic determinants for cell-mediated immunity existing in the BP molecule. Possibly a combination of genetic and anatomical factors may account for this phenomenon. A relationship may exist between multiple sclerosis and EAE as shown by peptide studies; lymphocytes are found in MS patients during exacerbation sensitized to the same region of BP active in the monkey. The major encephalitogenic sites are: Guinea Pig (9) Phe-Ser-Trp-Gly-Ala-Glu-Gly-Gln-Lys(Arg); Rabbit (10) Thr-Thr-His-Tyr-Gly-Ser-Leu-Pro-Gln-Lys; Rat (8) Ser-Gln-Arg-Ser-Gln-Asp-Glu-Asn; Monkey (14) Phe-Lys-Leu-Gly-Gly-Arg-Asp-Ser-Arg-Ser-Gly-Ser-Pro-Hser.
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PMID:Peptides and autoimmune disease. 8 85

Nine synthetic peptides containing sequences in the region of a threonine residue at position 98 of bovine basic myelin protein were prepared by the Merrifield solid-phase method and tested for their ability to be glycosylated with [14C]uridinediphospho-N-acetylgalactosamine and a crude detergent-solubilized preparation of uridinediphospho-N-acetylgalactosamine:mucin polypeptide N-acetylgalactosaminyltransferase obtained from porcine submaxillary glands. The tetrapeptide Thr-Pro-Pro-Pro and all larger peptides containing this sequence were glycosylated. The glycosylation was greater for peptides containing residues N-terminal to the Thr-Pro-Pro-Pro. Under the conditions used, the peptide Val-Thr-Pro-Arg-Thr-Pro-Pro-Pro was glycoslyated twice as much as bovine basic myelin protein. Thr-Pro and Thr-Pro-Pro, as well as 10 other synthetic peptides which did not contain the Thr-Pro-Pro-Pro sequence, were not glycosylated. Treatment of the glycopeptide of Phe-Lys-Asn-Leu-Val-Thr-Pro-Arg-Thr-Pro-Pro-Pro-Ser with an alpha-N-acetylgalactosaminidase released N-acetylgalactosamine from the peptide, indicating that the hexosamine was covalently bonded to the peptide in an alpha linkage.
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PMID:Enzymic O-glycosylation of synthetic peptides from sequences in basic myelin protein. 9 May 21

Methylamine reacts with the plasma protease inhibitor, alpha 2-macroglobulin, to form an irreversible, covalent modification. Quantitation of the reaction indicates 3.9 +/- (SD) 0.4 reactive sites per native tetrameric protein (Mr = 725,000) or one site per subunit. The reaction is selective and specific in that only 1 or 2 labeled peptides are observed on radioautography of peptide maps derived from [14C]methylamine-treated alpha 2-macroglobulin. A single chymotryptic peptide was isolated in 56% overall yield from the labeled protein. The peptide sequence by Edman degradation was found to be Gly-Cys-Gly-Glu-X-Asn-Met-(Val, Leu), in which X was the only radiolabeled phenylthiohydantoin derivative. Amino acid analysis and mass spectral analysis of the derivative suggests that X is gamma-glutamylmethylamide. Because glutamic acid and glutamine residues do not normally react with alkylamines, this work presents presumptive evidence for an alternative activated center in selected proteins.
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PMID:Characterization of alkylamine-sensitive site in alpha 2-macroglobulin. 9 26


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