Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The amino acid sequences of the myoglobins of two rodents, the casiragua and the house mouse, have been determined. The myoglobin of casiragua differs from that of viscacha (another hystricomorph) at 6 positions. Mouse myoglobin differs from that of mole-rat (another myomorph) at 17 positions, whereas casiragua and mouse differ at 22 positions. Mouse myoglobin possesses several features unique among all known myoglobins (Gly 31, Cys 66, Thr 74 and Glu 113) and one substitution unique among known mammalian myoglobins (Glu 53).
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PMID:The myoglobin of rodents Proechimys guairae (casiragua) and Mus musculus (house mouse). 404 6

The N-terminal formic acid fragment (FA1) of the N-[3H]ethylmaleimide-labeled and carboxymethylated bovine mitochondrial phosphate transport protein (PTPN*CM) has been purified and completely sequenced: NH2-Ala-Val-Glu-Glu-Gln-Tyr-Ser-Cys-Asp-Tyr10-Gly-Ser-Gly-Arg-Phe- Phe-Ile-Leu-Cys- Gly20-Leu-Gly-Gly-Ile-Ile-Ser-Cys-Gly-Thr-Thr30-His-Thr -Ala-Leu-Val-Pro-Leu-Asp- -Leu-Val40-Lys-Cys(N-[3H]ethylmaleimide)-Arg-Met-Gln-Val-Asp- COOH. By thermolysin digestion of FA1 and high-performance liquid chromatography isolation of the radioactive subfragment Leu39-Arg43, the sole N-ethylmaleimide-binding residue has been identified as Cys42. FA1 contains a high mole percentage of cysteine (8.5%) and shows silver staining anomaly. Its sequence reveals significant homology in the triplicated gene regions (Pro27,132,229) of the mitochondrial ADP/ATP carrier from beef heart and Neurospora crassa. The hydropathic profile suggests that FA1 contains a transmembrane segment (Phe15-Val40) with only one basic (His31) and one acidic (Asp38) residue. The presence of the phosphate transport protein gene among nuclear genes is suggested from a lack of significant homology between the reverse-translated FA1 (mitochondrial codons) and the bovine mitochondrial genome. The inhibitory action of N-ethylmaleimide on the phosphate transport mechanism is discussed.
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PMID:Sequence of the N-terminal formic acid fragment and location of the N-ethylmaleimide-binding site of the phosphate transport protein from beef heart mitochondria. 406 97

The thiopeptins are a new group of sulfur-containing peptide antibiotics produced by Streptomyces tateyamensis. The antibiotic consists of a major component (designated as thiopeptin B) and four minor ones (thiopeptins A(1) to A(4)). These components were isolated by solvent extraction from mycelium followed by chromatography on silica gel with various ratios of chloroform and methanol as elution solvents. Acid hydrolysis of each of the thiopeptin components yielded 1 mole of valine, 1 of threonine, 1 of cysteine, and 2 of alanine as amino acids. Each component of the thiopeptin A group has chemical and biological properties closely similar to those of thiopeptin B, but detailed characterization has established that thiopeptins A(1), A(3), and A(4) are new antibiotics. We could not obtain accurate data for determination of the uniqueness of A(2) because of insufficient sample. Thiopeptin has strong antibacterial activity against gram-positive bacteria and Mycoplasma, and exhibits no cross-resistance to major human-use antibiotics.
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PMID:Thiopeptin, a new feed additive antibiotic: microbiological and chemical studies. 504 67

Mucopeptides isolated from Streptococcus bovis cell walls were found to be composed of alanine, glutamic acid, lysine, and threonine in a mole ratio of 3:1:1:1. A dipeptide, N(epsilon)-lysylthreonine, was isolated from S. bovis mucopeptide by ion-exchange chromatography. This finding suggests that threonine is associated with the bridge which cross-links adjacent tetrapeptides by connecting the epsilon-amino group of lysine of one tetrapeptide to the carboxyl group of d-alanine of another to form the mucopeptide matrix.
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PMID:Chemical studies on the structure of mucopeptide isolated from Streptococcus bovis. 580 3

Pyruvate, Pi dikinase in extracts of chloroplasts from mesophyll cells of Zea mays is inactivated by incubation with ADP plus ATP. This inactivation was associated with phosphorylation of a threonine residue on a 100 kDa polypeptide, the major polypeptide of the mesophyll chloroplast stroma, which was identified as the subunit of pyruvate, Pi dikinase. The phosphate originated from the beta-position of ADP as indicated by the labelling of the enzyme during inactivation in the presence of [beta-32P]ADP. During inactivation of the enzyme up to 1 mole of phosphate was incorporated per mole of pyruvate, Pi dikinase subunit inactivated. 32P label was lost from the protein during the Pi-dependent reactivation of pyruvate, Pi dikinase.
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PMID:Regulation of C4 photosynthesis: regulation of pyruvate, Pi dikinase by ADP-dependent phosphorylation and dephosphorylation. 631 Dec 12

The major gamma-carboxyglutamic acid-containing protein of rabbit cortical bone isolated and purified from near-neutral (pH 7.5) EDTA-extracts by DEAE-cellulose and Sephadex G 75 column chromatography had a molecular weight of about 5600 based on integral amino-acid composition; this was confirmed by high-performance liquid chromatography. The purified protein had high glutamic acid and aspartic-acid contents, two to three residues of gamma-carboxyglutamic acid per molecule and zero levels of serine, threonine, methionine, histidine and tryptophan. Equilibrium dialysis indicated that the protein has a weak affinity for calcium ions with a formation constant of 1515 M-1 at I 0.15, pH 7.5, 25 degrees C with a binding capacity of 2 mol calcium per mole protein.
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PMID:The small molecular weight, gamma-carboxyglutamic acid-containing protein of rabbit bone tissue. 659 60

Cutinase I and cutinase II, two extracellular enzymes produced by Fusarium solani pisi, were shown to be glycoproteins containing 4.3% and 5.1% carbohydrates, respectively. Upon treatment with alkali both enzymes generated chromophores which absorbed at 241 nm. Treatment of both proteins with alkaline NaB3H4 gave labeled protein and labeled monosaccharides. Hydrolysis of the labeled protein followed by chromatographic and enzymatic analyses of the products showed that alanine, 2-aminobutyrate, phenylalanine, tyrosine and L-gulonic acid accounted for nearly all of the 3H contained in the protein. The four labeled amino acids were shown to be 1:1 mixture of D and L isomers and 3H was nearly equally distributed between alpha and beta positions in each amino acid. The N-terminal amino group of cutinase I did not react with either phenylisothiocyanate of dansyl chloride. This amino group was suggested to be in amide linkage with glucuronic acid because upon treatment of the protein with neutral NaB3H4, gulonic acid attached to the protein became labeled and only gulonic acid was labeled when the protein was deglycosylated with HF prior to alkaline NaB3H4 treatment. Furthermore, N-gulonyglycine was isolated from the pronase digest of the labeled protein. Chromatographic identification and quantification of the labeled carbohydrates released from cutinase I by alkaline NaB3H4 showed that one mole of cutinase I has one mole each of mannose, arabinose, N-acetylglucosamine, and glucuronic acid O-glycosidically linked to serine, threonine, beta-hydroxyphenylalanine, and beta-hydroxytyrosine. In addition, the N-terminal glycine is in amide linkage with glucuronic acid. Since almost identical experimental results were obtained with cutinase II this protein is also suggested to have the same structural features as those suggested above for cutinase I.
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PMID:Structural studies on cutinase, a glycoprotein containing novel amino acids and glucuronic acid amide at the N terminus. 739 18

Hexokinase 1 (HK1) purified from rat brain exhibits protein kinase activity, including autophosphorylation and phosphorylation of other protein substrates. The amino acid specificity of rat brain autophosphorylation was analyzed with monoclonal antibodies directed against phosphotyrosine and by acid hydrolysis of the phosphorylated enzyme. The results show that serine, threonine, and tyrosine residues are phosphorylated after incubation with ATP. The stoichiometry of this phosphorylation was 0.2 mole phosphate per mole hexokinase after 30 min of incubation. Evaluation of freshly isolated HK1 with monoclonal anti-phosphotyrosine antibody indicates that the enzyme is phosphorylated at a basal level in its native state. We concluded that rat brain HK1 is a dual specificity protein kinase that is phosphorylated physiologically.
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PMID:Hexokinase autophosphorylation: identification of a new dual specificity protein kinase. 753 90

In the presence of Ca2+ and calmodulin (CM), purified smooth muscle myosin light chain kinase (MLCKase) was found to undergo autophosphorylation at a rate that was about 200-fold slower than its catalytic activity. Up to 1.7 mol of phosphate were incorporated per mole of kinase. Lower levels of incorporation could be correlated with the presence of an endogenous protein phosphatase which could be inhibited with okadaic acid or Microcystin-LR. The major autophosphorylation site was identified as Thr-863 or Thr-865 and was located on the 24-kDa C-terminal fragment of the kinase. In addition, there was a relatively low and variable contribution of a Ca/CM-independent autophosphorylation at Ser-814 or Ser-815. The initial autophosphorylation rates and maximal incorporation levels were highest at a molar ratio of 2 MLCKase to 1 CM and were inhibited at higher CM levels. This indicated that binding of one molecule of the kinase apoenzyme by a CM-kinase complex was necessary for the reaction to occur. Kinetic analysis of the autophosphorylation reaction was consistent with this interpretation and indicated a second-order intermolecular process that included MLCKase dimerization or oligomerization. In contrast, the low Ca/CM-independent contribution was of intramolecular type since it did not depend on the kinase concentration. The autophosphorylation appeared to be involved in a relatively slow modification of the oligomeric properties of the kinase leading to a 2-4-fold amplification of the kinase catalytic activity which followed its activation by CM. Oligomerization and dimerization of the kinase was independently demonstrated by light scattering measurements.
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PMID:Calmodulin-dependent autophosphorylation of smooth muscle myosin light chain kinase: intermolecular reaction mechanism via dimerization of the kinase and potentiation of the catalytic activity following activation. 754 20

Inhibitor 2 is a heat-stable protein that complexes with the catalytic subunit of type-1 protein phosphatase. The reversible phosphorylation of Thr 72 of the inhibitor in this complex has been shown to regulate phosphatase activity. Here we show that inhibitor 2 can also be phosphorylated on tyrosine residues. Inhibitor 2 was 32P-labeled by the insulin receptor kinase in vitro, in the presence of polylysine. Phosphorylation of inhibitor 2 was accompanied by decreased electrophoretic mobility. Dephosphorylation of inhibitor 2 by tyrosine phosphatase 1B, restored normal electrophoretic mobility. Phosphotyrosine in inhibitor 2 was detected by immunoblotting with antiphosphotyrosine antibodies and phosphoamino acid analysis. In addition, following tryptic digestion, one predominant phosphopeptide was recovered at the anode. The ability of inhibitor 2 to inhibit type-1 phosphatase activity was diminished with increasing phosphorylation up to a stoichiometry of 1 mole phosphate incorporated/mole of inhibitor 2, where inhibitory activity was completely lost. These data demonstrate that inhibitor 2 can be phosphorylated on tyrosine residues by the insulin receptor kinase, resulting in a molecule with decreased ability to inhibit type-1 phosphatase activity.
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PMID:Tyrosine phosphorylation of phosphatase inhibitor 2. 776 77


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