Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Peptidases capable of releasing proline residues from polypeptides are present in the cytoplasmic fraction of rabbit polymorphonuclear granulocytes. This was shown with peptide substrates where proline is present either at the carboxy-terminal or within the polypeptide chain. Lysosomal and plasma membrane enzymes were inactive towards such polypeptides. The proline residue was hydrolyzed at either its amino end or its carboxy end. It is noteworthy that a Pro:Pro bond was cleaved both in the pentapeptide Thr-Lys-Pro-Arg and the dipeptide Pro:Pro.
Mol Cell Biochem 1976 Feb 16
PMID:Proline endopeptidase and exopeptidase activity in polymorphonuclear granulocytes. 0 27

Kinetic studies have been performed on the "family" of aminoacyl synthetases from calf liver. All assays were based on the esterification of amino acids to tRNA. Optimized reaction conditions for each synthetase are reported. Most of the synthetases show hyperbolic kinetics with respect to both amino acid and tRNA concentration, however a few show sigmoidal kinetics with respect to one substrate. Arginine, methionine and proline synthetases show sigmoidal kinetics with respect to mixed tRNA solutions and have Hill coefficients of 1.30, 1.10 and 1.20 respectively. Alanine and isoleucine synthetases show sigmoidal kinetics with respect to amino acid concentration and have Hill coefficients of 1.21 and 1.40 respectively.
Mol Cell Biochem 1977 Aug 19
PMID:Aminoacyl-tRNA synthetases from calf liver: optimized assay conditions and kinetic properties. 2 May 69

Mutants of Pseudomonas aeruginosa PAO deficient in their utilization of DL-valine have been found to have lost their capacity to utilize DL-alanine and L-proline. Use of conjugal and transductional mediated gene transfers have established the chromosomal location of this gene and also its pleotropic function in the induction of the D-amino acid oxidase, involved in the oxidative utilization of DL-valine, DL-alanine and L-proline. These point mutations are clustered in a single locus designated as Val D and mapped around the 19th minute on the chromosome.
Mol Gen Genet 1978 Aug 04
PMID:Mapping of the locus involved in the catabolic oxidation of D-amino acids in Pseudomonas aeruginosa PAO. 3 39

Histochemical observations were made of the activities of nucleosidephosphatases splitting ATP, ADP, IDP, and AMP and exopeptidases splitting l-alanine, l-leucine and l-glycyl-proline in the spleen sinuses of man, mouse, rat, hamster, and rabbit. Of the exopeptidases, only glycylprolyl-naphthylamidase could be proved histochemically, and that only in man and rat. Nucleosidephosphatases showed only traces of activity except in the rabbit where there was highly active AMP-ase, the others being moderately active.
Virchows Arch B Cell Pathol Incl Mol Pathol 1979 Dec
PMID:Comments on spleen sinus enzyme equipment. A histochemical study. 4 57

Although the main characteristics of the parent virginiamycin S conformation i.e. a bend of type VI (Lewis, P.N., Momamy, F.A. and Scheraga, H.A. (1973) Biochim. Biophys. Acta 303, 211--229) formed by the Pro-N-MePhe-X-PhGly sequence is still present in patricin A, the substitution of X = pipecolic acid by proline in the latter results in a destabilization of the tertiary structure of the depsipeptide, since two isomeric states of a peptidic bond appear in C2HC13 solution. Addition of +/- 30% (v:v) (C2H3)2SO totally shifts this equilibrium in favor of the major parent isomer. These results completely fit with what is known up to now on the occurrence and structure of turns (Chou and Fasman (1977) J. Mol. Biol. 115,135--175).
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PMID:Solution conformation of virginiamycin S. III. Patricin A: A further model for cooperative effects of the Pro ring conformation and backbone. 11 Mar 55

Mutants altered in carbon catabolite regulation have been isolated by selecting for mutants of the areA217 strain capable of using acetamide as the sole nitrogen source in the presence of sucrose. In addition to creA mutants described previously be Arst and Cove, strains with mutations in two new genes, creB and cre C, have been found. The creB and creC mutants grow poorly on some sole carbon sources and have low levels of some enzymes of carbon catabolism e.g. beta-galactosidase and D-quinate dehydrogenase. The creB and creC mutants are hypersensitive to fluoroacetate, fluoroacetamide and allyl alcohol in the presence of glucose or sucrose but not glycerol; and the enzymes, acetamidase and alcohol dehydrogenase, are less sensitive to carbon catabolite repression than the wild-type strain. Extracellular protease and alpha-glucosidase enzyme activities are elevated in creB and creC mutants, while L-proline and L-glutamate uptake capacities are lower in both the presence and absence of glucose. Interactions between creA, B and C mutations have been investigated in double mutants, and the dominance properties of creB and creC mutants determined. The results indicate that the creB and creC genes may have a regulatory role in the control of carbon catabolism.
Mol Gen Genet 1977 Jan 18
PMID:Pleiotropic mutants of Aspergillus nidulans altered in carbon metabolism. 32 Apr 55

The prn gene cluster involved in L-proline catabolism in Aspergillus nidulans, has the gene order prnA-prnD-regulatory region-prnB-prnC. prnB, prnD, and prnC specify proline permease, proline oxidase, and delta1-pyrroline-5-carboxylate (P5C) dehydrogenase, respectively. prnA is probably a positive regulatory gene whose product is necessary for expression of the prn activities. Proline induces proline permease and P5C dehydrogenase in prnD- mutants which lack proline oxidase, showing that proline does not have to be converted to P5C to act as inducer. Deletion mutations extending from within prnD to within prnB result in considerably reduced expression of prnC, whereas a prnD- prnB- double mutant shows normal prnC expression. This strongly suggests that the deletion mutations eliminate a promotor/initiator site for transcription of a dicistronic messenger for prnB and prnC. The fact that the deletions do not eliminate prnC expression altogether indicates that at least one other species of prnC transcript (monocistronic, tricistronic, or tetracistronic) can be made.
Mol Gen Genet 1978 Jul 06
PMID:Reduced expression of a distal gene of the prn gene cluster in deletion mutants of Aspergillus nidulans: genetic evidence for a dicistronic messenger in an eukaryote. 35 39

The incorporation of labeled amino acids and glucosamine into LH and FSH by cultured rat anterior pituitary cells and anterior pituitary homogenates is reported. There was a significant augmentation in this incorporation by cells after 6 days of culture in the presence of GnRH. Tritiated LH and FSH were found in the cell extracts as well as in the media by the method of immunoprecipitation. An increase of approximately 7--13-fold in the release of LH and FSH into the cell incubation medium was observed in the presence of GnRH (3 ng/ml). The rate of incorporation of [3H]proline was higher than that of [3H]glucosamine into LH and FSH. At the same time a higher incorporation of labeled amino acids was observed in the case of FSH than with LH. Cycloheximide inhibited completely the incorporation of labeled proline but the inhibition was partial for the incorporation of labeled glucosamine. Freshly dispersed cells, short-time cultures maintained for 20 h and pituitary homogenates also incorporated labeled amino acids into LH and FSH, but GnRH had no effect on this incorporation. Pituitary homogenates also incorporated [3H]glucosamine into LH and FSH with an optimal incorporation after 30 min of incubation. Three different concentrations of GnRH had no effect on the incorporation of [3H]proline by homogenates. Cycloheximide and puromycin inhibited this incorporation completely.
Mol Cell Endocrinol 1978 Oct
PMID:Biosynthesis of gonadotropins by rat pituitary cells in culture and in pituitary homogenates: effect of gonadotropin-releasing hormone. 36 88

Somatic cell hybrids between mouse and human cell lines have been used to identify the specific chromosome that governs the synthesis of type I procollagen. Fourteen hybrid clones and subclones were derived independently from crosses between mouse parents [LM (thymidine kinase-negative) or A9 (hypoxanthine phosphoribosyltransferase-negative)] and human cells (human diploid lung fibroblasts WI-38 or diploid skin fibroblasts GM5, GM17, and GM9). The cultures were labeled with [(3)H]proline in modified Eagle's medium without serum. Radioactive procollagens were purified from the medium by the method of Church et al. [(1974) J. Mol. Biol. 86, 785-799]. DEAE-cellulose chromatography was used to separate collagen and type I and type III procollagen. Human type I procollagen was assayed by double immunodiffusion analysis with type I procollagen antibodies prepared by immunizing rabbits with purified human type I procollagen. These analyses combined with karyology and isozyme analyses of each hybrid line have produced evidence for the assignment of the gene for human type I procollagen to chromosome 17. A human microcell-mouse hybrid cell line containing only human chromosome 17 was positive for human type I procollagen, lending further support to the assignment of the human type I procollagen gene to chromosome 17. Finally, by using a hybrid line containing only the long arm of human chromosome 17 translocated onto a mouse chromosome, the type I procollagen gene can be assigned more specifically to the long arm of chromosome 17.
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PMID:Genetics of the connective tissue proteins: assignment of the gene for human type I procollagen to chromosome 17 by analysis of cell hybrids and microcell hybrids. 41 88

Cytoplasmic and mitochondrial isozymes of NADP+-dependent isocitrate dehydrogenase were purified from kidney and heart tissue of an inbred strain of mice. The cytoplasmic isozyme was purified from kidney of DBA/2J mice by means of a four-step procedure which included affinity chromatography with an 8-(6-aminohexyl)-amino-NADP+-Sepharose column. The heart mitochondrial isozyme of DBA/2J mice was purified by a two-step procedure involving the use of 8-(6-aminohexyl)-amino-AMP-Sepharose and 8-(6-aminohexyl)-amino-NADP+-Sepharose columns. The specific activity of the homogeneous cytoplasmic and mitochondrial isozymes was 40 units/mg and 45 units/mg, respectively. Native and subunit molecular weights of these two isozymes were determined by chromatography on Sephadex G-100, G-150 and G-200 Superfine and polyacrylamide gel electrophoresis. Both isozymes were found to be dimers with the subunit molecular weight of approximately 35,000. The sedimentation coefficients were determined to be 5.9 and 6.1 for the mitochondrial and cytoplasmic isozyme, respectively. The amino acid compositions of these two isozymes revealed distinct differences in arginine and proline contents. A modified procedure regarding the use of affinity columns for the purification of the weakly bound enzymes is also discussed.
Mol Cell Biochem 1979 Feb 09
PMID:Purification and structural properties of isozymes of isocitrate dehydrogenase from the mouse. 48 28


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