Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
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Several mouse monoclonal antibodies to carboxypeptidase A (CPA) were prepared and purified, and their interaction with the enzyme was investigated. CPA is a well-characterized zinc-containing exopeptidase exhibiting peptidase as well as esterase activity. The antibodies obtained could be classified as follows: antibodies inhibiting mainly the peptidase activity of the enzyme, antibodies inhibiting mainly its esterase activity, antibodies affecting both activities, and antibodies which bind to the enzyme but have no marked effect on its catalytic properties. Binding constants of approximately 10(6) M-1 were obtained for most of the antibody-enzyme complexes tested. Additional information on the effect of the monoclonal antibodies on the active site of CPA was obtained by determining the change in the circular dichroism spectra of arsanilazotyrosine-248 carboxypeptidase A occurring as a result of the interaction of the enzyme with the antibodies studied. These findings suggest that CPA possesses at least three different specific antigenic sites, and that the active site of the enzyme for its peptidase activity differs from that for its esterase activity, though both sites seem to overlap to a considerable extent.
Mol Immunol 1984 Jan
PMID:Interaction of carboxypeptidase A with monoclonal antibodies. 620 Jul 67

U1 small nuclear RNA (U1 snRNA) is encoded by a large family of genes (30-125 copies/haploid genome) which are transcribed by RNA polymerase II. U1 snRNA is thought to function in gene splicing. Since the U1 genes were found to be greater than 20 kb apart by analyzing genomic phage clones, the chromosomal location of U1 genes in the human genome was determined using Southern filter analysis of DNA isolated from human-rodent somatic cell hybrids and by in situ hybridization. Human DNA digested with PvuII and probed with a U1-specific probe, pD2, show several major hybridizing fragments. Of these, two human PvuII fragments of 1.4 kb and 2.4 kb had unique mobilities compared to mouse fragments. In a study of 19 cell hybrids, the human-specific U1 fragments segregated with the chromosome 1 markers peptidase C and adenylate kinase 2. All other chromosomes showed greater than or equal to 19% discordancy . An additional 13 karyotyped cell hybrids, analyzed by Southern filter analysis, confirmed the assignment of this class of U1 genes to chromosome 1. Additional digests with MspI and PstI indicated that most U1 genes are located on chromosome 1. To determine if the U1 RNAs are located predominantly at one site or dispersed over chromosome 1, a tritium-labeled U1 probe was hybridized in situ to metaphase chromosomes. The majority of the grains were at band 1p36 .3, suggesting that most of the U1 genes are located in this region.
Somat Cell Mol Genet 1984 May
PMID:Localization of human U1 small nuclear RNA genes to band p36.3 of chromosome 1 by in situ hybridization. 620 11

Leishmania mexicana mexicana amastigotes have been shown to contain greater activities than promastigotes of the enzymes that catalyse the beta-oxidation of fatty acids, but lower activities of several glycolytic enzymes, with the activity of pyruvate kinase being especially low. The results suggest the beta-oxidation of fatty acids is relatively more important to Leishmania amastigotes than promastigotes, whereas the reverse is true for glycolysis. Succinic dehydrogenase and peptidase activities were much higher in promastigotes than amastigotes. The activities of glucose-6-phosphatase, fructose-1,6-bisphosphatase, acid phosphatase and glucose-6-phosphate dehydrogenase varied less, although in each case the activity was significantly lower in the mammalian stage. A method for lysing and fractionating L. m. mexicana promastigotes has been developed. Using this procedure it has been established that many of the glycolytic and functionally related enzymes are located in cell organelles, that hexokinase is intimately connected with the particulate part of the parasite, and that the microsomal fraction of L. m. mexicana is very different in composition from the microsomes of mammalian liver cells.
Mol Biochem Parasitol 1982 Mar
PMID:A comparative study of Leishmania mexicana amastigotes and promastigotes. Enzyme activities and subcellular locations. 621 17

Presecretory signal peptides of 39 proteins from diverse prokaryotic and eukaryotic sources have been compared. Although varying in length and amino acid composition, the labile peptides share a hydrophobic core of approximately 12 amino acids. A positively charged residue (Lys or Arg) usually precedes the hydrophobic core. Core termination is defined by the occurrence of a charged residue, a sequence of residues which may induce a beta-turn in a polypeptide, or an interruption in potential alpha-helix or beta-extended strand structure. The hydrophobic cores contain, by weight average, 37% Leu: 15% Ala: 10% Val: 10% Phe: 7% Ile plus 21% other hydrophobic amino acids arranged in a non-random sequence. Following the hydrophobic cores (aligned by their last residue) a highly non-random and localized distribution of Ala is apparent within the initial eight positions following the core: (formula; see text) Coincident with this observation, Ala-X-Ala is the most frequent sequence preceding signal peptidase cleavage. We propose the existence of a signal peptidase recognition sequence A-X-B with the preferred cleavage site located after the sixth amino acid following the core sequence. Twenty-two of the above 27 underlined Ala residues would participate as A or B in peptidase cleavage. Position A includes the larger aliphatic amino acids, Leu, Val and Ile, as well as the residues already found at B (principally Ala, Gly and Ser). Since a preferred cleavage site can be discerned from carboxyl and not amino terminal alignment of the hydrophobic cores it is proposed that the carboxyl ends are oriented inward toward the lumen of the endoplasmic reticulum where cleavage is thought to occur. This orientation coupled with the predicted beta-turn typically found between the core and the cleavage site implies reverse hairpin insertion of the signal sequence. The structural features which we describe should help identify signal peptides and cleavage sites in presumptive amino acid sequences derived from DNA sequences.
J Mol Biol 1983 Jun 25
PMID:A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. 634 94

When an Escherichia coli K-12 culture was starved for glucose, 50% of the cells lost viability in about 6 days. When a K-12 mutant lacking five distinct peptidase activities, CM89, was starved in the same manner, viability was lost much more rapidly; 50% of the cells lost viability in about 2 days, whereas a parent strain lacking only one peptidase activity lost 50% viability in about 4 days. Compared with the wild-type strain and with its parent strain CM17, CM89 was defective in both protein degradation and protein synthesis during carbon starvation. Similar results were obtained with glucose-starved Salmonella typhimurium LT2 and LT2-derived mutants lacking various peptidase activities. An S. typhimurium mutant lacking four peptidases, TN852, which was deficient in both protein degradation and synthesis during carbon starvation (Yen et al., J. Mol. Biol. 143:21-33, 1980), was roughly one-third as stable as the isogenic wild type. Isogenic S. typhimurium strains that lacked various combinations of three of four peptidases and that displayed protein degradation and synthesis rates intermediate between those of LT2 and TN852 (Yen et al., J. Mol. Biol. 143:21-33, 1980) displayed corresponding stabilities during carbon starvation. These results point to a role for protein degradation in the survival of bacteria during starvation for carbon.
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PMID:Role of protein degradation in the survival of carbon-starved Escherichia coli and Salmonella typhimurium. 636 90

The considerable expansion in studies on the enzymic inactivation of thyrotrophin-releasing hormone, luteinizing hormone-releasing hormone and somatostatin (growth hormone release-inhibiting hormone) has necessitated a re-evaluation of the peptidase enzymes responsible. Through the use of new methods such as high-performance liquid chromatography and the development of artificial enzyme substrates, it has been possible to clarify the mechanisms of enzyme cleavage of these hypothalamic regulatory hormones and to attempt purification of the peptidases. This has brought about a renewed interest in the physiological significance of the enzymes, as well as their role in biotransformation of the hypothalamic hormones. From such studies, the information gained may be used in the design of agonist and antagonist analogues, as well as providing details of the mechanisms of action of such analogues through their increased stability to enzymic degradation. The characterization of corticotrophin-releasing factor and growth hormone-releasing factor will provide a new field for the application of peptidase inactivation to analogue design. Similarly, future examination of the peptidases inactivating the hypothalamic hormones in certain clinical conditions may give new insight into the significance of the enzymes in pathological conditions. Identification of these enzymes, investigation of their localization, properties and functions and assessment of their contribution to the control of hormone action may yield valuable insight into the physiology and pathology of the hypothalamic regulatory hormones.
Mol Cell Endocrinol 1983 Nov
PMID:Enzymic inactivation of hypothalamic regulatory hormones. 641 8

The major proteins of yellowjacket venoms have been isolated and characterized immuno-chemically. They consist of hyaluronidase, phospholipase, and antigen 5. Venoms from three species of yellowjacket were studied. Vespula germanica, V. maculifrons, and V. vulgaris. The phospholipases could be isolated in good yield only when affinity chromatography was used to minimize limited proteolysis. A kallikrein-like peptidase was found present in the yellowjacket venom. Phospholipases from these three species were immunochemically indistinguishable from each other, as were their antigen 5s. Sera from individuals sensitive to yellowjacket venom contained IgE and IgG specific for antigen 5 and phospholipase.
Mol Immunol 1983 Mar
PMID:Immunochemical studies of yellowjacket venom proteins. 686 52

L-leucine-beta-naphthylamide (LNA) will support growth of a leucine auxotroph of Salmonella typhimurium. Utilization of this compound depends on the presence in the cells of active peptidase N. Selection for improved growth on a suboptimal concentration of LNA yields mutants some of which contain elevated levels of peptidase N. The properties of these strains indicate that they carry tandem genetic duplication of the pepN locus: they show rec-dependent genetic instability; they contain an approximately doubled level of the pepN gene product; neighboring chromosomal loci are also duplicated; and, the mutants occur with a greatly diminished frequency in rec- strains. When selection for improved growth on LNA is applied to a rec- strain, the mutants obtained do not contain duplications. These strains appear to contain lesions in the pepN gene that lead to the production of a peptidase N with altered substrate specificity.
Mol Gen Genet 1982
PMID:Salmonella typhimurium mutations affecting utilization of L-leucine beta-naphthylamide. 695 84

An acid peptidase that degrades hemoglobin optimally at pH 3.5, a neutral aminopeptidase and an alkaline endopeptidase that acts on an alpha-N-blocked synthetic substrate have been demonstrated in Plasmodium falciparum in culture. The enzymes were shown to be distinct by anion exchange chromatography, gel filtration on Sephadex G-200 and isoelectric focusing. The activities of the acid peptidase and the aminopeptidase were inhibited by antimalarial compounds.
Mol Biochem Parasitol 1982 Apr
PMID:Peptidases from Plasmodium falciparum cultured in vitro. 704 89

Respiratory epithelial cell surface neutral endopeptidase 24.11 (NEP-24.11) degrades proinflammatory peptides, and it has been suggested that glucocorticoids may reduce airway inflammation, in part, by upregulation of NEP-24.11. Despite the potential importance of the epithelium as a metabolic barrier, little is known regarding what other peptidases may be present on the epithelial cell surface. Using an immortalized bronchial epithelial cell line (BEAS-2B), we have shown that human epithelial cells express no detectable angiotensin-converting enzyme, carboxypeptidase N, or dipeptidyl(amino)peptidase IV, but express significant levels of aminopeptidase M (AmM), as well as NEP-24.11. The presence of these enzymes was demonstrated via their degradation of biologically active peptides and by flow cytometry. Exposure of cells to the glucocorticoid budesonide (10(-7) M) for up to 5 days did not markedly alter the expression of NEP-24.11 or AmM, as assessed by flow cytometry, nor did glucocorticoid treatment modify rates of peptide hydrolysis by NEP-24.11 or AmM. Thus, BEAS-2B cells have both AmM and NEP-24.11 on their surface, and expression of these enzymes is not altered by glucocorticoids.
Am J Respir Cell Mol Biol 1994 Jul
PMID:Glucocorticoids do not alter peptidase expression on a human bronchial epithelial cell line. 751 43


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