Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

T and B lymphocytes from human tonsils were separated on a nylon wool column. T. cells are enriched in the nonadherent, B cells in the adherent fraction. Several enzymes and other markers were tested in separated and non separated lymphocyte populations. Certain enzymes and other properties can be used as T or B lymphocyte markers because of their preferential occurrence and because of the advantages of their estimation (simple, quick methods, objective evaluation). The following characteristics were considered as markers on the basis of our results: (I) acid phosphatase, Na+-K+-activated ATPase, BAEE-peptidase and chromium labeling in T lymphocytes; (II) 5'-nucleotidase, FITC-IgG binding, N-acetyl-D-glucosaminidase, thymidine and valine incorporation in B lymphocytes.
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PMID:Characteristic biochemical differences in human T and B lymphocytes separated on nylon wool. 387 65

Particulates containing a large part of the alkaline phosphatase activity of renal tissue were separated from homogenates and from ribosomal preparations by zonal centrifugation. The particles had a high content of phospholipid and cholesterol that was not removed by treatment with I percent deoxycholate. Enzymatic activities concentrated with the particles were the alkaline phosphatase, a peptidase resistant to proteolysis, glucose-6-phosphatase, inorganic pyrophos-phatase, and adenosine triphosphatase. The particles accumulated leucine with no stimulation from soluble factors and with inhibition by other amino acids; the accumulation was stimulated by adenosine triphosphate and was not inhibited by puromycin. The particles appear to be derived from the membranes of the brush borders of tubular cells.
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PMID:Brush border particulates of renal tissue. 430 46

Most of the gamma-glutamyltransferase occurring in semen was found to be bound to the membranes of prostatic organelles, as is the case with Mg++-Ca++-dependent ATPase, and Zn++-dependent peptidase hydrolysing succinyl (alanine)3-paranitroanilide. Organelle-bound gamma-glutamyltransferase was released in a water-soluble form by papain. Charge shift electrophoresis revealed the presence in seminal fluid of a small additional amount of gamma-glutamyltransferase that is unbound and water-soluble, but also of prostatic origin. After papain treatment there was no sign of the organelle-bound Zn++-dependent peptidase activity, nor of the Mg++-Ca++ dependent ATPase activity, both having been inactivated by the papain. Both organelle-bound gamma-glutamyltransferase and Zn++-dependent peptidase could be rendered soluble in active form with the non-ionic detergent Triton X-100.
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PMID:gamma-Glutamyltransferase bound to prostatic subcellular organelles and in free form in human seminal plasma. 613 49

Subunit 9 (dicyclohexylcarbodiimide binding protein, 'proteolipid') of the mitochondrial F1F0-ATPase is a nuclearly coded protein in Neurospora crassa. It is synthesized on free cytoplasmic ribosomes as a larger precursor with an NH2-terminal peptide extension. The peptide extension is cleaved off after transport of the protein into the mitochondria. A processing activity referred to as processing peptidase that cleaves the precursor to subunit 9 and other mitochondrial proteins is described and characterized using a cell-free system. Precursor synthesized in vitro was incubated with extracts of mitochondria. Processing peptidase required Mn2+ for its activity. Localization studies suggested that it is a soluble component of the mitochondrial matrix. The precursor was cleaved in two sequential steps via an intermediate-sized polypeptide. The intermediate form in the processing of subunit 9 was also seen in vivo and upon import of the precursor into isolated mitochondria in vitro. The two cleavage sites in the precursor molecule were determined. The data indicate that: the correct NH2-terminus of the mature protein was generated, the NH2-terminal amino acid of the intermediate-sized polypeptide is isoleucine in position -31. The cleavage sites show similarity of primary structure. It is concluded that processing peptidase removes the peptide extension from the precursor to subunit 9 (and probably other precursors) after translocation of these polypeptides (or the NH2-terminal part of these polypeptides) into the matrix space of mitochondria.
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PMID:Processing peptidase of Neurospora mitochondria. Two-step cleavage of imported ATPase subunit 9. 623 9

A recently developed procedure, that has been shown to be suitable for detailed immunohistological analysis, has been used to prepare cryostat sections of bone marrow to investigate whether enzyme-histochemical techniques are also feasible on such material. A selected group of enzymes, some of which are inhibited or destroyed in paraffin- or plastic-embedded samples, have been demonstrated. The morphological details obtained were satisfactory in the preparations. The enzymes were dipeptidyl(amino)peptidase IV (for T lymphocytes); tartrate-resistant acid phosphatase (for hairy cell leukaemia); acid phosphatase and non-specific esterase (for macrophages and monocytes); ATPase and 5'nucleotidase (for B lymphocytes); and peroxidase or chloroacetate esterase (for granulocytic cells). In these preparations strong enzyme activities were shown. In adjacent sections the immunological analysis of membrane markers could also be performed contributing to a comprehensive study of the normal and malignant bone marrow cells.
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PMID:Enzyme histochemical analysis on cryostat sections of human bone marrow. 714 30

The function of the proteasome is controlled by a variety of specific regulatory proteins including activators, inhibitors, and modulators. Two recently discovered activators, termed PA28 and PA700, bind to the terminal rings of the proteasome to form proteasome-regulatory complexes which display greatly increased proteolytic activity. PA28 is a high-affinity activator of the proteasome's multiple peptidase activities. The carboxyl terminus of PA28 is required for its binding to the proteasome. PA700 binds to the proteasome via an ATP-dependent mechanism. PA700 has ATPase activity, and at least four of PA700's 16 subunits are members of a protein family containing a concensus sequence for ATP binding. Proteasome-PA700 complexes are activated with respect to both the hydrolysis of peptide substrates and the hydrolysis of ubiquitinated proteins.
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PMID:Regulatory proteins of the proteasome. 769 29

cDNA clone MS73 codes for an ATPase that is a regulatory subunit of the 26 S proteasome. Reverse transcriptase polymerase chain reaction analysis demonstrates that the expression of the gene dramatically increases in the pre-eclosion period. Western analyses show increases in other related. ATPases including MS73, MSS1, and mts2 but not TBP1. A similar increase in the 30-kDa subunit of the 20 S proteasome occurs. There are accompanying large changes in the peptidase activities of the 26 S proteasome. Relative to the 30-kDa subunit, there is no change in MSS1 and MS73, a 3-fold increase in mts2, and a 5-fold decline in TBP1. A large increase in the concentration of 26 S proteasomes together with extensive regulatory reprogramming may facilitate rapid muscular proteolysis.
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PMID:Developmental changes of the 26 S proteasome in abdominal intersegmental muscles of Manduca sexta during programmed cell death. 782 21

A point mutant in the ATP-binding motif (GPPGVGK362T) of the ATP-dependent protease La from Escherichia coli was investigated in which the lysine at position 362 was replaced by an alanine. The catalytic efficiency of the K362A mutant is at least two orders of magnitude lower than that of wild-type protease La due to a decreased Vmax and an increased KM for ATP. Simultaneously, the peptidase activity of La K362A is almost completely eliminated. Since selective inactivation of the peptidase activity of La does not affect its intrinsic ATPase activity, coupling of proteolysis with ATP hydrolysis is only uni-directional in this energy-dependent protease.
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PMID:A point mutation within the ATP-binding site inactivates both catalytic functions of the ATP-dependent protease La (Lon) from Escherichia coli. 798 99

The multicatalytic protease (MCP) associates with a 20 S ATPase complex in the presence of ATP to form the 26 S ubiquitin/ATP-dependent protease. This association results in a uniform 3-fold activation of peptide hydrolysis by MCP. In the absence of nucleotides, an 11 S regulator binds MCP and differentially stimulates its peptidase activities from 3-fold to 25-fold depending upon the peptide. When incubated separately with ATPase complex or regulator, all MCP molecules are converted to 26 S protease or to an activated MCP, respectively. Competition between ATPase complex and regulator for limiting amounts of MCP results in the 26 S protease as the only assembled species. Rabbit reticulocyte regulator is composed of a single 30-kDa protein. Among the 15 subunits in the ATPase complex, there is also a 30-kDa protein. Three findings demonstrate that the 30-kDa subunits in each complex are distinct proteins. First, two-dimensional polyacrylamide gel revealed different isoelectric points for each 30-kDa protein. Second, anti-regulator antibodies did not cross-react with proteins in the ATPase complex or in the 26 S protease. Third, directly sequenced peptides from the 30-kDa subunit of the ATPase complex are not present in the deduced amino acid sequence of the regulator. Thus, the regulator and ATPase complex are independent activators of MCP.
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PMID:Activation of the multicatalytic protease. The 11 S regulator and 20 S ATPase complexes contain distinct 30-kilodalton subunits. 820 11

The role of mitochondrial 70-kD heat shock protein (mt-hsp70) in protein translocation across both the outer and inner mitochondrial membranes was studied using two temperature-sensitive yeast mutants. The degree of polypeptide translocation into the matrix of mutant mitochondria was analyzed using a matrix-targeted preprotein that was cleaved twice by the processing peptidase. A short amino-terminal segment of the preprotein (40-60 amino acids) was driven into the matrix by the membrane potential, independent of hsp70 function, allowing a single cleavage of the presequence. Artificial unfolding of the preprotein allowed complete translocation into the matrix in the case where mutant mt-hsp70 had detectable binding activity. However, in the mutant mitochondria in which binding to mt-hsp70 could not be detected the mature part of the preprotein was only translocated to the intermembrane space. We propose that mt-hsp70 fulfills a dual role in membrane translocation of preproteins. (a) Mt-hsp70 facilitates unfolding of the polypeptide chain for translocation across the mitochondrial membranes. (b) Binding of mt-hsp70 to the polypeptide chain is essential for driving the completion of transport of a matrix-targeted preprotein across the inner membrane. This second role is independent of the folding state of the preprotein, thus identifying mt-hsp70 as a genuine component of the inner membrane translocation machinery. Furthermore we determined the sites of the mutations and show that both a functional ATPase domain and ATP are needed for mt-hsp70 to bind to the polypeptide chain and drive its translocation into the matrix.
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PMID:A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins. 840 91


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