Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Radiochemical determination of a unique sequence around the reactive serine residue of a di-isopropyl phosphorofluoridate-sensitive plant carboxypeptidase and a yeast peptidase.

ABSTRACT: Phaseolain, a carboxypeptidase from French-bean leaves, and a partially purified peptidase from baker's yeast are inhibited by reaction with di-isopropyl phosphorofluoridate. Radioactive di-isopropyl [(32)P]phosphorofluoridate was used to show that the site of reaction is a unique serine residue and that the sequence of amino acids adjacent to the reactive serine is Glu-Ser-Tyr. This sequence is different from those of other ;serine' enzymes previously reported and, for phaseolain, represents an unequivocal example of a ;serine' carboxypeptidase.

SUBMITTER: Shaw DC

PROVIDER: S-EPMC1173758 | biostudies-other | 1972 Jun

REPOSITORIES: biostudies-other

ACCESS DATA

Json Xml

Similar Datasets

The reactive serine residue of epidermolytic toxin A.

Project description:Comparison of amino acid sequence data suggested that there may be a functional relationship between the staphylococcal epidermolytic toxins and V8 proteinase. The hypothesis was tested by treating epidermolytic toxin with di-isopropyl phosphorofluoridate, which bound specifically at serine-195, the homologue of the active-site serine residue of V8 proteinase.

| S-EPMC1131611 | biostudies-other

Bovine pepsinogens and pepsins. The sequence around a reactive aspartyl residue.

Project description:The specific inhibitor, N-diazoacetylnorleucine methyl ester reacts stoicheiometrically with bovine pepsin resulting in a simultaneous loss of all enzymic activity. A peptide containing a modified aspartyl group was isolated from bovine pepsin labelled with (14)C-labelled inhibitor. The aspartic acid residue is presumed to be part of the active centre and is in the same heptapeptide sequence as in porcine pepsin: Ile-Val-Asp-Thr-Gly-Thr-Ser.

| S-EPMC1177243 | biostudies-other

The reactive serine residue in phosphoglucomutase of Micrococcus lysodeikiticus.

Project description:1. Phosphoglucomutase of Micrococcus lysodeikticus was labelled at the active site by exchange with (32)P-labelled substrates of high specific radioactivity. 2. Partial acid hydrolysis gave rise to radioactive peptides; serine phosphate was identified as one of the derivatives. 3. Comparison of the other (32)P-labelled peptides with the peptides obtained from the (32)P-labelled rabbit muscle phosphoglucomutase indicates that the sequence around the reactive serine residue is identical in both enzymes.

| S-EPMC1165860 | biostudies-other

The amino acid sequence around the reactive cysteine residue in human plasma Factor XII.

Project description:1. Activated human plasma factor XIII was 65% inhibited by iodo[(14)C]acetate and incorporated 0.6 mol of label into the alpha subunit, which eventually was allowed to form a precipitate. 2. All the label was recovered as S-carboxymethylcysteine in a tetra-peptide of sequence Gly-Gln-Cys-Trp.

| S-EPMC1165912 | biostudies-other

A tryptic peptide containing a unique serine phosphate residue in rabbit phosphoglucomutase.

Project description:(32)P-labelled phosphoglucomutase was digested with trypsin after denaturation and two peptides were isolated that contained the bulk of the radioactivity bound to peptides. Both peptides appeared to derive from an identical section of the molecule. Peptic and subtilisin digests of the tryptic peptides were prepared. The resulting radioactive peptides were purified and their sequences studied. The presence of a single serine [(32)P]phosphate residue was clearly established. Difficulties in purification and low yields, especially of the tryptic peptide, prevented exhaustive sequence studies, but a tentative sequence is proposed as:Ala-Ile-Gly-Gly-Ile-Ile-Leu-Thr-Ala-SerP-His-Asx-Pro-Gly-Gly-Pro-(Asx(2),Gly)-Phe-Gly-Ile-Lys(where SerP represents serine phosphate and Asx represents aspartic acid or asparagine). The results do not support the presence of two serine phosphate residues in the denatured enzyme, but confirm previous results of a unique sequence around a single serine phosphate residue.

| S-EPMC1186757 | biostudies-other

Rapid aging of neurotoxic esterase after inhibition by di-isopropyl phosphorofluoridate.

Project description:1. It was proposed [Johnson (1974) J. Neurochem.23, 785-789] that an essential step in the genesis of delayed neuropathy caused by some organophosphorus esters was aging of phosphorylated neurotoxic esterase, involving generation of a charged monosubstituted phosphoric acid residue on the protein. 2. Neurotoxic esterase of hen brain was inhibited with di-isopropyl phosphorofluoridate either unlabelled or mixed-labelled with (3)H and (32)P. 3. Reactivation of inhibited enzyme by KF was possible only immediately after a brief inhibition:aging at pH8.0 and 37 degrees C occurred with a half-life of about 2-4min. 4. When the radiolabelled enzyme was studied no loss of label was observed during the expected aging period, but a change in the nature of the bound radioisotopes occurred (half-life=3.25min). 5. Alkaline hydrolysis of labelled enzyme liberated di-isopropyl phosphate at early times after labelling, but increasing amounts of monoisopropyl phosphate plus a volatile tritiated compound (possibly propan-2-ol) at later times. 6. Treatment of labelled enzyme with KF released di-isopropyl phosphate and caused reactivation of enzyme to similar degrees. It is concluded that the chemical change from di-isopropyl phosphoryl-enzyme to mono-isopropyl phosphoryl-enzyme and the loss of reactivatibility are related. 7. The rate of aging is similar at pH5.2, 6.5 and 8. Aging is unaffected by addition of reduced glutathione and imidazole at pH5.2 or 8, and none of the transferred (3)H is trapped by these reagents. The mechanism of aging must be different from the better-known dealkylation aging of the cholinesterases.

| S-EPMC1186405 | biostudies-other

Pestivirus NS2-3/NS3 Serine Peptidase

Project description:The third edition of the Handbook of Proteolytic Enzymes aims to be a comprehensive reference work for the enzymes that cleave proteins and peptides, and contains over 800 chapters. Each chapter is organized into sections describing the name and history, activity and specificity, structural chemistry, preparation, biological aspects, and distinguishing features for a specific peptidase. The subject of Chapter 690 is Pestivirus NS2-3/NS3 Serine Peptidase. Keywords Bovine viral diarrhea virus, Cis cleavage, cofactor, flaviviridae, hepacivirus, NS4A cofactor, pestivirus, peptidyl mimetic, serine protease.

| S-EPMC7150157 | biostudies-literature

Evolution of serine carboxypeptidase-like acyltransferases in the monocots.

Project description: Not available

| S-EPMC2884133 | biostudies-literature

BRS1, a serine carboxypeptidase, regulates BRI1 signaling in Arabidopsis thaliana.

Project description:Brassinosteroid-insensitive 1 (BRI1) of Arabidopsis thaliana encodes a cell surface receptor for brassinosteroids. Mutations in BRI1 severely affect plant growth and development. Activation tagging of a weak bri1 allele (bri1-5) resulted in the identification of a new locus, brs1-1D. BRS1 is predicted to encode a secreted carboxypeptidase. Whereas a brs1 loss-of-function allele has no obvious mutant phenotype, overexpression of BRS1 can suppress bri1 extracellular domain mutants. Genetic analyses showed that brassinosteroids and a functional BRI1 protein kinase domain are required for suppression. In addition, overexpressed BRS1 missense mutants, predicted to abolish BRS1 protease activity, failed to suppress bri1-5. Finally, the effects of BRS1 are selective: overexpression in either wild-type or two other receptor kinase mutants resulted in no phenotypic alterations. These results strongly suggest that BRS1 processes a protein involved in an early event in the BRI1 signaling.

| S-EPMC33313 | biostudies-literature

Effects of di-isopropyl phosphorofluoridate on rat liver microsomal and lysosomal beta-glucuronidase.

Project description:iPr(2)P-F (di-isopropyl phosphorofluoridate) administration to rats produces a liver-dependent specific elevation of plasma beta-glucuronidase activity. The response is unaffected by puromycin pretreatment. By using subcellular-fractionation techniques, the rise in plasma beta-glucuronidase activity was correlated temporally with a fall in liver microsomal beta-glucuronidase activity. After iPr(2)P-F treatment, liver microsomal membranes are depleted of beta-glucuronidase but slowly return to normal over 1 week. On the other hand, liver lysosomal beta-glucuronidase activity is high at early time points (less than 60min) after iPr(2)P-F administration but decreases to below control values; this lasts for a few days. The response to iPr(2)P-F was demonstrated in isolated hepatocytes prepared from iPr(2)P-F-treated rats. In such preparations, microsomal beta-glucuronidase is lost rapidly, followed by a specific decrease in hepatocyte lysosomal beta-glucuronidase. The results suggest that a pool of microsomal beta-glucuronidase serves as precursor to plasma beta-glucuronidase in iPr(2)P-F-treated rats, and further, that microsomal beta-glucuronidase may serve as precursor to lysosomal beta-glucuronidase.

| S-EPMC1164831 | biostudies-other

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data