scholarly journals Covalent Linkage of Polyamines to Peptidoglycan inAnaerovibrio lipolytica

2000 ◽  
Vol 182 (4) ◽  
pp. 1154-1157 ◽  
Author(s):  
Takashi Hirao ◽  
Masahide Sato ◽  
Akira Shirahata ◽  
Yoshiyuki Kamio
Keyword(s):  
Glutamic Acid ◽  
Anaerobic Bacterium ◽  
Diaminopimelic Acid ◽  
Molar Ratio ◽  
Carboxyl Group ◽  
Strictly Anaerobic ◽  
Amino Group ◽  
Peptide Fragments ◽  
Covalent Linkage ◽  
Glutamic Acid Residue

ABSTRACT Spermidine and cadaverine were found to be constituents of the cell wall peptidoglycan of Anaerovibrio lipolytica, a strictly anaerobic bacterium. The peptidoglycan was degraded with theN-acetylmuramyl-l-alanine amidase and endopeptidase into two peptide fragments, peptide I and peptide II, at a molar ratio of 4:1. Peptides I and II were identified asl-alanine–d-glutamic acid(αcadaverine)γ meso-diaminopimelic acid (DAP)–d-alanine andl-alanine–d-glutamic acid(αspermidine)γ meso-DAP–d-alanine, respectively. The N1-amino group of spermidine was linked to the α-carboxyl group of the d-glutamic acid residue of peptide II.

scholarly journals Autolysis of cell walls of Bacillus stearothermophilus B65 and the chemical structure of the peptidoglycan

1970 ◽  
Vol 118 (5) ◽  
pp. 859-868 ◽  
Author(s):  
W. D. Grant ◽  
A. J. Wicken
Keyword(s):  
Glutamic Acid ◽  
Cell Walls ◽  
Bacillus Stearothermophilus ◽  
Teichoic Acid ◽  
Paper Electrophoresis ◽  
Diaminopimelic Acid ◽  
Peptide Fragments ◽  
Acid Complex ◽  
Acid Hydrolysate ◽  
Peptide Mixture

1. The cell walls of Bacillus stearothermophilus B65 contain glucosamine, muramic acid, alanine, α∈-diaminopimelic acid (Dap), glutamic acid, aspartic acid, glycine, and serine in the molecular proportions 0.60:0.64:2.30:0.85:1.00:0.11:0.13:0.31. 2. Both d- and l-alanine are present, but glutamic acid and diaminopimelic acid are present only as the d- and meso-isomers respectively. 3. The peptide fragments Ala-Dap, Dap-Ala, and Dap-Ala-Dap have been isolated from a partial acid hydrolysate of the cell walls. 4. The major products of autolysis of the cell wall were d-alanine, a peptide mixture, peptidoglycan material and a peptidoglycan–teichoic acid complex. 5. Separation of the peptide mixture into ten major peptides was achieved by DEAE-Sephadex and paper chromatography, and paper electrophoresis. 6. The structures of these peptides have been determined and they fall into four groups, the individual members of each group differing only in number or position of carboxamide substituents. 7. The structures are I, a tripeptide l-Ala–d-Glu-meso-Dap; II, a pentapeptide made up by the tripeptide (I) linked through the ∈-amino group of its diaminopimelic acid residue to the carboxyterminal of the dipeptide meso-Dap-d-Ala; III, a heptapeptide made up by a similar linkage between the tripeptide (I) and the tetrapeptide l-Ala-d-Glu-meso-Dap-d-Ala; IV, a possible undecapeptide made up by a further tetrapeptide similarly linked to the heptapeptide (III) structure. 8. The structure of the peptidoglycan and the actions of the autolytic enzymes are discussed in terms of these peptide structures.

scholarly journals Sortase C-Mediated Anchoring of BasI to the Cell Wall Envelope of Bacillus anthracis

2007 ◽  
Vol 189 (17) ◽  
pp. 6425-6436 ◽  
Author(s):  
Luciano A. Marraffini ◽  
Olaf Schneewind
Keyword(s):  
Cell Wall ◽  
Bacillus Anthracis ◽  
Active Site ◽  
Diaminopimelic Acid ◽  
Side Chain ◽  
Carboxyl Group ◽  
Amino Group ◽  
Active Site Cysteine ◽  
New Hosts ◽  
Host Death

ABSTRACT Vegetative forms of Bacillus anthracis replicate in tissues of an infected host and precipitate lethal anthrax disease. Upon host death, bacilli form dormant spores that contaminate the environment, thereby gaining entry into new hosts where spores germinate and once again replicate as vegetative forms. We show here that sortase C, an enzyme that is required for the formation of infectious spores, anchors BasI polypeptide to the envelope of predivisional sporulating bacilli. BasI anchoring to the cell wall requires the active site cysteine of sortase C and an LPNTA motif sorting signal at the C-terminal end of the BasI precursor. The LPNTA motif of BasI is cleaved between the threonine (T) and the alanine (A) residue; the C-terminal carboxyl group of threonine is subsequently amide linked to the side chain amino group of diaminopimelic acid within the wall peptides of B. anthracis peptidoglycan.

Isolierung und Identifizierung eines serinhaltigen UDP-muramyl-tripeptides aus Butyribacterium rettgeri

1968 ◽  
Vol 23 (2) ◽  
pp. 217-220 ◽  
Author(s):  
I. Miller ◽  
R. Plapp ◽  
O. Kandler
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Glutamic Acid ◽  
Group Analysis ◽  
Partial Hydrolysis ◽  
Carboxyl Group ◽  
Amino Group ◽  
Muramic Acid ◽  
End Group

An UDP-activated murein precursor was isolated from Butyribacterium rettgeri after one hour inhibition by D-cycloserine. The compound contains UDP, muramic acid, L-serine, D-glutamic acid and L-ornithine in equimolar amounts. The amino acid sequence of the tripeptide attached to muramic acid is L-Ser-D-Glu-L-Orn as determined by end group analysis and identification of peptides obtained after partial hydrolysis. As shown by the identification of glutamic acid -γ-hydrazid after hydrazinolysis of the compound, ornithine is bound by its α-amino group to the γ-carboxyl group of glutamic acid. The amino acid sequence of the precursor is in agreement with the structure of the corresponding part of the whole murein of Butyribacterium rettgeri, as proposed recently.

scholarly journals The Identification of a Glutamic Acid Residue as Part of the Active Site of Ribonuclease T1

1967 ◽  
Vol 242 (20) ◽  
pp. 4682-4690 ◽  
Author(s):  
Kenji Takahashi ◽  
William H. Stein ◽  
Stanford Moore
Keyword(s):  
Glutamic Acid ◽  
Active Site ◽  
Ribonuclease T1 ◽  
Glutamic Acid Residue

scholarly journals Conversion of Daidzein and Genistein by an Anaerobic Bacterium Newly Isolated from the Mouse Intestine

2008 ◽  
Vol 74 (15) ◽  
pp. 4847-4852 ◽  
Author(s):  
Anastasia Matthies ◽  
Thomas Clavel ◽  
Michael Gütschow ◽  
Wolfram Engst ◽  
Dirk Haller ◽  
...  
Keyword(s):  
Stationary Phase ◽  
Enzyme Induction ◽  
Growth Phase ◽  
Anaerobic Bacterium ◽  
Stationary Growth Phase ◽  
Gut Bacteria ◽  
Soy Isoflavones ◽  
Strictly Anaerobic ◽  
Stationary Growth ◽  
Mouse Intestine

ABSTRACT The metabolism of isoflavones by gut bacteria plays a key role in the availability and bioactivation of these compounds in the intestine. Daidzein and genistein are the most common dietary soy isoflavones. While daidzein conversion yielding equol has been known for some time, the corresponding formation of 5-hydroxy-equol from genistein has not been reported previously. We isolated a strictly anaerobic bacterium (Mt1B8) from the mouse intestine which converted daidzein via dihydrodaidzein to equol as well as genistein via dihydrogenistein to 5-hydroxy-equol. Strain Mt1B8 was a gram-positive, rod-shaped bacterium identified as a member of the Coriobacteriaceae. Strain Mt1B8 also transformed dihydrodaidzein and dihydrogenistein to equol and 5-hydroxy-equol, respectively. The conversion of daidzein, genistein, dihydrodaidzein, and dihydrogenistein in the stationary growth phase depended on preincubation with the corresponding isoflavonoid, indicating enzyme induction. Moreover, dihydrogenistein was transformed even more rapidly in the stationary phase when strain Mt1B8 was grown on either genistein or daidzein. Growing the cells on daidzein also enabled conversion of genistein. This suggests that the same enzymes are involved in the conversion of the two isoflavones.

Tu1049 Serum Des-y-Carboxy Prothrombin Ratio by Glutamic Acid Residue Is a Novel Useful Biomarker for Hepatocellular Carcinoma

2013 ◽  
Vol 144 (5) ◽  
pp. S-1040
Author(s):  
Masahiko Tameda ◽  
Katsuya Shiraki ◽  
Kazushi Sugimoto ◽  
Suguru Ogura ◽  
Yuji Inagaki ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Glutamic Acid ◽  
Glutamic Acid Residue

scholarly journals Targeting of the transcription factor Max during apoptosis: phosphorylation-regulated cleavage by caspase-5 at an unusual glutamic acid residue in position P1

2001 ◽  
Vol 358 (3) ◽  
pp. 705 ◽  
Author(s):  
Anja KRIPPNER-HEIDENREICH ◽  
Robert V. TALANIAN ◽  
Renate SEKUL ◽  
Regine KRAFT ◽  
Hubert THOLE ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Glutamic Acid ◽  
Glutamic Acid Residue

Calcium-activated proteases in the bovine parathyroid gland: potential role in degradation of parathyroid hormone to peptide fragments

1995 ◽  
Vol 15 (1) ◽  
pp. 61-71 ◽  
Author(s):  
P H Watson ◽  
S T Mortimer ◽  
K K W Wang ◽  
D E Croall ◽  
D A Hanley
Keyword(s):  
Parathyroid Hormone ◽  
Parathyroid Tissue ◽  
Area Under The Curve ◽  
Molar Ratio ◽  
Cell Protein ◽  
Parathyroid Cell ◽  
Peptide Fragments ◽  
Intracellular Degradation ◽  
Peak Areas

ABSTRACT Our studies suggest that protein kinase C is involved in low calcium (Ca2+)-stimulated secretion of parathyroid hormone (PTH) but not directly in high Ca2+-stimulated intracellular degradation of PTH to secreted carboxyl-terminal fragments (C-PTH), an important component of Ca2+-regulated PTH secretion. The present study was undertaken to determine the presence of calciumactivated proteases, 84 kDa (micro)-calpain and 80 kDa (milli)-calpain, in the bovine parathyroid, and whether they could degrade PTH to C-terminal fragments. Immunocytochemistry of bovine parathyroid tissue using antibodies raised against bovine heart micro- and milli-calpain detected both isoforms of calpain. Western blotting of total bovine parathyroid cell protein prepared from primary cell cultures confirmed the presence of both isoforms of calpain, demonstrated by specific milli- and micro-calpain bands. Purified bovine PTH (bPTH) was incubated in vitro with human erythrocyte micro-calpain and the cleavage products were separated by reverse-phase HPLC. Eluant fractions were assayed with an RIA with equimolar sensitivity to C-PTH and bPTH, and peak areas integrated. Micro-calpain produced a C-PTH peak from bPTH which co-eluted with the major C-PTH secreted by parathyroid cells in culture. C-PTH production by micro-calpain, expressed as per cent area under the curve, increased from 0% in the absence of either micro-calpain or Ca2+, to 71·5% when a 5:1 molar ratio of bPTH to calpain was used. Amino acid sequencing and analysis of the immunoreactive PTH cleavage products indicated the presence of two fragments of bPTH in the C-PTH peak, bPTH47–84 and bPTH69–84. In summary, both isoforms of calpain are present in the bovine parathyroid and calpains may play a role in the Ca2+-dependent degradation of PTH to secreted C-terminal fragments.

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