The Carboxylation Of Bovine Vitamin K-Dependent Proteins By Bovine Carboxylase

1981 ◽  
Author(s):  
C Vermeer ◽  
B A M Soute ◽  
H C Hemker ◽  
M de Metz
Keyword(s):  
Amino Acid ◽  
Vitamin K ◽  
Specific Adsorption ◽  
The Other ◽  
Amino Acid Residues ◽  
Factor X ◽  
Good Substrate ◽  
Enzyme Systems ◽  
Endogenous Substrate ◽  
Low Efficiency

Bovine vitamin K-dependent carboxylase was prepared, both from normal cows and from warfarin-treated ones. The two carboxylating enzyme systems were similar except for the fact that carboxylase from warfarin-treated cows contained a 100-fold higher amount of endogenous substrate. About 65% of this substrate consisted of one-chain factor X-precursor (s) and 25% of prothrombin-precursor(s). Solubilized carboxylase could be purified more than 100-fold by immuno- specific adsorption onto immobilized antifactor X antibodies. The purified enzyme contained 40% (w/w) phospholipid (mainly phosphatidylcholine), which was absolutely required for the carboxylating activity.Carboxylase from non-anticoagulated cows was used for studying exogenous substrates. Bovine descarboxyprothrombin, descarboxyfragment-1 and the pentapeptide Phe-Leu-Glu- Glu-Leu were carboxylated with a low efficiency (Km, between 0.4 and 11 mM). On the other hand a peptide, identical to the amino acid residues 13-29 in descarboxyprothrombin, had a Km of 0.001 mM. It seems probable therefore that the latter peptide contains all information required for a good substrate.

Substrate Recognition by Vitamin K-Dependent Carboxylase

1987 ◽  
Vol 57 (01) ◽  
pp. 017-019 ◽  
Author(s):  
Magda M W Ulrich ◽  
Berry A M Soute ◽  
L Johan M van Haarlem ◽  
Cees Vermeer
Keyword(s):  
Amino Acid ◽  
Vitamin K ◽  
Substrate Recognition ◽  
Bovine Liver ◽  
Amino Acid Residues

SummaryDecarboxylated osteocalcins were prepared and purified from bovine, chicken, human and monkey bones and assayed for their ability to serve as a substrate for vitamin K-dependent carboxylase from bovine liver. Substantial differences were observed, especially between bovine and monkey d-osteocalcin. Since these substrates differ only in their amino acid residues 3 and 4, it seems that these residues play a role in the recognition of a substrate by hepatic carboxylase.

Oxytocin analogues with non-coded amino acid residues in position 8: [8-Neopentylglycine]oxytocin and [8-cycloleucine]oxytocin

1987 ◽  
Vol 52 (9) ◽  
pp. 2317-2325 ◽  
Author(s):  
Jan Hlaváček ◽  
Jan Pospíšek ◽  
Jiřina Slaninová ◽  
Walter Y. Chan ◽  
Victor J. Hruby
Keyword(s):  
Amino Acid ◽  
Solid Phase Synthesis ◽  
Solid Phase ◽  
The Other ◽  
Amino Acid Residues ◽  
Phase Synthesis ◽  
Other Hand ◽  
Fragment Condensation

[8-Neopentylglycine]oxytocin (II) and [8-cycloleucine]oxytocin (III) were prepared by a combination of solid-phase synthesis and fragment condensation. Both analogues exhibited decreased uterotonic potency in vitro, each being about 15-30% that of oxytocin. Analogue II also displayed similarly decreased uterotonic potency in vivo and galactogogic potency. On the other hand, analogue III exhibited almost the same potency as oxytocin in the uterotonic assay in vivo and in the galactogogic assay.

New Antibiotic Uperin Peptides From the Dorsal Glands of the Australian Toadlet Uperoleia mjobergii

1996 ◽  
Vol 49 (12) ◽  
pp. 1325 ◽  
Author(s):  
AM Bradford ◽  
JH Bowie ◽  
MJ Tyler ◽  
JC Wallace
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Related Species ◽  
Antibiotic Activity ◽  
Amino Acid Sequences ◽  
The Other ◽  
Cationic Peptides ◽  
Amino Acid Residues ◽  
Skin Glands ◽  
Edman Sequencing

The dorsal glandular extract of the toadlet Uperoleia mjobergii contains more than 20 peptides. We report the amino acid sequences of the seven major peptides: these were determined by a combination of mass spectrometry and automated Edman sequencing. Three of these peptides have 19 amino acid residues and belong to the uperin 2 group of peptides [e.g. uperin 2.6, Gly Ile Leu Asp Ile Ala Lys Lys Leu Val Gly Gly Ile Arg Asn Val Leu Gly Ile (OH)], while the other four have 17 residues and are classified as uperins 3 [e.g. Uperin 3.4, Gly Val Gly Asp Leu Ile Arg Lys Ala Val Ala Ala Ile Lys Asn Ile Val (NH2)]. Several of these cationic peptides have been synthesized in order for bioassays to be carried out: they show significant antibiotic activity against a range of Gram-positive microorganisms. A major skin peptide from the related species Uperoleia inundata is a powerful neuropeptide named uperin 1.1 ([Ala2] uperolein ): no corresponding neuropeptide is detected in the skin glands of Uperoleia mjobergii.

Plural Origins of Molecular Homochirality in Our Biota Part II. The Relative Stabilities of Homochiral and Mixed Oligoribotides and Peptides

1997 ◽  
Vol 52 (1-2) ◽  
pp. 89-96 ◽  
Author(s):  
Thereza Amélia Soares ◽  
Roberto Dias Lins ◽  
Ricardo Longo ◽  
Richard Garratt ◽  
Ricardo Ferreira
Keyword(s):  
Molecular Dynamics ◽  
Amino Acid ◽  
Force Field ◽  
Molecular Mechanics ◽  
Computer Simulations ◽  
The Other ◽  
Amino Acid Residues ◽  
Relative Stabilities ◽  
Amber Force Field ◽  
Cross Inhibition

Abstract By computer simulations -molecular mechanics and molecular dynamics with the amber force field (Weiner et al., (1986), J. Comp. Chem. 7, 2 30-252) -we have determined the stabilities of oligoribotide strands built with ᴅ -and ʟ-riboses, and of peptide chains with ᴅ -and ʟ-amino acid residues. In particular, complementary double-chains of oligoribotides were studied, since they are an important feature of the growing mechanism of modern nucleic acids. Peptide chains on the other hand, grow without need of a template. We found that mixed oligoribotides are less stable than homochiral ones, and that this chiral effect is less noticeable in peptide chains. The results support the interpretation that ʟ-riboses act as terminators to the template-assisted growth of oligo-r-Gᴅ (enantiomeric cross-inhibition; Joyce et al., (1987), Proc. Natl. Acad. Sci. USA 84, 4398-4402). Based on this effect, a chemical pathway is proposed which could, under assumed prebiotic conditions, bypass the hindrance of homochiral growth.

The power of the force: mechano-physiology of the giant titin

2018 ◽  
Vol 2 (5) ◽  
pp. 681-686 ◽  
Author(s):  
Jaime Andrés Rivas-Pardo
Keyword(s):  
Amino Acid ◽  
Human Body ◽  
Actin Filaments ◽  
Polypeptide Chain ◽  
Single Gene ◽  
The Other ◽  
Amino Acid Residues ◽  
The Third ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

Titin — the largest protein in the human body — spans half of the muscle sarcomere from the Z-disk to the M-band through a single polypeptide chain. More than 30 000 amino acid residues coded from a single gene (TTN, in humans Q8WZ42) form a long filamentous protein organized in individual globular domains concatenated in tandem. Owing to its location and close interaction with the other muscle filaments, titin is considered the third filament of muscle, after the thick-myosin and the thin-actin filaments.

Isolation of Two Bovine Amelogenin Peptides and Their Amino Acid Sequences

1987 ◽  
Vol 1 (2) ◽  
pp. 276-281 ◽  
Author(s):  
J.-H. Yeh ◽  
T. Takagi ◽  
S. Sasaki
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Amino Acid Sequences ◽  
Polyacrylamide Gel ◽  
The Other ◽  
Edman Degradation ◽  
Amino Acid Residues ◽  
Peptide Fractions

Two peptide fractions of bovine amelogenin having a highly aggregative property to form polymers were purified by chromatography, SDS-polyacrylamide gel electrophoresis, and HPLC. Amino acid sequences of purified peptides were determined by automated Edman degradation. One peptide was found to be composed of 63 amino acid residues having a molecular weight of 7105, and the other of 86 residues having that of 9683. The sequence of the smaller peptide was identical to the C-terminal 63 residues of the amelogenin molecule of 170 residues previously reported, but the larger contained eight residues which are absent in the amelogenin sequence. There is a possibility that the latter peptide might be synthesized independently from mRNA spliced at different positions.

PRP19: a novel spliceosomal component

1993 ◽  
Vol 13 (3) ◽  
pp. 1876-1882
Author(s):  
S C Cheng ◽  
W Y Tarn ◽  
T Y Tsao ◽  
J Abelson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Molecular Weight ◽  
Amino Acid ◽  
The Other ◽  
Splicing Factor ◽  
Growth Defect ◽  
Splicing Factors ◽  
Temperature Sensitive ◽  
Amino Acid Residues ◽  
Exact Function

We have isolated the gene of a splicing factor, PRP19, by complementation of the temperature-sensitive growth defect of the prp19 mutant of Saccharomyces cerevisiae. The gene encodes a protein of 502 amino acid residues of molecular weight 56,500, with no homology to sequences in the data base. Unlike other PRP proteins or mammalian splicing factors, the sequence of PRP19 has no discernible motif. Immunoprecipitation studies showed that PRP19 is associated with the spliceosome during the splicing reaction. Although the exact function of PRP19 remains unknown, PRP19 appears to be distinct from the other PRP proteins or other spliceosomal components.

scholarly journals Structure of human nucleosome containing the testis-specific histone variant TSH2B

2014 ◽  
Vol 70 (4) ◽  
pp. 444-449 ◽  
Author(s):  
Takashi Urahama ◽  
Naoki Horikoshi ◽  
Akihisa Osakabe ◽  
Hiroaki Tachiwana ◽  
Hitoshi Kurumizaka
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Structural Changes ◽  
Structural Difference ◽  
Histone Variants ◽  
The Other ◽  
Human Testis ◽  
Amino Acid Residues ◽  
Histone H2b ◽  
Specific Amino Acid

The human histone H2B variant TSH2B is highly expressed in testis and may function in the chromatin transition during spermatogenesis. In the present study, the crystal structure of the human testis-specific nucleosome containing TSH2B was determined at 2.8 Å resolution. A local structural difference between TSH2B and canonical H2B in nucleosomes was detected around the TSH2B-specific amino-acid residue Ser85. The TSH2B Ser85 residue does not interact with H4 in the nucleosome, but in the canonical nucleosome the H2B Asn84 residue (corresponding to the TSH2B Ser85 residue) forms water-mediated hydrogen bonds with the H4 Arg78 residue. In contrast, the other TSH2B-specific amino-acid residues did not induce any significant local structural changes in the TSH2B nucleosome. These findings may provide important information for understanding how testis-specific histone variants form nucleosomes during spermatogenesis.

scholarly journals Structural Insights into the Subclass B3 Metallo-β-Lactamase SMB-1 and the Mode of Inhibition by the Common Metallo-β-Lactamase Inhibitor Mercaptoacetate

2012 ◽  
Vol 57 (1) ◽  
pp. 101-109 ◽  
Author(s):  
Jun-ichi Wachino ◽  
Yoshihiro Yamaguchi ◽  
Shigetarou Mori ◽  
Hiromasa Kurosaki ◽  
Yoshichika Arakawa ◽  
...  
Keyword(s):  
Amino Acid ◽  
Active Site ◽  
Hydrolytic Activity ◽  
The Other ◽  
Amino Acid Residues ◽  
Hydrogen Bond Interaction ◽  
Content Type ◽  
Carboxylate Oxygen ◽  
Wide Range ◽  
Environmental Bacteria

ABSTRACTA novel subclass B3 metallo-β-lactamase (MBL), SMB-1, recently identified from aSerratia marcescensclinical isolate, showed a higher hydrolytic activity against a wide range of β-lactams than did the other subclass B3 MBLs, i.e., BJP-1 and FEZ-1, from environmental bacteria. To identify the mechanism underlying the differences in substrate specificity among the subclass B3 MBLs, we determined the structure of SMB-1, using 1.6-Å diffraction data. Consequently, we found that SMB-1 reserves a space in the active site to accommodate β-lactam, even with a bulky R1 side chain, due to a loss of amino acid residues corresponding to F31 and L226 of BJP-1, which protrude into the active site to prevent β-lactam from binding. The protein also possesses a unique amino acid residue, Q157, which probably plays a role in recognition of β-lactams via the hydrogen bond interaction, which is missing in BJP-1 and FEZ-1, whoseKmvalues for β-lactams are particularly high. In addition, we determined the mercaptoacetate (MCR)-complexed SMB-1 structure and revealed the mode of its inhibition by MCR: the thiolate group bridges to two zinc ions (Zn1 and Zn2). One of the carboxylate oxygen atoms of MCR makes contact with Zn2 and Ser221, and the other makes contact with T223 and a water molecule. Our results demonstrate the possibility that MCR could be a potent inhibitor for subclass B3 MBLs and that the screening technique using MCR as an inhibitor would be effective for detecting subclass B3 MBL producers.

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