Proteolytic specificity of chicken cathepsin L on bovine β-casein

1988 ◽  
Vol 8 (2) ◽  
pp. 185-191 ◽  
Author(s):  
Eric Dufour ◽  
Bruno Ribadeau-Dumas
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Cathepsin L ◽  
Amino Acid Residues ◽  
Rp Hplc ◽  
Peptide Mixtures ◽  
Scissile Bond

The proteolytic specificity of chicken cathepsin L was studied using bovine β-casein as substrate. The peptide mixtures obtained after various times of hydrolysis were separated by RP-HPLC and ten peptides were identified. Chicken cathepsin L accepts proline residues in all positions except P1′. Looking at the amino acid residues on the amino side of the scissile bond we found three times the Tyr-Pro pair at P1′–P2′ positions and that the S1′ subsite can interact with modified amino acids such as phosphoserine.

The C-terminal sequence of amino acid residues of κ-casein isolated from buffalo's milk

1967 ◽  
Vol 34 (1) ◽  
pp. 85-88 ◽  
Author(s):  
M. H. Abd El-Salam ◽  
W. Manson
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Peptide Chain ◽  
Amino Acid Residues ◽  
Terminal Sequence ◽  
Carboxypeptidase A ◽  
Phosphorous Content ◽  
Single Peptide

SummaryWhen κ-casein from buffalo's milk was treated with carboxypeptidase A (EC 3. 4. 2. 1),4 amino acids, valine, threonine, serine and alanine were released from the protein in a manner consistent with the view that they originate in the C-terminal sequence of a single peptide chain. The amounts produced suggest a minimum molecular weight for buffalo κ-casein of approximately 17000, in agreement with the value calculated from the phosphorous content on the basis of the presence of 2 phosphorus atoms/molecule. A comparison is made with the C-terminal sequence reported for bovine κ-casein.

Structural characterization of folded and extended conformations in peptides containing γ amino acids with proteinogenic side chains: crystal structures of γn, (αγ)n and γγδγ sequences

2015 ◽  
Vol 39 (5) ◽  
pp. 3319-3326 ◽  
Author(s):  
Madhusudana M. B. Reddy ◽  
K. Basuroy ◽  
S. Chandrappa ◽  
B. Dinesh ◽  
B. Vasantha ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Crystal Structures ◽  
Structural Characterization ◽  
Side Chains ◽  
Amino Acid Residues

γn amino acid residues can be incorporated into structures in γn and hybrid sequences containing folded and extended α and δ residues.

scholarly journals SLC6A14, a Pivotal Actor on Cancer Stage: When Function Meets Structure

2019 ◽  
Vol 24 (9) ◽  
pp. 928-938 ◽  
Author(s):  
Luca Palazzolo ◽  
Chiara Paravicini ◽  
Tommaso Laurenzi ◽  
Sara Adobati ◽  
Simona Saporiti ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Amino Acids ◽  
Amino Acid ◽  
Molecular Dynamics Simulations ◽  
Electrostatic Interactions ◽  
Amino Acid Residues ◽  
Dibasic Amino Acid ◽  
Novel Target ◽  
Function Relationship ◽  
Dynamics Simulations

SLC6A14 (ATB0,+) is a sodium- and chloride-dependent neutral and dibasic amino acid transporter that regulates the distribution of amino acids across cell membranes. The transporter is overexpressed in many human cancers characterized by an increased demand for amino acids; as such, it was recently acknowledged as a novel target for cancer therapy. The knowledge on the molecular mechanism of SLC6A14 transport is still limited, but some elegant studies on related transporters report the involvement of the 12 transmembrane α-helices in the transport mechanism, and describe structural rearrangements mediated by electrostatic interactions with some pivotal gating residues. In the present work, we constructed a SLC6A14 model in outward-facing conformation via homology modeling and used molecular dynamics simulations to predict amino acid residues critical for substrate recognition and translocation. We docked the proteinogenic amino acids and other known substrates in the SLC6A14 binding site to study both gating regions and the exposed residues involved in transport. Interestingly, some of these residues correspond to those previously identified in other LeuT-fold transporters; however, we could also identify a novel relevant residue with such function. For the first time, by combined approaches of molecular docking and molecular dynamics simulations, we highlight the potential role of these residues in neutral amino acid transport. This novel information unravels new aspects of the human SLC6A14 structure–function relationship and may have important outcomes for cancer treatment through the design of novel inhibitors of SLC6A14-mediated transport.

scholarly journals Hyaluronan-binding region of aggrecan from pig laryngeal cartilage. Amino acid sequence, analysis of N-linked oligosaccharides and location of the keratan sulphate

1992 ◽  
Vol 286 (3) ◽  
pp. 761-769 ◽  
Author(s):  
F P Barry ◽  
J U Gaw ◽  
C N Young ◽  
P J Neame
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Signal Peptidase ◽  
Amino Acid Residues ◽  
Terminal Sequence ◽  
Binding Region ◽  
Keratan Sulphate ◽  
Laryngeal Cartilage ◽  
Hyaluronan Binding

The hyaluronan-binding region (HABR) was prepared from pig laryngeal cartilage aggrecan and the amino acid sequence was determined. The HABR had two N-termini: one N-terminal sequence was Val-Glu-Val-Ser-Glu-Pro (367 amino acids in total), and a second N-terminal sequence (Ala-Ile-Ser-Val-Glu-Val; 370 amino acids in total) was found to arise due to alternate cleavage by the signal peptidase. The N-linked oligosaccharides were analysed by examining their reactivity with a series of lectins. It was found that the N-linked oligosaccharide on loop A was of the mannose type, while that on loop B was of the complex type. No reactivity was detected between the N-linked oligosaccharide on loop B' and any of the lectins. The location of keratan sulphate (KS) in the HABR was determined by Edman degradation of the immobilized KS-containing peptide. The released amino acid derivatives were collected and tested for the presence of epitope to antibody 5-D-4. On the basis of 5-D-4 reactivity and sequencing yields, the KS chains are attached to threonine residues 352 and 357. There is no KS at threonine-355. This site is not in fact in G1, but about 16 amino acid residues into the interglobular domain. Comparison of the structure of the KS chain from the HABR and from the KS domain of pig laryngeal cartilage aggrecan was made by separation on polyacrylamide gels of the oligosaccharides arising from digestion with keratanase. Comparison of the oligosaccharide maps suggests that the KS chains from both parts of the aggrecan molecule have the same structure.

ChemInform Abstract: β-Nitro-α-amino Acids as Latent α,β-Dehydro-α-amino Acid Residues in Peptides.

ChemInform ◽  
2010 ◽  
Vol 30 (34) ◽  
pp. no-no
Author(s):  
Phillip A. Coghlan ◽  
Christopher J. Easton
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Residues

RP-HPLC Determination of Tiger Nut and Orgeat Amino Acid Contents

2005 ◽  
Vol 11 (1) ◽  
pp. 33-40 ◽  
Author(s):  
L. Bosch ◽  
A. Alegría ◽  
R. Farré
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Profile ◽  
African Origin ◽  
Rp Hplc ◽  
Precision And Accuracy ◽  
Amino Acid Contents ◽  
Tiger Nuts ◽  
Abundant Amino Acid

The amino acid profile of 11 samples of tiger nuts ( Cyperus esculentusL.) grown in the area of “L'Horta Nord” in Valencia (Spain) and one sample of African origin were determined, along with the amino acid contents of 10 samples of natural orgeat from Valencia. Protein was hydrolysed by hydrochloric acid at 110 °C for 23 h, and amino acids were derivatised with AQC and determined by RP-HPLC with fluorescence detection. The chromatographic conditions were optimised. The analytical parameters (detection and quantification limits, precision and accuracy) showed the method to be sufficiently sensitive and reproducible for determining amino acids resistant to acid hydrolysis in tiger nuts and orgeat. Arginine was the most abundant amino acid in both tiger nuts and orgeat and the lowest contents corresponding to histidine and tyrosine. The essential amino acid contents of tiger nuts and orgeat protein were greater than those proposed in the protein standard for adults by the FAO/WHO, with the exception of histidine. No significant differences were found among the arginine, lysine and isoleucine amino acid contents in tiger nuts from Valencia, Alboraya and Alm‡ssera; nor were they found among amino acids in tiger nuts from Valencia and Alm‡ssera, with the exception of tyrosine.

MAPRes: Mining association patterns among preferred amino acid residues in the vicinity of amino acids targeted for post-translational modifications

PROTEOMICS ◽  
2008 ◽  
Vol 8 (10) ◽  
pp. 1954-1958 ◽  
Author(s):  
Ishtiaq Ahmad ◽  
Wajahat M. Qazi ◽  
Ahmed Khurshid ◽  
Munir Ahmad ◽  
Daniel C. Hoessli ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Residues ◽  
Association Patterns ◽  
Post Translational Modifications

Targeting motifs and functional parameters governing the assembly of connexins into gap junctions

2000 ◽  
Vol 349 (1) ◽  
pp. 281-287 ◽  
Author(s):  
Patricia E. M. MARTIN ◽  
James STEGGLES ◽  
Claire WILSON ◽  
Shoeb AHMAD ◽  
W. Howard EVANS
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Gap Junctions ◽  
Gap Junction ◽  
Mammalian Cells ◽  
Fluorescent Protein ◽  
Lucifer Yellow ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Green Fluorescent

To study the assembly of gap junctions, connexin-green-fluorescent-protein (Cx-GFP) chimeras were expressed in COS-7 and HeLa cells. Cx26- and Cx32-GFP were targeted to gap junctions where they formed functional channels that transferred Lucifer Yellow. A series of Cx32-GFP chimeras, truncated from the C-terminal cytoplasmic tail, were studied to identify amino acid sequences governing targeting from intracellular assembly sites to the gap junction. Extensive truncation of Cx32 resulted in failure to integrate into membranes. Truncation of Cx32 to residue 207, corresponding to removal of most of the 78 amino acids on the cytoplasmic C-terminal tail, led to arrest in the endoplasmic reticulum and incomplete oligomerization. However, truncation to amino acid 219 did not impair Cx oligomerization and connexon hemichannels were targeted to the plasma membrane. It was concluded that a crucial gap-junction targeting sequence resides between amino acid residues 207 and 219 on the cytoplasmic C-terminal tail of Cx32. Studies of a Cx32E208K mutation identified this as one of the key amino acids dictating targeting to the gap junction, although oligomerization of this site-specific mutation into hexameric hemichannels was relatively unimpaired. The studies show that expression of these Cx-GFP constructs in mammalian cells allowed an analysis of amino acid residues involved in gap-junction assembly.

Two-dimensional classification of amphiphilic monomers based on interfacial and partitioning properties. 2. Amino acids and amino acid residues

2006 ◽  
Vol 284 (6) ◽  
pp. 575-585 ◽  
Author(s):  
Ivan M. Okhapkin ◽  
Andrei A. Askadskii ◽  
Vladimir A. Markov ◽  
Elena E. Makhaeva ◽  
Alexei R. Khokhlov
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Two Dimensional ◽  
Amino Acid Residues ◽  
Dimensional Classification
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