scholarly journals Cysteine in Broiler Poultry Nutrition

2021 ◽  
Author(s):  
Iyakutye Jacob Nte ◽  
Hollinshead Holly Gunn
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequences ◽  
Broiler Chicks ◽  
Feed Ingredients ◽  
Amino Acid Requirements ◽  
Protein Amino Acids ◽  
Poultry Diets ◽  
Soya Bean Meal ◽  
And Function

The SAAs are limiting in the major poultry feed ingredients, ranking first and fifth in soya bean meal and maize, respectively. Feed ingredients rich in protein, in particular and other nutrients, enhance Energy supply and protein accretion. Modern commercial broilers have reduced maintenance needs and high amino acid requirements, and are more responsive to protein (amino acids) than energy. Cysteine is a semi-essential amino acid belonging to the SAAs. It plays essential roles in protein synthesis, structure and function, causing growth depressing effects in broiler chicks when there is methionine:cysteine imbalance. Genetically predetermined amino acid sequences in proteins are essential for production of adequate quantities of meat, milk and eggs. Therefore, ideal amino acid ratios which conform to the requirements of broilers should be utilized. In nutrition, amino acids are equivalent to proteins, hence the shift in focus from proteins to individual amino acids, expressed as ideal ratios to lysine. The SAAs are practically relevant and have critical nutritional roles in animal nutrition with over 90% production being used to fortify animal (particularly poultry) diets. A balance in the methionine:cysteine ratio is necessary to ensure efficient utilization of the SAAs for proper growth and development in broiler poultry.

scholarly journals Roles of the C-Terminal Amino Acids of Non-Hexameric Helicases: Insights from Escherichia coli UvrD

2021 ◽  
Vol 22 (3) ◽  
pp. 1018
Author(s):  
Hiroaki Yokota
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Amino Acid ◽  
Single Molecule ◽  
Underlying Mechanism ◽  
Amino Acid Sequences ◽  
E Coli ◽  
X Ray Crystallography ◽  
Terminal Amino

Helicases are nucleic acid-unwinding enzymes that are involved in the maintenance of genome integrity. Several parts of the amino acid sequences of helicases are very similar, and these quite well-conserved amino acid sequences are termed “helicase motifs”. Previous studies by X-ray crystallography and single-molecule measurements have suggested a common underlying mechanism for their function. These studies indicate the role of the helicase motifs in unwinding nucleic acids. In contrast, the sequence and length of the C-terminal amino acids of helicases are highly variable. In this paper, I review past and recent studies that proposed helicase mechanisms and studies that investigated the roles of the C-terminal amino acids on helicase and dimerization activities, primarily on the non-hexermeric Escherichia coli (E. coli) UvrD helicase. Then, I center on my recent study of single-molecule direct visualization of a UvrD mutant lacking the C-terminal 40 amino acids (UvrDΔ40C) used in studies proposing the monomer helicase model. The study demonstrated that multiple UvrDΔ40C molecules jointly participated in DNA unwinding, presumably by forming an oligomer. Thus, the single-molecule observation addressed how the C-terminal amino acids affect the number of helicases bound to DNA, oligomerization, and unwinding activity, which can be applied to other helicases.

Effect of Intraduodenal Starch Infusion on Net Portal Absorption of Amino Acids in Growing steers Fed Lucerne

1994 ◽  
Vol 1994 ◽  
pp. 28-28
Author(s):  
C.J. Seal ◽  
D.S. Parker ◽  
J.C. MacRae ◽  
G.E. Lobley
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Gastrointestinal Tract ◽  
Protein Turnover ◽  
Portal Blood ◽  
Intestinal Lumen ◽  
Short Term ◽  
Net Uptake ◽  
Amino Acid Requirements ◽  
Glucose Availability

Amino acid requirements for energy metabolism and protein turnover within the gastrointestinal tract are substantial and may be met from luminal and arterial pools of amino acids. Several studies have demonstrated that the quantity of amino acids appearing in the portal blood does not balance apparent disappearance from the intestinal lumen and that changing diet or the availability of energy-yielding substrates to the gut tissues may influence the uptake of amino acids into the portal blood (Seal & Reynolds, 1993). For example, increased net absorption of amino acids was observed in animals receiving exogenous intraruminal propionate (Seal & Parker, 1991) and this was accompanied by changes in glucose utilisation by the gut tissues. In contrast, there was no apparent change in net uptake of [l-13C]-leucine into the portal vein of sheep receiving short term intraduodenal infusions of glucose (Piccioli Cappelli et al, 1993). This experiment was designed to further investigate the effects on amino acid absorption of changing glucose availability to the gut with short term (seven hours) or prolonged (three days) exposure to starch infused directly into the duodenum.

scholarly journals BIOSYNTHESIS IN ISOLATED ACETABULARIA CHLOROPLASTS

1972 ◽  
Vol 54 (2) ◽  
pp. 279-294 ◽  
Author(s):  
David C. Shephard ◽  
Wendy B. Levin
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Technical Problems ◽  
Hydrolyzed Protein ◽  
Protein Amino Acids ◽  
Amino Acid Labeling ◽  
Labeling Pattern

The ability of chloroplasts isolated from Acetabulana mediterranea to synthesize the protein amino acids has been investigated. When this chloroplast isolate was presented with 14CO2 for periods of 6–8 hr, tracer was found in essentially all amino acid species of their hydrolyzed protein Phenylalanine labeling was not detected, probably due to technical problems, and hydroxyproline labeling was not tested for The incorporation of 14CO2 into the amino acids is driven by light and, as indicated by the amount of radioactivity lost during ninhydrin decarboxylation on the chromatograms, the amino acids appear to be uniformly labeled. The amino acid labeling pattern of the isolate is similar to that found in plastids labeled with 14CO2 in vivo. The chloroplast isolate did not utilize detectable amounts of externally supplied amino acids in light or, with added adenosine triphosphate (ATP), in darkness. It is concluded that these chloroplasts are a tight cytoplasmic compartment that is independent in supplying the amino acids used for its own protein synthesis. These results are discussed in terms of the role of contaminants in the observed synthesis, the "normalcy" of Acetabularia chloroplasts, the synthetic pathways for amino acids in plastids, and the implications of these observations for cell compartmentation and chloroplast autonomy.

scholarly journals The amino acid sequence of cytochromes c-551 from three species of Pseudomonas

1973 ◽  
Vol 131 (3) ◽  
pp. 485-498 ◽  
Author(s):  
R. P. Ambler ◽  
Margaret Wynn
Keyword(s):  
Amino Acids ◽  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Mitochondrial Cytochrome ◽  
Cytochromes C ◽  
Lending Library ◽  
Single Peptide

The amino acid sequences of the cytochromes c-551 from three species of Pseudomonas have been determined. Each resembles the protein from Pseudomonas strain P6009 (now known to be Pseudomonas aeruginosa, not Pseudomonas fluorescens) in containing 82 amino acids in a single peptide chain, with a haem group covalently attached to cysteine residues 12 and 15. In all four sequences 43 residues are identical. Although by bacteriological criteria the organisms are closely related, the differences between pairs of sequences range from 22% to 39%. These values should be compared with the differences in the sequence of mitochondrial cytochrome c between mammals and amphibians (about 18%) or between mammals and insects (about 33%). Detailed evidence for the amino acid sequences of the proteins has been deposited as Supplementary Publication SUP 50015 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973), 131, 5.

Inter-annual and seasonal dynamics of amino acid, mineral and vitamin composition of silver belly Leiognathus splendens

2014 ◽  
Vol 95 (4) ◽  
pp. 817-828 ◽  
Author(s):  
Kajal Chakraborty ◽  
Deepu Joseph
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Content ◽  
West Coast ◽  
Sensor Data ◽  
The South ◽  
Post Monsoon ◽  
South West ◽  
South West Coast ◽  
Protein Amino Acids

Silver bellies, Leiognathus splendens were studied for their spatial (south-west and south-east coasts of India), annual (2008–2011) and seasonal (pre-monsoon, monsoon and post-monsoon) variations of protein, amino acids, vitamins and minerals. The monthly mean Sea Viewing Wide Field-of-view Sensor data for the period from January 2008 to December 2011 were taken into account to indicate the distribution of the photosynthetic pigment chlorophyll-a to test the hypothesis that surface productivity might be related to nutritional biochemistry of this species. The four year average total protein content and chlorophyll-a showed good correlation during monsoon on the south-west coast and monsoon/post-monsoon on the south-east coast, suggesting that the protein content is prejudiced by the chlorophyll-a concentration. Amino acid scores observed monsoon maxima along the south-west and south-east coasts. Significant seasonal variations in vitamin content were observed at the study locations with high content of vitamins D3, E, K1 and C on the south-west coast. Na content was maximal during pre-monsoon on the south-west coast, while post-monsoon maxima of Ca and K content were observed. The Fe, Mn and Zn were abundant in the samples collected from the south-west coast. The concentration of Se exhibited maximum values post-monsoon along the south-west and south-east coasts. The present study demonstrated L. splendens as a valuable source of the protein, amino acids, minerals and vitamins, showing that this low-value species is a good source of well balanced proteins with high biological value to be qualified as a preferred healthy food for human consumption.

scholarly journals Functional Analysis of PA Binding by Influenza A Virus PB1: Effects on Polymerase Activity and Viral Infectivity

2001 ◽  
Vol 75 (17) ◽  
pp. 8127-8136 ◽  
Author(s):  
Daniel R. Perez ◽  
Ruben O. Donis
Keyword(s):  
Amino Acids ◽  
Influenza Virus ◽  
Amino Acid ◽  
Viral Replication ◽  
Influenza A Virus ◽  
Influenza A ◽  
Amino Acid Sequences ◽  
Influenza Viruses ◽  
Virus Growth ◽  
Transcription And Replication

ABSTRACT Influenza A virus expresses three viral polymerase (P) subunits—PB1, PB2, and PA—all of which are essential for RNA and viral replication. The functions of P proteins in transcription and replication have been partially elucidated, yet some of these functions seem to be dependent on the formation of a heterotrimer for optimal viral RNA transcription and replication. Although it is conceivable that heterotrimer subunit interactions may allow a more efficient catalysis, direct evidence of their essentiality for viral replication is lacking. Biochemical studies addressing the molecular anatomy of the P complexes have revealed direct interactions between PB1 and PB2 as well as between PB1 and PA. Previous studies have shown that the N-terminal 48 amino acids of PB1, termed domain α, contain the residues required for binding PA. We report here the refined mapping of the amino acid sequences within this small region of PB1 that are indispensable for binding PA by deletion mutagenesis of PB1 in a two-hybrid assay. Subsequently, we used site-directed mutagenesis to identify the critical amino acid residues of PB1 for interaction with PA in vivo. The first 12 amino acids of PB1 were found to constitute the core of the interaction interface, thus narrowing the previous boundaries of domain α. The role of the minimal PB1 domain α in influenza virus gene expression and genome replication was subsequently analyzed by evaluating the activity of a set of PB1 mutants in a model reporter minigenome system. A strong correlation was observed between a functional PA binding site on PB1 and P activity. Influenza viruses bearing mutant PB1 genes were recovered using a plasmid-based influenza virus reverse genetics system. Interestingly, mutations that rendered PB1 unable to bind PA were either nonviable or severely growth impaired. These data are consistent with an essential role for the N terminus of PB1 in binding PA, P activity, and virus growth.

Sequence and expression of the dCMP deaminase gene (DCD1) of Saccharomyces cerevisiae

1986 ◽  
Vol 6 (5) ◽  
pp. 1711-1721
Author(s):  
E M McIntosh ◽  
R H Haynes
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequences ◽  
Open Reading Frame ◽  
Northern Analysis ◽  
Hindiii Site ◽  
Reading Frame ◽  
Hindiii Restriction Site ◽  
Cycle Dependent

The dCMP deaminase gene (DCD1) of Saccharomyces cerevisiae has been isolated by screening a Sau3A clone bank for complementation of the dUMP auxotrophy exhibited by dcd1 dmp1 haploids. Plasmid pDC3, containing a 7-kilobase (kb) Sau3A insert, restores dCMP deaminase activity to dcd1 mutants and leads to an average 17.5-fold overproduction of the enzyme in wild-type cells. The complementing activity of the plasmid was localized to a 4.2-kb PvuII restriction fragment within the Sau3A insert. Subcloning experiments demonstrated that a single HindIII restriction site within this fragment lies within the DCD1 gene. Subsequent DNA sequence analysis revealed a 936-nucleotide open reading frame encompassing this HindIII site. Disruption of the open reading frame by integrative transformation led to a loss of enzyme activity and confirmed that this region constitutes the dCMP deaminase gene. Northern analysis indicated that the DCD1 mRNA is a 1.15-kb poly(A)+ transcript. The 5' end of the transcript was mapped by primer extension and appears to exhibit heterogeneous termini. Comparison of the amino acid sequence of the T2 bacteriophage dCMP deaminase with that deduced for the yeast enzyme revealed a limited degree of homology which extends over the entire length of the phage polypeptide (188 amino acids) but is confined to the carboxy-terminal half of the yeast protein (312 amino acids). A potential dTTP-binding site in the yeast and phage enzymes was identified by comparison of homologous regions with the amino acid sequences of a variety of other dTTP-binding enzymes. Despite the role of dCMP deaminase in dTTP biosynthesis, Northern analysis revealed that the DCD1 gene is not subject to the same cell cycle-dependent pattern of transcription recently found for the yeast thymidylate synthetase gene (TMP1).

scholarly journals The substrate specificity of adenosine 3′:5′-cyclic monophosphate-dependent protein kinase of rabbit skeletal muscle

1977 ◽  
Vol 162 (2) ◽  
pp. 411-421 ◽  
Author(s):  
S J Yeaman ◽  
P Cohen ◽  
D C Watson ◽  
G H Dixon
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Protein Kinase ◽  
Phosphorylation Site ◽  
Amino Acid Sequences ◽  
Beta Subunit ◽  
Alpha Subunit ◽  
Phosphorylase Kinase ◽  
Dependent Protein Kinase ◽  
Dependent Protein

The known amino acid sequences at the two sites on phosphorylase kinase that are phosphorylated by cyclic AMP-dependent protein kinase were extended. The sequences of 42 amino acids around the phosphorylation site on the alpha-subunit and of 14 amino acids around the phosphorylation site on the beta-subunit were shown to be: alpha-subunit Phe-Arg-Arg-Leu-Ser(P)-Ile-Ser-Thr-Glu-Ser-Glx-Pro-Asx-Gly-Gly-His-Ser-Leu-Gly-Ala-Asp-Leu-Met-Ser-Pro-Ser-Phe-Leu-Ser-Pro-Gly-Thr-Ser-Val-Phe(Ser,Pro,Gly)His-Thr-Ser-Lys; beta-subunit, Ala-Arg-Thr-Lys-Arg-Ser-Gly-Ser(P)-VALIle-Tyr-Glu-Pro-Leu-Lys. The sites on histone H2B which are phosphorylated by cyclic AMP-dependent protein kinase in vitro were identified as serine-36 and serine-32. The amino acid sequence in this region is: Lys-Lys-Arg-Lys-Arg-Ser32(P)-Arg-Lys-Glu-Ser36(P)-Tyr-Ser-Val-Tyr-Val- [Iwai, K., Ishikawa, K. & Hayashi, H. (1970) Nature (London) 226, 1056-1058]. Serine-36 was phosphorylated at 50% of the rate at which the beta-subunit of phosphorylase kinase was phosphorylated, and it was phosphorylated 6-7-fold more rapidly than was serine-32. The amino acid sequences when compared with those at the phosphorylation sites of other physiological substrates suggest that the presence of two adjacent basic amino acids on the N-terminal side of the susceptible serine residue may be critical for specific substrate recognition in vivo.

THE PROTEOLYTIC ACTIVITY OF INSULIN

1967 ◽  
Vol 45 (9) ◽  
pp. 1329-1333
Author(s):  
Michel Page ◽  
Claude Godin
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Proteolytic Activity ◽  
Protein Amino Acids

The action of insulin on hemoglobin at pH 7.5 was studied. Four different methods were used to determine the degree of proteolysis. After mixtures of hemoglobin and insulin were incubated for 2 hours, very little amino acid or peptide material was liberated from the proteins. As many amino acids are liberated from hemoglobin when it is incubated alone under the same conditions. It is concluded that autolysis is responsible for the observed increases in non-protein amino acids and that insulin has no proteolytic activity under the conditions used in this study.

Amino acids in blood plasma and tissues of rats following glucose force-feeding

1969 ◽  
Vol 47 (3) ◽  
pp. 323-327 ◽  
Author(s):  
J. E. Knipfel ◽  
H. G. Botting ◽  
F. J. Noel ◽  
J. M. McLaughlan
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Blood Plasma ◽  
Protein Composition ◽  
Tissue Uptake ◽  
Body Protein ◽  
Glucose Administration ◽  
Force Feeding ◽  
Amino Acid Requirements ◽  
Concentration Changes

Changes in plasma amino acid (PAA) concentrations effected by force-feeding glucose to rats were studied in two experiments. Attempts were made to relate PAA concentration changes to amino acid requirements, previous diet, time after feeding glucose, and composition of several body proteins. Distribution of 14C-lysine between blood and tissues was examined in an additional rat experiment. Previous diet did not affect the relative quantities of amino acids removed from plasma (PAA removal pattern) after glucose force-feeding. Minimal PAA concentrations occurred by 40 min after glucose administration. The PAA removal pattern was not distinctly related to either amino acid requirements or to any particular body protein composition. Results of administering 14C-lysine simultaneously with glucose indicated that decreased plasma 14C-lysine levels were caused by increased tissue uptake of 14C, likely mediated by insulin. Muscle acted as the major recipient of 14C from plasma, with liver a lesser and more dynamic reservoir of 14C accumulation. Work is continuing to further clarify the significance of the PAA removal pattern, caused by the force-feeding of glucose.

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