Amino acid sequence around the histidine residue of the .alpha.-lytic protease of Sorangium species, a bacterial homolog of the pancreatic serine proteases

1967 ◽  
Vol 89 (13) ◽  
pp. 3350-3352 ◽  
Author(s):  
Lawrence B. Smillie ◽  
Donald R. Whitaker
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Serine Proteases ◽  
Histidine Residue ◽  
Bacterial Homolog

scholarly journals Analysis of Htra Gene from Zebrafish (Danio Rerio)

2015 ◽  
Vol 10 (2) ◽  
Author(s):  
M. Murwantoko ◽  
Chio Oka ◽  
Masashi Kawaichi
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Danio Rerio ◽  
Serine Proteases ◽  
Catalytic Domain ◽  
Fruit Fly ◽  
Wide Range ◽  
Igf Binding ◽  
Bacterial Homolog

HtrA which is characterized by the combination of a trypsin-like catalytic domain with at least one C-terminalPDZ domain is a highly conserved family of serine proteases found in a wide range of organisms. However theidentified HtrA family numbers varies among spesies, for example the number of mammalian, Eschericia coli,fruit fly-HtrA family are 4, 3 and 1 gene respectively. One gene is predicted exist in zebrafish. Since no completeinformation available on zebrafish HtrA, in this paper zebrafish HtrA (zHtrA) gene was analyzed. The zHtrA isbelonged to HtrA1 member and predicted encodes 478 amino acids with a signal peptide, a IGF binding domain,a Kazal-type inhibitor domain in the up stream of HtrA-bacterial homolog. At the amino acid sequence the zHtrA1showed the 69%, 69%, 68%, 54% and 54% with the rat HtrA1, mouse HtrA1, human HtrA1, human HtrA3 andmouse HtrA4 respectively. The zHtrA1 is firstly expressed at 60 hpf and mainly in the vertebral rudiments in thetail region.

Determination of Factor Xa Activity by Means of Chromogenic Substrates Based on the Primary Structure of Prothrombin

1975 ◽  
Author(s):  
L. Aurell ◽  
A. Olausson ◽  
G. Claeson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Serine Proteases ◽  
Factor Xa ◽  
Amino Acid Sequences ◽  
Peptide Substrate ◽  
Chromogenic Substrates ◽  
Special Regard

Through the work of Magnusson and co-workers leading to the elucidation of the primary structure of prothrombin including the amino acid sequences around the two bonds split by factor Xa it has been possible to design a synthetic chromogenic peptide substrate. Bz-Ile-Glu-Gly-Arg-pNA, specifically intended for the determination of factor Xa. Furthermore, additional substrates have been synthezised with various alterations in the amino acid sequence. The activity of factor Xa and other serine proteases within the coagulation and fibrinolytic systems towards these substrates will be discussed with special regard to their possible use in coagulation studies.

Cl̄r and Cl̄s subcomponents of human complement: Two serine proteinases lacking the ‘histidine-loop’ disulphide bridge

1981 ◽  
Vol 1 (10) ◽  
pp. 779-784 ◽  
Author(s):  
Gerard J. Arlaud ◽  
Jean Gagnon
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Histidine Residue ◽  
Serine Proteinases ◽  
Human Complement ◽  
Disulphide Bridge ◽  
Terminal Amino Acid ◽  
Relay System ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence

The N-terminal amino acid sequence of human Cl̄s b chain has been extended to 52 residues. The histidine residue involved in the charge-relay system is located at position 38, whereas the ‘histidine-loop’ disulphide bridge is missing. So far, human complement subcomponents Cl̄s are the only known mammalian serine proteinases lacking this disulphide bridge.

scholarly journals Identification and in silico structural and functional analysis of a trypsin-like protease from shrimp Macrobrachium carcinus

PeerJ ◽  
2020 ◽  
Vol 8 ◽  
pp. e9030 ◽  
Author(s):  
José M. Viader-Salvadó ◽  
José Alberto Aguilar Briseño ◽  
Juan A. Gallegos-López ◽  
José A. Fuentes-Garibay ◽  
Carlos Alfonso Alvarez-González ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Serine Proteases ◽  
Macrobrachium Rosenbergii ◽  
Catalytic Triad ◽  
Activation Mechanism ◽  
Collagenolytic Activity ◽  
Sequence Motif ◽  
Bioinformatics Analyses ◽  
Race Technique

Macrobrachium carcinus (Linnaeus, 1758) is a species of freshwater shrimp widely distributed from Florida southwards to southern Brazil, including southeast of Mexico. In the present work, we identified a putative trypsin-like protease cDNA fragment of 736 nucleotides from M. carcinus hepatopancreas tissue by the 3′RACE technique and compared the deduced amino acid sequence to other trypsin-related proteases to describe its structure and function relationship. The bioinformatics analyses showed that the deduced amino acid sequence likely corresponds to a trypsin-like protease closely related to brachyurins, which comprise a subset of serine proteases with collagenolytic activity found in crabs and other crustacea. The M. carcinus trypsin-like protease sequence showed a global sequence identity of 94% with an unpublished trypsin from Macrobrachium rosenbergii (GenBank accession no. AMQ98968), and only 57% with Penaeus vannamei trypsin (GenBank accession no. CAA60129). A detailed analysis of the amino acid sequence revealed specific differences with crustacean trypsins, such as the sequence motif at the beginning of the mature protein, activation mechanism of the corresponding zymogen, amino acid residues of the catalytic triad and residues responsible for substrate specificity.

scholarly journals Protease B of the lysosomelike vacuole of the yeast Saccharomyces cerevisiae is homologous to the subtilisin family of serine proteases.

1987 ◽  
Vol 7 (12) ◽  
pp. 4390-4399 ◽  
Author(s):  
C M Moehle ◽  
R Tizard ◽  
S K Lemmon ◽  
J Smart ◽  
E W Jones
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Serine Proteases ◽  
Proteinase K ◽  
Yeast Saccharomyces Cerevisiae ◽  
Amino Terminal ◽  
Protease B ◽  
Mature Protease

The PRB1 gene of Saccharomyces cerevisiae encodes the vacuolar endoprotease protease B. We have determined the DNA sequence of the PRB1 gene and the amino acid sequence of the amino terminus of mature protease B. The deduced amino acid sequence of this serine protease shares extensive homology with those of subtilisin, proteinase K, and related proteases. The open reading frame of PRB1 consists of 635 codons and, therefore, encodes a very large protein (molecular weight, greater than 69,000) relative to the observed size of mature protease B (molecular weight, 33,000). Examination of the gene sequence, the determined amino-terminal sequence, and empirical molecular weight determinations suggests that the preproenzyme must be processed at both amino and carboxy termini and that asparagine-linked glycosylation occurs at an unusual tripeptide acceptor sequence.

scholarly journals Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli

1992 ◽  
Vol 288 (2) ◽  
pp. 649-655 ◽  
Author(s):  
N Ioannidis ◽  
C E Cooper ◽  
R K Poole
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Spectroscopic Studies ◽  
Oxygen Binding ◽  
Histidine Residue ◽  
Nitrosyl Complex ◽  
Sds Page ◽  
Prosthetic Groups

The Escherichia coli haemoglobin-like flavohaemoprotein (Hmp) has been purified to near homogeneity using two chromatographic steps. The prosthetic groups are identified as FAD and protohaem IX. SDS/PAGE has indicated a molecular mass of 44 kDa for the monomeric protein consistent with the amino-acid sequence deduced from the hmp+ gene. The protein, as isolated, is in the Fe(III) state, exhibiting absorbance maxima at 403.5, 540 (shoulder) and 627 nm. The ferrous and carbonmonoxyferrous states resemble those of haemoglobin, showing maxima at 431.5 and 558 nm, and 421, 542 and 566 nm respectively. Upon aerobic addition of NAD(P)H, the ferric state is reduced to the oxygenated Fe(II) state, characterized by maxima at 413, 544 and 580 nm. This oxy form is not stable and slowly decays to the ferric state. Addition of dithionite and nitrite to the ferric protein results in the formation of a nitrosyl complex, whose e.p.r. characteristics indicate that the b-type haem is attached to the protein through a nitrogenous ligand, probably originating from a histidine residue.

scholarly journals Molecular and immunological characterization and IgE epitope mapping of Pen n 18, a major allergen of Penicillium notatum

2002 ◽  
Vol 363 (3) ◽  
pp. 707-715 ◽  
Author(s):  
Chia-Jung YU ◽  
Yen-Ming CHEN ◽  
Song-Nan SU ◽  
Farhad FOROUHAR ◽  
Shu-Hua LEE ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Serine Proteases ◽  
Major Allergen ◽  
Penicillium Notatum ◽  
Ige Binding ◽  
Acid Protein ◽  
Binding Epitope ◽  
Cross Inhibition ◽  
Amino Acid Protein

The mould genus, Penicillium, is a significant source of environmental aero-allergens. A major allergen from Penicillium notatum, Pen n 18, was identified by two-dimensional immunoblotting using monoclonal antibody G11A10, raised against the vacuolar serine protease of Penicillium citrinum, followed by matrix-assisted laser-desorption ionization—time-of-flight MS analysis of the peptide digest. Pen n 18 was then cloned and the amino acid sequence deduced from the cDNA sequence. The cDNA encoded a 494 amino acid protein, considerably larger than mature Pen n 18, the differences being due to the N- and C-terminal prosequences. The deduced amino acid sequence showed extensive similarity with those of vacuolar serine proteases from various fungi. The Pen n 18 coding sequence was expressed in Escherichia coli as a His-tagged fusion protein and purified by Ni2+-chelate affinity chromatography. On immunoblots, the purified recombinant protein specifically bound IgE from mould-allergic patients, and cross-inhibition assays demonstrated the presence of common IgE-binding epitopes on Pen n 18 and a major allergen of P. citrinum, Pen c 18. When mapping of the allergenic epitopes was performed, at least nine different linear IgE-binding epitopes, located throughout the Pen n 18 protein, were identified. Of these, peptide C12, located in the N-terminal region of the molecule, was recognized by serum from 75% of the patients tested and therefore appears to be an immunodominant IgE-binding epitope.

Amino acid sequence of rat submaxillary tonin reveals similarities to serine proteases

Nature ◽  
1984 ◽  
Vol 307 (5951) ◽  
pp. 555-558 ◽  
Author(s):  
Claude Lazure ◽  
Richard Leduc ◽  
Nabil G. Seidah ◽  
Gaétan Thibault ◽  
Jacques Genest ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Serine Proteases
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