Identification and in silico structural and functional analysis of a trypsin-like protease from shrimp 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 hepatopancreas tissue by the 3'RACE techniqu...

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Published in:PeerJ (San Francisco, CA) CA), 2020-04, Vol.8, p.e9030-e9030, Article e9030
Main Authors: Viader-Salvadó, José M, Aguilar Briseño, José Alberto, Gallegos-López, Juan A, Fuentes-Garibay, José A, Alvarez-González, Carlos Alfonso, Guerrero-Olazarán, Martha
Format: Article
Language:English
Subjects:
Amino acid sequence
Amino acids
Aquaculture, Fisheries and Fish Science
Biochemistry
Bioinformatics
Brachyurins
Collagen
Computational Biology
Decapoda
Deoxyribonucleic acid
DNA
DNA polymerase
E coli
Hepatopancreas
Litopenaeus vannamei
Macrobrachium carcinus
Macrobrachium rosenbergii
Nucleotides
Peptides
Physiology
Plasmids
Proenzymes
Proteinase
Proteins
Serine
Serine proteases
Structure-function relationships
Substrate specificity
Threonine proteases
Trypsin
Trypsin-like protease
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Summary:(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 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 The trypsin-like protease sequence showed a global sequence identity of 94% with an unpublished trypsin from (GenBank accession no. AMQ98968), and only 57% with 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.
ISSN:2167-8359
2167-8359
DOI:10.7717/peerj.9030