In:
Recent Patents on Biotechnology, Bentham Science Publishers Ltd., Vol. 15, No. 4 ( 2021-12), p. 286-301
Abstract:
L-Methioninase (EC 4.4.1.11; MGL) is a pyridoxal
phosphate (PLP)-dependent enzyme that is produced by a variety of bacteria, fungi, and plants. L-methioninase, especially from Pseudomonas and Citrobacter
sp., is considered as the efficient therapeutic enzyme, particularly in cancers such as glioblastomas, medulloblastoma, and neuroblastoma that are more sensitive to
methionine starvation. Objective: The low stability is one of the main drawbacks of the enzyme; in this regard, in the current study, different features of the enzyme,
including phylogenetic, functional, and structural from Pseudomonas, Escherichia, Clostridium, and Citrobacter strains were evaluated to find the best
bacterial L-Methioninase. Methods: After the initial screening of L-Methioninase sequences from the
above-mentioned bacterial strains, the three-dimensional structures of enzymes from Escherichia fergusonii, Pseudomonas fluorescens, and Clostridium homopropionicum
were determined through homology modeling via GalaxyTBM server and refined by GalaxyRefine server. Results & Conclusion: Afterwards, PROCHECK, verify 3D, and ERRAT
servers were used for verification of the obtained models. Moreover, antigenicity, allergenicity, and physico-chemical analysis of enzymes were also carried
out. In order to get insight into the interaction of the enzyme with other proteins, the STRING server was used. The secondary structure of the enzyme is mainly
composed of random coils and alpha-helices. However, these outcomes should further be validated by wet-lab investigations.
Type of Medium:
Online Resource
ISSN:
1872-2083
DOI:
10.2174/1872208315666210910091438
Language:
English
Publisher:
Bentham Science Publishers Ltd.
Publication Date:
2021
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