Discovery of two transglutaminases derived from same zymogen for the <i>Streptomyces hygroscopicus</i> and analysis of their formation processes

Cui, Wenjing; Yang, Xiaoyan; Fang, Yueqin; Zhou, Shengmin; Liu, Song; Du, Guocheng; Du, Kun; Chen, Jian; Tao, Guanjun; Zhou, Zhemin

doi:10.1002/jsfa.5956

Cited by 4 publications

(2 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Unfortunately, protein accumulation mediated by cetyltrimethyl ammonium bromide precipitation was not sufficient to show a protease band [33]. In addition, auto‐activation was observed in S. hygroscopicus , thus showing cysteine protease activity of Sh MTG [37]. Auto‐processed Sh MTG was active but could not activate the MTG zymogen.…”

Section: Production Of Transglutaminase By Streptomyces Bacteriamentioning

confidence: 99%

Approaching transglutaminase from Streptomyces bacteria over three decades

Fuchsbauer

2021

The FEBS Journal

View full text Add to dashboard Cite

Transglutaminases are protein cross-linking and protein modifying enzymes that have attracted considerable interest due to their causal involvement in various diseases and versatility in industrial applications. In particular, microbial transglutaminases (MTG) from Streptomyces bacteria have managed in recent years to evolve from simple food additives to specialized enzymes for the sitedirected modification of therapeutic proteins. The review summarizes relevant studies from the beginning dealing with the occurrence, production, structure, catalysis, and substrate molecules of MTG enzymes. It also addresses biotechnological procedures with MTG from S. mobaraensis (SmMTG) as the most prominent representative in focus. Reassessment of the available data revealed unexpected insights into catalysis of SmMTG and other transglutaminases, suggesting selection of glutamine donor proteins by subsites at the front vestibule and the existence of distinct lysine pockets.Flexibility of the SmMTG-accessible glutamine donor substrate regions seems to be more important than the glutamine environment. Nevertheless, residues in close vicinity to glutamines also determine interaction with the SmMTG subsites. The apparent lack of subsites for lysine donor proteins suggests self-assembly of the substrate proteins prior to enzymatic cross-linking. The study of natural substrate proteins, especially their mutual interaction, is proposed to further illuminate catalysis of SmMTG. To this end, structure and function of the characterized substrate proteins from S. mobaraensis are discussed in conclusion.

show abstract

Section: Production Of Transglutaminase By Streptomyces Bacteriamentioning

confidence: 99%

Approaching transglutaminase from Streptomyces bacteria over three decades

Fuchsbauer

2021

The FEBS Journal

View full text Add to dashboard Cite

show abstract

“…1) Many useful enzymes have also been found in and purified from Streptomyces species: for example, xylanase, chitinase, tannase, lignin peroxidase, and transglutaminase. [2][3][4][5][6][7][8] Moreover, these enzymes have showed potential for industrial application. Xylanase has already been used in the paper industry for subsequent treatment of kraft pulp to reduce the use of harsh chemicals.…”

mentioning

confidence: 99%

Development of nitrilase promoter-derived inducible vectors for Streptomyces

Matsumoto

Hashimoto

Saitoh

et al. 2016

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

An inducible expression vector, pSH19, which harbors regulatory expression system PnitA-NitR, for streptomycetes was constructed previously. Here, we have modified pSH19 to obtain shuttle vectors for Streptomyces-E. coli by introducing the replication origin of a plasmid for E. coli (ColE1) and an antibiotic-resistant gene. Six inducible shuttle vectors, pESH19cF, pESH19cR, pESH19kF, pESH19kR, pESH19aF, and pESH19aR, for Streptomyces-E. coli, were successfully developed. The stability of these vectors was examined in five different E. coli strains and Streptomyces lividans TK24. The stability test showed that the pSH19-derived shuttle vectors were stable in E. coli Stbl2 and S. lividans TK24. Heterologous expression experiments involving each of the catechol 2,3-dioxygenase, nitrilase, and N-substituted formamide deformylase genes as a reporter gene showed that pESH19cF, pESH19kF, and pESH19aF possess inducible expression ability in S. lividans TK24. Thus, these vectors were found to be useful expression tools for experiments on both Gram-negative and Gram-positive bacterial genes.

show abstract