Tricorn Protease in Bacteria: Characterization of the Enzyme from Streptomyces coelicolor

2001 ◽  
Vol 382 (3) ◽  
Author(s):  
Noriko Tamura ◽  
Günther Pfeifer ◽  
Wolfgang Baumeister ◽  
Tomohiro Tamura
Keyword(s):  
Streptomyces Coelicolor

Cloning and characterization of the histidine biosynthetic gene cluster of Streptomyces coelicolor A3(2)

Gene ◽  
1990 ◽  
Vol 90 (1) ◽  
pp. 31-41 ◽  
Author(s):  
Danila Limauro ◽  
Alessandra Avitabile ◽  
Carmela Cappellano ◽  
Anna Maria Puglia ◽  
Carmelo B. Bruni
Keyword(s):  
Gene Cluster ◽  
Streptomyces Coelicolor ◽  
Biosynthetic Gene Cluster ◽  
Biosynthetic Gene

scholarly journals Development and application of versatile high density microarrays for genome-wide analysis of Streptomyces coelicolor: characterization of the HspR regulon

2009 ◽  
Vol 10 (1) ◽  
pp. R5 ◽  
Author(s):  
Giselda Bucca ◽  
Emma Laing ◽  
Vassilis Mersinias ◽  
Nicholas Allenby ◽  
Douglas Hurd ◽  
...  
Keyword(s):  
Streptomyces Coelicolor ◽  
High Density ◽  
Genome Wide Analysis ◽  
Genome Wide

Expression and characterization of the processive exo-β-1,4-cellobiohydrolase SCO6546 from Streptomyces coelicolor A(3)

2018 ◽  
Vol 58 (4) ◽  
pp. 310-321 ◽  
Author(s):  
Chang-Ro Lee ◽  
Won-Jae Chi ◽  
Ju-Hyeon Lim ◽  
Vijayalakshmi Dhakshnamoorthy ◽  
Soon-Kwang Hong
Keyword(s):  
Streptomyces Coelicolor

scholarly journals Preliminary Characterization of a Ni2+-Activated and Mycothiol-Dependent Glyoxalase I Enzyme from Streptomyces coelicolor

Inorganics ◽  
2019 ◽  
Vol 7 (8) ◽  
pp. 99 ◽  
Author(s):  
Uthaiwan Suttisansanee ◽  
John F. Honek
Keyword(s):  
Leishmania Major ◽  
Homo Sapiens ◽  
Streptomyces Coelicolor ◽  
Glyoxalase I ◽  
Glyoxalase System ◽  
Genetic Studies ◽  
Preliminary Characterization ◽  
Glyoxalase Ii ◽  
Activation Profile

The glyoxalase system consists of two enzymes, glyoxalase I (Glo1) and glyoxalase II (Glo2), and converts a hemithioacetal substrate formed between a cytotoxic alpha-ketoaldehyde, such as methylglyoxal (MG), and an intracellular thiol, such as glutathione, to a non-toxic alpha-hydroxy acid, such as d-lactate, and the regenerated thiol. Two classes of Glo1 have been identified. The first is a Zn2+-activated class and is exemplified by the Homo sapiens Glo1. The second class is a Ni2+-activated enzyme and is exemplified by the Escherichia coli Glo1. Glutathione is the intracellular thiol employed by Glo1 from both these sources. However, many organisms employ other intracellular thiols. These include trypanothione, bacillithiol, and mycothiol. The trypanothione-dependent Glo1 from Leishmania major has been shown to be Ni2+-activated. Genetic studies on Bacillus subtilis and Corynebacterium glutamicum focused on MG resistance have indicated the likely existence of Glo1 enzymes employing bacillithiol or mycothiol respectively, although no protein characterizations have been reported. The current investigation provides a preliminary characterization of an isolated mycothiol-dependent Glo1 from Streptomyces coelicolor. The enzyme has been determined to display a Ni2+-activation profile and indicates that Ni2+-activated Glo1 are indeed widespread in nature regardless of the intracellular thiol employed by an organism.

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