Recombinant Gloeobacter violaceus 3-dehydroquinate dehydratase (aroQ)

Introduction

Recombinant Gloeobacter violaceus 3-dehydroquinate dehydratase (aroQ) is an enzyme that plays a crucial role in the shikimate pathway, which is essential for the biosynthesis of aromatic amino acids (AAA) in many microorganisms . Specifically, AroQ catalyzes the trans-dehydration reaction that converts 3-dehydroshikimate into 3-dehydroquinate . Gloeobacter violaceus is a cyanobacterium, and its AroQ enzyme has been produced recombinantly for research purposes .

Characteristics of Gloeobacter violaceus AroQ

Gloeobacter violaceus AroQ is a 3-dehydroquinate dehydratase enzyme that participates in the shikimate pathway . The enzyme is encoded by the aroQ gene and has been recombinantly produced for various studies . The recombinant protein is produced in yeast and is reported to have high purity .

Basic Information :

• Product Code: CSB-BP762887GCI

• Abbreviation: aroQ

• Source Organism: Gloeobacter violaceus (strain PCC 7421)

• Purity: >85% (SDS-PAGE)

• UniProt No.: Q7NHU3

• Sequence: MPIAASLRVL LLNGPNLSLL GRREVDVYGT VTLADIERTL QLDAQDLDVE LSCLQSNHEG VLIDAIHDAF GRCDGLVINP GGLTHTSVAL RDAIAGVGLP TVEVHMSNVY RRESFRHHSF IAPVAVGQIS GFGADSYRLG LRAIALFLRR RAEQDEGPCR

Storage and Stability :

• Liquid form: Stable for 6 months at -20°C/-80°C

• Lyophilized form: Stable for 12 months at -20°C/-80°C

Function and Mechanism

AroQ enzymes, including the one from Gloeobacter violaceus, are essential for the shikimate pathway, which leads to the production of aromatic amino acids such as phenylalanine, tyrosine, and tryptophan . These amino acids are vital for protein synthesis and various other metabolic processes in organisms . AroQ catalyzes the third step in this pathway, converting 3-dehydroshikimate to 3-dehydroquinate via a trans-dehydration reaction .

Role in Pathogenicity and Metabolism

In some bacteria, such as Ralstonia solanacearum, AroQ enzymes play a significant role in pathogenicity . Mutants lacking AroQ1 and AroQ2 showed impaired growth and reduced virulence in host plants . This indicates the importance of AroQ in bacterial metabolism and its impact on the ability of bacteria to cause disease . Furthermore, the enzyme activity of 3-dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH) has been studied in the context of gallotannin (GA) synthesis in Camellia sinensis .

Functional Analysis and Mutant Studies

Studies on other organisms, like C. sinensis, have explored the functional aspects of 3-dehydroquinate dehydratase/shikimate dehydrogenase (DQD/SDH) . These studies involve enzyme activity assays, product analysis, and site-directed mutagenesis to understand the enzyme's catalytic efficiency and its role in metabolic pathways . Site-directed mutagenesis has been used to identify key amino acid residues responsible for the enzyme's activity .

Relevance to Cyanobacteria

Cyanobacteria, including Gloeobacter violaceus, are ancient life forms that have played a crucial role in the Earth's history . Understanding the metabolic pathways in these organisms, including the shikimate pathway and the enzymes involved, is important for understanding their biology and potential applications .

Potential Applications

Inhibitors of mycobacterial leucyl-tRNA synthetase have been designed and synthesized as potential antimicrobial agents . Given the role of AroQ in essential metabolic pathways, it could be a target for developing new antimicrobial compounds .