Aspartate transcarbamoylase (ATCase) and dihydroorotase (DHOase) catalyse the first two steps unique to pyrimidine synthesis. In many bacteria they form non-covalently bonded complexes. There are two types of DHOase, type I and type II which share a common ancestry. Type I is the more ancient form and is present in the complexes. In recently evolved bacteria the DHOase is defective and its function has been replaced by a type II DHOase which is separate from the complex. Deinococcus radiophilus diverges early on the phylogenetic tree and so might be expected to have an active type I DHOase. Purification of the 500 kDa ATCase-DHOase complex, by conventional techniques, showed it to possess an active DHOase.

Download full-text PDF

Source
http://dx.doi.org/10.1007/s00203-005-0075-3DOI Listing

Publication Analysis

Top Keywords

complex deinococcus
8
deinococcus radiophilus
8
type dhoase
8
dhoase
6
type
5
aspartate transcarbamoylase-dihydroorotase
4
transcarbamoylase-dihydroorotase complex
4
radiophilus active
4
active dihydroorotase
4
dihydroorotase aspartate
4

Similar Publications

Radiation-resistant bacteria are of great application potential in various fields, including bioindustry and bioremediation of radioactive waste. However, how radiation-resistant bacteria combat against invading phages is seldom addressed. Here, we present a series of crystal structures of a sensor and an effector of the cyclic oligonucleotide-based anti-phage signaling system (CBASS) from a radioresistant bacterium Deinococcus wulumuqiensis.

View Article and Find Full Text PDF

The bacterium responsible for Lyme disease, , accumulates high levels of manganese without iron and possesses a polyploid genome, characteristics suggesting potential extreme resistance to radiation. Contrary to expectations, we report that wild-type B31 cells are radiosensitive, with a gamma-radiation survival limit for 10 wild-type cells of <1 kGy. Thus, we explored radiosensitivity through electron paramagnetic resonance (EPR) spectroscopy by quantitating the fraction of Mn present as antioxidant Mn metabolite complexes (H-Mn).

View Article and Find Full Text PDF

Mn coordinated by orthophosphate (Pi), metabolites, or peptides acts as a superoxide dismutase (SOD), and these Mn antioxidant complexes are universally accumulated in extremely radiation-resistant cell types across the tree of life. This behavior prompted design of decapeptide DP1 (DEHGTAVMLK) as a Mn ligand, and development of a highly potent Mn-antioxidant (MDP) containing [Pi] = 25 mM, and [DP1] = 3 mM, the ratio found in the radioresistant bacterium , with [Mn] = 1 mM. MDP is an exceptional antioxidant, both in vitro and in vivo, and has reinvigorated the development of radiation-inactivated whole-cell vaccines.

View Article and Find Full Text PDF

Agricultural practices significantly influence microbial diversity and the distribution of virulence and antimicrobial resistance (AMR) genes, with implications for ecosystem health and food safety. This study used metagenomic sequencing to analyze 60 samples (30 per state) including water, soil, and manure (10 each) from Alabama (a mix of cattle and poultry sources) and Tennessee (primarily from cattle). The results highlighted a rich microbial diversity, predominantly comprising Bacteria (67%) and Viruses (33%), with a total of over 1,950 microbial species identified.

View Article and Find Full Text PDF

Construction and enzymatic characterization of a monomeric variant of dimeric amylosucrase from Deinococcus geothermalis.

Int J Biol Macromol

January 2025

Department of Food Science and Biotechnology, and Carbohydrate Bioproduct Research Center, Sejong University, Seoul 05006, Republic of Korea. Electronic address:

Article Synopsis
  • Amylosucrase (ASase) from Deinococcus geothermalis (DgAS) is characterized as a dimeric enzyme that produces α-1,4-glucans using sucrose, and this study reveals key amino acids important for maintaining its dimeric structure.
  • The mutated monomeric form (DgAS R30A) shows a stronger affinity for sucrose and preferentially produces shorter α-glucans with a degree of polymerization (DP) of ≤20.
  • The research also uncovers the first high-resolution structure of dimeric DgAS, providing insights into enzyme activity and the significance of dimerization for its functional properties.
View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!