Catalytic mechanism of the novel non-haem iron containing peroxidase produced by the thermophilic actinomycete Thermomonospora fusca BD25

1997 ◽  
Vol 25 (1) ◽  
pp. 64S-64S ◽  
Author(s):  
ABDUL ROB ◽  
ANDREW S. BALL ◽  
MUNIR TUNCER ◽  
MICHAEL T. WILSON
Keyword(s):  
Catalytic Mechanism ◽  
The Novel ◽  
Thermomonospora Fusca ◽  
Thermophilic Actinomycete ◽  
Haem Iron

REDOX REACTION OF THE NOVEL NON-HAEM GLYCOSYLATED PEROXIDASES FROM THERMOPHILIC ACTINOMYCETE THERMOMONOSPORA FUSCA BD25

1996 ◽  
Vol 24 (3) ◽  
pp. 455S-455S ◽  
Author(s):  
Abdul Rob ◽  
Andrew S. Ball ◽  
Munir Tuncer ◽  
Gareth D. Jones ◽  
Paul D. Taylor ◽  
...  
Keyword(s):  
Redox Reaction ◽  
The Novel ◽  
Thermomonospora Fusca ◽  
Thermophilic Actinomycete

PLP undergoes conformational changes during the course of an enzymatic reaction

2014 ◽  
Vol 70 (2) ◽  
pp. 596-606 ◽  
Author(s):  
Ho-Phuong-Thuy Ngo ◽  
Nuno M. F. S. A. Cerqueira ◽  
Jin-Kwang Kim ◽  
Myoung-Ki Hong ◽  
Pedro Alexandrino Fernandes ◽  
...  
Keyword(s):  
Conformational Change ◽  
Conformational Changes ◽  
Catalytic Mechanism ◽  
Enzymatic Reaction ◽  
Nucleophilic Attack ◽  
The Novel ◽  
X Ray ◽  
X Ray Crystallography ◽  
Starting Point ◽  
High Level

Numerous enzymes, such as the pyridoxal 5′-phosphate (PLP)-dependent enzymes, require cofactors for their activities. Using X-ray crystallography, structural snapshots of the L-serine dehydratase catalytic reaction of a bacterial PLP-dependent enzyme were determined. In the structures, the dihedral angle between the pyridine ring and the Schiff-base linkage of PLP varied from 18° to 52°. It is proposed that the organic cofactor PLP directly catalyzes reactions by active conformational changes, and the novel catalytic mechanism involving the PLP cofactor was confirmed by high-level quantum-mechanical calculations. The conformational change was essential for nucleophilic attack of the substrate on PLP, for concerted proton transfer from the substrate to the protein and for directing carbanion formation of the substrate. Over the whole catalytic cycle, the organic cofactor catalyzes a series of reactions, like the enzyme. The conformational change of the PLP cofactor in catalysis serves as a starting point for identifying the previously unknown catalytic roles of organic cofactors.

scholarly journals Novel enzyme for dimethyl sulfide-releasing in bacteria reveals a missing route in the marine sulfur cycle

2020 ◽  
Author(s):  
Chun-Yang Li ◽  
Xiu-Juan Wang ◽  
Xiu-Lan Chen ◽  
Qi Sheng ◽  
Shan Zhang ◽  
...  
Keyword(s):  
Dimethyl Sulfide ◽  
Catalytic Mechanism ◽  
Global Climate ◽  
Sulfur Cycle ◽  
The Novel ◽  
Key Enzyme ◽  
Biochemical Analyses ◽  
Bacterial Lineages

AbstractDimethylsulfoniopropionate (DMSP) is an abundant and ubiquitous organosulfur molecule and plays important roles in the global sulfur cycle. Cleavage of DMSP produces volatile dimethyl sulfide (DMS), which has impacts on the global climate. Multiple pathways for DMSP catabolism have been identified. Here we identified yet another novel pathway, the ATP DMSP lysis pathway. The key enzyme, AcoD, is an ATP-dependent DMSP lyase. AcoD belongs to the acyl-CoA synthetase superfamily, which is totally different from other DMSP lyases, showing a new evolution route. AcoD catalyses the conversion of DMSP to DMS by a two-step reaction: the ligation of DMSP with CoA to form the intermediate DMSP-CoA, which is then cleaved to DMS and acryloyl-CoA. The novel catalytic mechanism was elucidated by structural and biochemical analyses. AcoD is widely distributed in many bacterial lineages including Alphaproteobacteria, Betaproteobacteria, Gammaproteobacteria and Firmicutes, revealing this new pathway plays important roles in global DMSP/DMS cycles.

scholarly journals Revealing the Intrinsic Peroxidase-Like Catalytic Mechanism of Heterogeneous Single-Atom Co–MoS2

2019 ◽  
Vol 11 (1) ◽  
Author(s):  
Ying Wang ◽  
Kun Qi ◽  
Shansheng Yu ◽  
Guangri Jia ◽  
Zhiliang Cheng ◽  
...  
Keyword(s):  
High Performance ◽  
Catalytic Mechanism ◽  
Single Atom ◽  
Theoretical Studies ◽  
The Novel ◽  
Peroxidase Mimic ◽  
Adsorption Energies ◽  
Experimental And Theoretical Studies ◽  
Transfer Mechanisms ◽  
Different Parts

AbstractThe single-atom nanozyme is a new concept and has tremendous prospects to become a next-generation nanozyme. However, few studies have been carried out to elucidate the intrinsic mechanisms for both the single atoms and the supports in single-atom nanozymes. Herein, the heterogeneous single-atom Co–MoS2 (SA Co–MoS2) is demonstrated to have excellent potential as a high-performance peroxidase mimic. Because of the well-defined structure of SA Co–MoS2, its peroxidase-like mechanism is extensively interpreted through experimental and theoretical studies. Due to the different adsorption energies of substrates on different parts of SA Co–MoS2 in the peroxidase-like reaction, SA Co favors electron transfer mechanisms, while MoS2 relies on Fenton-like reactions. The different catalytic pathways provide an intrinsic understanding of the remarkable performance of SA Co–MoS2. The present study not only develops a new kind of single-atom catalyst (SAC) as an elegant platform for understanding the enzyme-like activities of heterogeneous nanomaterials but also facilitates the novel application of SACs in biocatalysis.

Growth of Thermomonospora fusca on lignocellulosic pulps of varying lignin content

1974 ◽  
Vol 20 (7) ◽  
pp. 1069-1072 ◽  
Author(s):  
Don L. Crawford
Keyword(s):  
Lignin Degradation ◽  
Lignin Content ◽  
Carbohydrate Utilization ◽  
Thermomonospora Fusca ◽  
Thermophilic Actinomycete ◽  
Carbohydrate Fraction ◽  
Carbohydrate Degradation

The ability of the thermophilic actinomycete, Thermomonospora fusca, to degrade lignocellulose was investigated. Thermomonospora fusca was grown at 55C on lignocellulosic pulps varying in lignin content between 3% and 18%. Thermomonospora fusca was found to degrade primarily the carbohydrate fraction of these substrates. Small, and probably insignificant, losses of lignin were observed after 14 days growth on the substrates. Increasing lignin content in the pulps proportionally blocked carbohydrate utilization by T. fusca. The organism, however, could still substantially solubilize even the substrate containing 18% lignin. It is thought that T. fusca plays a role in the decomposition of lignocellulose in nature; however, it is probably involved with carbohydrate degradation, not lignin degradation.

scholarly journals A novel ATP dependent dimethylsulfoniopropionate lyase in bacteria that releases dimethyl sulfide and acryloyl-CoA

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Chun-Yang Li ◽  
Xiu-Juan Wang ◽  
Xiu-Lan Chen ◽  
Qi Sheng ◽  
Shan Zhang ◽  
...  
Keyword(s):  
Nutrient Cycling ◽  
Atmospheric Chemistry ◽  
Dimethyl Sulfide ◽  
Catalytic Mechanism ◽  
The Novel ◽  
Marine Environments ◽  
Biochemical Analyses ◽  
Bacteria And Fungi

Dimethylsulfoniopropionate (DMSP) is an abundant and ubiquitous organosulfur molecule in marine environments with important roles in global sulfur and nutrient cycling. Diverse DMSP lyases in some algae, bacteria and fungi cleave DMSP to yield gaseous dimethyl sulfide (DMS), an infochemical with important roles in atmospheric chemistry. Here we identified a novel ATP-dependent DMSP lyase, DddX. DddX belongs to the acyl-CoA synthetase superfamily and is distinct from the eight other known DMSP lyases. DddX catalyses the conversion of DMSP to DMS via a two-step reaction: the ligation of DMSP with CoA to form the intermediate DMSP-CoA, which is then cleaved to DMS and acryloyl-CoA. The novel catalytic mechanism was elucidated by structural and biochemical analyses. DddX is found in several Alphaproteobacteria, Gammaproteobacteria and Firmicutes, suggesting that this new DMSP lyase may play an overlooked role in DMSP/DMS cycles.

scholarly journals The biochemical characterization of a novel non-haem-iron hydroxylamine oxidase from Paracoccus denitrificans GB17

1996 ◽  
Vol 319 (3) ◽  
pp. 823-827 ◽  
Author(s):  
James W. B. MOIR ◽  
Josa-Marie WEHRFRITZ ◽  
Stephen SPIRO ◽  
David J RICHARDSON
Keyword(s):  
Nitrous Oxide ◽  
Catalytic Mechanism ◽  
Biochemical Characterization ◽  
Paracoccus Denitrificans ◽  
Anaerobic Conditions ◽  
Carboxylate Ligands ◽  
Prosthetic Groups ◽  
Haem Iron ◽  
Sole Product

The characterization of the hydroxylamine oxidase from the heterotrophic nitrifier Paracoccus denitrificans GB17 indicates the enzyme to be entirely distinct from the hydroxylamine oxidase from the autotrophic nitrifier Nitrosomonas europaea. Hydroxylamine oxidase from P. denitrificans contains three to five non-haem, non-iron-sulphur iron atoms as prosthetic groups, predominantly co-ordinated by carboxylate ligands. The interaction of the enzyme with the electron-accepting proteins cytochrome c550 and pseudoazurin is mainly hydrophobic. The catalytic mechanism of hydroxylamine oxidase from P. denitrificans is different from the enzyme from N. europaea because the production of nitrite by the former requires molecular oxygen. Under anaerobic conditions the enzyme makes nitrous oxide as a sole product.

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