scholarly journals The crystal structure of the tetrameric DABA‐aminotransferase EctB, a rate‐limiting enzyme in the ectoine biosynthesis pathway

FEBS Journal ◽  
2020 ◽  
Vol 287 (21) ◽  
pp. 4641-4658 ◽  
Author(s):  
Heidi Therese Hillier ◽  
Bjørn Altermark ◽  
Ingar Leiros
Keyword(s):  
Crystal Structure ◽  
Biosynthesis Pathway ◽  
Rate Limiting ◽  
Ectoine Biosynthesis

scholarly journals Threonine 57 is required for the post-translational activation ofEscherichia coliaspartate α-decarboxylase

2014 ◽  
Vol 70 (4) ◽  
pp. 1166-1172 ◽  
Author(s):  
Michael E. Webb ◽  
Briony A. Yorke ◽  
Tom Kershaw ◽  
Sarah Lovelock ◽  
Carina M. C. Lobley ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Active Site ◽  
Site Directed Mutagenesis ◽  
Intramolecular Rearrangement ◽  
Directed Mutagenesis ◽  
Vitamin B ◽  
Biosynthesis Pathway ◽  
Serine Residue ◽  
Translational Activation

Aspartate α-decarboxylase is a pyruvoyl-dependent decarboxylase required for the production of β-alanine in the bacterial pantothenate (vitamin B5) biosynthesis pathway. The pyruvoyl group is formedviathe intramolecular rearrangement of a serine residue to generate a backbone ester intermediate which is cleaved to generate an N-terminal pyruvoyl group. Site-directed mutagenesis of residues adjacent to the active site, including Tyr22, Thr57 and Tyr58, reveals that only mutation of Thr57 leads to changes in the degree of post-translational activation. The crystal structure of the site-directed mutant T57V is consistent with a non-rearranged backbone, supporting the hypothesis that Thr57 is required for the formation of the ester intermediate in activation.

scholarly journals Crystal Structure and Mechanistic Implications of N2-(2-Carboxyethyl)arginine Synthase, the First Enzyme in the Clavulanic Acid Biosynthesis Pathway

2003 ◽  
Vol 279 (7) ◽  
pp. 5685-5692 ◽  
Author(s):  
Matthew E. C. Caines ◽  
Jonathan M. Elkins ◽  
Kirsty S. Hewitson ◽  
Christopher J. Schofield
Keyword(s):  
Crystal Structure ◽  
Clavulanic Acid ◽  
Biosynthesis Pathway ◽  
Acid Biosynthesis

scholarly journals The dissociation mechanism of processive cellulases

2019 ◽  
Vol 116 (46) ◽  
pp. 23061-23067 ◽  
Author(s):  
Josh V. Vermaas ◽  
Riin Kont ◽  
Gregg T. Beckham ◽  
Michael F. Crowley ◽  
Mikael Gudmundsson ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Molecular Mechanisms ◽  
Soluble Sugars ◽  
Dissociation Rate ◽  
Replica Exchange ◽  
Wild Type ◽  
Replica Exchange Molecular Dynamics ◽  
Hamiltonian Replica Exchange ◽  
Biochemical Measurements ◽  
Rate Limiting

Cellulase enzymes deconstruct recalcitrant cellulose into soluble sugars, making them a biocatalyst of biotechnological interest for use in the nascent lignocellulosic bioeconomy. Cellobiohydrolases (CBHs) are cellulases capable of liberating many sugar molecules in a processive manner without dissociating from the substrate. Within the complete processive cycle of CBHs, dissociation from the cellulose substrate is rate limiting, but the molecular mechanism of this step is unknown. Here, we present a direct comparison of potential molecular mechanisms for dissociation via Hamiltonian replica exchange molecular dynamics of the model fungal CBH, Trichoderma reesei Cel7A. Computational rate estimates indicate that stepwise cellulose dethreading from the binding tunnel is 4 orders of magnitude faster than a clamshell mechanism, in which the substrate-enclosing loops open and release the substrate without reversing. We also present the crystal structure of a disulfide variant that covalently links substrate-enclosing loops on either side of the substrate-binding tunnel, which constitutes a CBH that can only dissociate via stepwise dethreading. Biochemical measurements indicate that this variant has a dissociation rate constant essentially equivalent to the wild type, implying that dethreading is likely the predominant mechanism for dissociation.

scholarly journals Fatty Acids Regulate Porcine Reproductive and Respiratory Syndrome Virus Infection via the AMPK-ACC1 Signaling Pathway

Viruses ◽  
2019 ◽  
Vol 11 (12) ◽  
pp. 1145 ◽  
Author(s):  
Siwen Long ◽  
Yanrong Zhou ◽  
Dongcheng Bai ◽  
Wanjun Hao ◽  
Bohan Zheng ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Adenosine Monophosphate ◽  
Respiratory Syndrome Virus ◽  
Biosynthesis Pathway ◽  
Acetyl Coa Carboxylase ◽  
Inactive Form ◽  
Antiviral Targets ◽  
Amp Activated Protein Kinase ◽  
New Evidence ◽  
Rate Limiting

Lipids play a crucial role in the replication of porcine reproductive and respiratory syndrome virus (PRRSV), a porcine virus that is endemic throughout the world. However, little is known about the effect of fatty acids (FAs), a type of vital lipid, on PRRSV infection. In this study, we found that treatment with a FA biosynthetic inhibitor significantly inhibited PRRSV propagation, indicating the necessity of FAs for optimal replication of PRRSV. Further study revealed that 5′-adenosine monophosphate (AMP)-activated protein kinase (AMPK), a key kinase antagonizing FA biosynthesis, was strongly activated by PRRSV and the pharmacological activator of AMPK exhibited anti-PRRSV activity. Additionally, we found that acetyl-CoA carboxylase 1 (ACC1), the first rate-limiting enzyme in the FA biosynthesis pathway, was phosphorylated (inactive form) by PRRSV-activated AMPK, and active ACC1 was required for PRRSV proliferation, suggesting that the PRRSV infection induced the activation of the AMPK–ACC1 pathway, which was not conducive to PRRSV replication. This work provides new evidence about the mechanisms involved in host lipid metabolism during PRRSV infection and identifies novel potential antiviral targets for PRRSV.

scholarly journals Bisphenol A Impairs Follicle Growth, Inhibits Steroidogenesis, and Downregulates Rate-Limiting Enzymes in the Estradiol Biosynthesis Pathway

2010 ◽  
Vol 119 (1) ◽  
pp. 209-217 ◽  
Author(s):  
Jackye Peretz ◽  
Rupesh K. Gupta ◽  
Jeffrey Singh ◽  
Isabel Hernández-Ochoa ◽  
Jodi A. Flaws
Keyword(s):  
Bisphenol A ◽  
Biosynthesis Pathway ◽  
Follicle Growth ◽  
Rate Limiting

scholarly journals Crystal structure of norcoclaurine-6-O-methyltransferase, a key rate-limiting step in the synthesis of benzylisoquinoline alkaloids

2016 ◽  
Vol 87 (6) ◽  
pp. 641-653 ◽  
Author(s):  
Adeline Y. Robin ◽  
Cécile Giustini ◽  
Matthieu Graindorge ◽  
Michel Matringe ◽  
Renaud Dumas
Keyword(s):  
Crystal Structure ◽  
Benzylisoquinoline Alkaloids ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Rate Limiting

scholarly journals Draft Genome Sequences of Vibrio alginolyticus Strain S6-61 and Vibrio diabolicus Strain S7-71, Isolated from Corals in the Andaman Sea

2020 ◽  
Vol 9 (8) ◽  
Author(s):  
Sushanta Deb ◽  
Jhasketan Badhai ◽  
Subrata K. Das
Keyword(s):  
Draft Genome ◽  
Vibrio Alginolyticus ◽  
Andaman Sea ◽  
Biosynthesis Pathway ◽  
Genome Sequences ◽  
Protein Coding ◽  
Content Type ◽  
Protein Coding Genes ◽  
Ectoine Biosynthesis ◽  
Pocillopora Verrucosa

We report the draft genome sequences of Vibrio alginolyticus strain S6-61 and Vibrio diabolicus strain S7-71, isolated from the corals Pocillopora verrucosa and Fungia danai, respectively. The genomes of strains S6-61 and S7-71 contain 4,880 and 4,641 protein coding genes, respectively, and harbor genes associated with the ectoine biosynthesis pathway.

scholarly journals The crystal structure of AbsH3 : A putative flavin adenine dinucleotide‐dependent reductase in the abyssomicin biosynthesis pathway

2020 ◽  
Vol 89 (1) ◽  
pp. 132-137
Author(s):  
Jonathan A. Clinger ◽  
Xiachang Wang ◽  
Wenlong Cai ◽  
Yanyan Zhu ◽  
Mitchell D. Miller ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Flavin Adenine Dinucleotide ◽  
Biosynthesis Pathway

scholarly journals Crystal structure of thebaine 6-O-demethylase from the morphine biosynthesis pathway

2018 ◽  
Vol 202 (3) ◽  
pp. 229-235 ◽  
Author(s):  
Anna Kluza ◽  
Ewa Niedzialkowska ◽  
Katarzyna Kurpiewska ◽  
Zuzanna Wojdyla ◽  
Matthew Quesne ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Biosynthesis Pathway
Sign in / Sign up

Export Citation Format

Share Document