scholarly journals A novel catalytic heme cofactor in SfmD with a single thioether bond and a bis-His ligand set revealed by a de novo crystal structural and spectroscopic study

2021 ◽  
Author(s):  
Inchul Shin ◽  
Ian Davis ◽  
Karinel Nieves-Merced ◽  
Yifan Wang ◽  
Stanton McHardy ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Spectroscopic Study ◽  
Biosynthetic Pathway ◽  
De Novo ◽  
Crystal Structural ◽  
Heme Cofactor

The de novo crystal structure of SfmD reveals a novel c-type heme cofactor for promoting a monooxygenation reaction in the biosynthetic pathway of saframycin A.

Iron in kornerupine; a57Fe Moessbauer spectroscopic study and comparison with single-crystal structure refinement

1999 ◽  
Vol 84 (4) ◽  
pp. 536-549 ◽  
Author(s):  
Edward S. Grew ◽  
Guenther J. Redhammer ◽  
Georg Amthauer ◽  
Mark A. Cooper ◽  
Frank C. Hawthorne ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Single Crystal ◽  
Spectroscopic Study ◽  
Structure Refinement ◽  
Single Crystal Structure ◽  
Crystal Structure Refinement

scholarly journals The 1.6 Å Crystal Structure ofMycobacterium smegmatisMshC: The Penultimate Enzyme in the Mycothiol Biosynthetic Pathway†

Biochemistry ◽  
2008 ◽  
Vol 47 (50) ◽  
pp. 13326-13335 ◽  
Author(s):  
L. W. Tremblay ◽  
F. Fan ◽  
M. W. Vetting ◽  
J. S. Blanchard
Keyword(s):  
Crystal Structure ◽  
Biosynthetic Pathway

Crystal Structure of Vancosaminyltransferase GtfD from the Vancomycin Biosynthetic Pathway:  Interactions with Acceptor and Nucleotide Ligands†,‡

Biochemistry ◽  
2004 ◽  
Vol 43 (18) ◽  
pp. 5170-5180 ◽  
Author(s):  
Anne M. Mulichak ◽  
Wei Lu ◽  
Heather C. Losey ◽  
Christopher T. Walsh ◽  
R. Michael Garavito
Keyword(s):  
Crystal Structure ◽  
Biosynthetic Pathway

Synthesis, crystal structure and spectroscopic study of para substituted 2-hydroxy-3-methoxybenzalideneanilines

2003 ◽  
Vol 658 (1-2) ◽  
pp. 87-99 ◽  
Author(s):  
Guan-Yeow Yeap ◽  
Sie-Tiong Ha ◽  
Nobuo Ishizawa ◽  
Katsumi Suda ◽  
Peng-Lim Boey ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Spectroscopic Study

scholarly journals The biosynthetic origin of psychoactive kavalactones in kava

2018 ◽  
Author(s):  
Tomáš Pluskal ◽  
Michael P. Torrens-Spence ◽  
Timothy R. Fallon ◽  
Andrea De Abreu ◽  
Cindy H. Shi ◽  
...  
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Biosynthetic Pathway ◽  
Chalcone Synthase ◽  
De Novo ◽  
Piper Methysticum ◽  
Heterologous Production ◽  
Traditional Use ◽  
Plant Biochemistry ◽  
Tailoring Enzymes

AbstractFor millennia, humans have used plants for medicinal purposes. However, our limited understanding of plant biochemistry hinders the translation of such ancient wisdom into modern pharmaceuticals1. Kava (Piper methysticum) is a medicinal plant native to the Polynesian islands with anxiolytic and analgesic properties supported by over 3,000 years of traditional use as well as numerous recent clinical trials2–5. The main psychoactive principles of kava, kavalactones, are a unique class of polyketide natural products known to interact with central nervous system through mechanisms distinct from those of the prescription psychiatric drugs benzodiazepines and opioids6,7. Here we reportde novoelucidation of the biosynthetic pathway of kavalactones, consisting of seven specialized metabolic enzymes. Based on phylogenetic and crystallographic analyses, we highlight the emergence of two paralogous styrylpyrone synthases, both of which have neofunctionalized from an ancestral chalcone synthase to catalyze the formation of the kavalactone scaffold. Structurally diverse kavalactones are then biosynthesized by subsequent regio- and stereo-specific tailoring enzymes. We demonstrate the feasibility of engineering heterologous production of kavalactones and their derivatives in bacterial, yeast, and plant hosts, thus opening an avenue towards the development of new psychiatric therapeutics for anxiety disorders, which affect over 260 million people globally8.

scholarly journals The Arabidopsis locus AT3G03890 encodes a dimeric β-barrel protein implicated in heme degradation

2020 ◽  
Vol 477 (24) ◽  
pp. 4785-4796
Author(s):  
Jia Wang ◽  
Qi Guo ◽  
Xiaoyi Li ◽  
Xiao Wang ◽  
Lin Liu
Keyword(s):  
Crystal Structure ◽  
Recombinant Protein ◽  
Water Molecule ◽  
Heme Oxygenase ◽  
Protein Complex ◽  
Biosynthetic Pathway ◽  
Initial Step ◽  
Heme Iron ◽  
Heme Binding ◽  
New Protein

Plant tetrapyrroles, including heme and bilins, are synthesized in plastids. Heme oxygenase (HO) catalyzes the oxidative cleavage of heme to the linear tetrapyrrole biliverdin as the initial step in bilin biosynthesis. Besides the canonical α-helical HO that is conserved from prokaryotes to human, a subfamily of non-canonical dimeric β-barrel HO has been found in bacteria. In this work, we discovered that the Arabidopsis locus AT3G03890 encodes a dimeric β-barrel protein that is structurally related to the putative non-canonical HO and is located in chloroplasts. The recombinant protein was able to bind and degrade heme in a manner different from known HO proteins. Crystal structure of the heme–protein complex reveals that the heme-binding site is in the interdimer interface and the heme iron is co-ordinated by a fixed water molecule. Our results identify a new protein that may function additionally in the tetrapyrrole biosynthetic pathway.

scholarly journals Surprising Arginine Biosynthesis: a Reappraisal of the Enzymology and Evolution of the Pathway in Microorganisms

2007 ◽  
Vol 71 (1) ◽  
pp. 36-47 ◽  
Author(s):  
Ying Xu ◽  
Bernard Labedan ◽  
Nicolas Glansdorff
Keyword(s):  
Biosynthetic Pathway ◽  
De Novo ◽  
Single Gene ◽  
Metabolic Function ◽  
Gene Products ◽  
Arginine Biosynthesis ◽  
Acetyl Coenzyme A ◽  
Bacterial Phyla ◽  
Acetyl Group ◽  
Acetylglutamate Synthase

SUMMARY Major aspects of the pathway of de novo arginine biosynthesis via acetylated intermediates in microorganisms must be revised in light of recent enzymatic and genomic investigations. The enzyme N-acetylglutamate synthase (NAGS), which used to be considered responsible for the first committed step of the pathway, is present in a limited number of bacterial phyla only and is absent from Archaea. In many Bacteria, shorter proteins related to the Gcn5-related N-acetyltransferase family appear to acetylate l-glutamate; some are clearly similar to the C-terminal, acetyl-coenzyme A (CoA) binding domain of classical NAGS, while others are more distantly related. Short NAGSs can be single gene products, as in Mycobacterium spp. and Thermus spp., or fused to the enzyme catalyzing the last step of the pathway (argininosuccinase), as in members of the Alteromonas-Vibrio group. How these proteins bind glutamate remains to be determined. In some Bacteria, a bifunctional ornithine acetyltransferase (i.e., using both acetylornithine and acetyl-CoA as donors of the acetyl group) accounts for glutamate acetylation. In many Archaea, the enzyme responsible for glutamate acetylation remains elusive, but possible connections with a novel lysine biosynthetic pathway arose recently from genomic investigations. In some Proteobacteria (notably Xanthomonadaceae) and Bacteroidetes, the carbamoylation step of the pathway appears to involve N-acetylornithine or N-succinylornithine rather than ornithine. The product N-acetylcitrulline is deacetylated by an enzyme that is also involved in the provision of ornithine from acetylornithine; this is an important metabolic function, as ornithine itself can become essential as a source of other metabolites. This review insists on the biochemical and evolutionary implications of these findings.

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