scholarly journals Crystal Structure of Geranylgeranyl Pyrophosphate Synthase (CrtE) Involved in Cyanobacterial Terpenoid Biosynthesis

2020 ◽  
Vol 11 ◽  
Author(s):  
Yuchi Feng ◽  
R. Marc L. Morgan ◽  
Paul D. Fraser ◽  
Klaus Hellgardt ◽  
Peter J. Nixon
2006 ◽  
Vol 281 (31) ◽  
pp. 22004-22012 ◽  
Author(s):  
Kathryn L. Kavanagh ◽  
James E. Dunford ◽  
Gabor Bunkoczi ◽  
R. Graham G. Russell ◽  
Udo Oppermann

Marine Drugs ◽  
2019 ◽  
Vol 17 (12) ◽  
pp. 696
Author(s):  
Danqiong Huang ◽  
Wenfu Liu ◽  
Anguo Li ◽  
Chaogang Wang ◽  
Zhangli Hu

Haematococcus pluvialis is widely distributed in the world and well known as the richest natural source of astaxanthin that is a strong antioxidant with excellent commercial value. The pathway of astaxanthin biosynthesis in H. pluvialis has been documented as an enzymatic reaction. Several enzymes have been reported, but their isoforms or homologs have not been investigated genome-wide. To better understand the astaxanthin biosynthesis pathway in H. pluvialis, eight candidates of the geranylgeranyl pyrophosphate synthase gene (HpGGPPS) predicted from Iso-seq data were isolated in this study. The length of coding region of these candidates varied from 960 bp to 1272 bp, composing of 7–9 exons. The putative amino acids of all candidates composed the signature domain of GGPPS gene. However, the motifs in the domain region are varied, indicating different bio-functions. Phylogenetic analysis revealed eight candidates can be clustered into three groups. Only two candidates in Group1 encode the synthase participating in the astaxanthin formation. The yield of astaxanthin from these two candidates, 7.1 mg/g (DW) and 6.5 mg/g (DW) respectively, is significant higher than that from CrtE (2.4 mg/g DW), a GGPPS gene from Pantoea ananatis. This study provides a potential productive pathway for astaxanthin synthesis.


Author(s):  
Kristin Rudolph ◽  
Christoph Parthier ◽  
Claudia Egerer-Sieber ◽  
Daniel Geiger ◽  
Yves A. Muller ◽  
...  

The biosynthesis of γ-terpinene, a precursor of the phenolic isomers thymol and carvacrol found in the essential oil fromThymussp., is attributed to the activitiy of γ-terpinene synthase (TPS). Purified γ-terpinene synthase fromT. vulgaris(TvTPS), theThymusspecies that is the most widely spread and of the greatest economical importance, is able to catalyze the enzymatic conversion of geranyl diphosphate (GPP) to γ-terpinene. The crystal structure of recombinantly expressed and purifiedTvTPS is reported at 1.65 Å resolution, confirming the dimeric structure of the enzyme. The putative active site ofTvTPS is deduced from its pronounced structural similarity to enzymes from other species of the Lamiaceae family involved in terpenoid biosynthesis: to (+)-bornyl diphosphate synthase and 1,8-cineole synthase fromSalviasp. and to (4S)-limonene synthase fromMentha spicata.


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