A biosynthetic thiolase in complex with a reaction intermediate: the crystal structure provides new insights into the catalytic mechanism.
Yorgo Modis,Rik K. Wierenga +1 more
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TL;DR: The shape of the substrate-binding pocket reveals the basis for the short-chain substrate specificity of the enzyme, and suggests an important role for the thioester oxygen atom of the acetylated enzyme in catalysis.
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About: This article is published in Structure. The article was published on 15 Oct 1999. and is currently open access. The article focuses on the topics: Thiolase & Reaction intermediate.
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Citations
Crystal structure of cytoplasmic acetoacetyl-CoA thiolase from Saccharomyces cerevisiae
TL;DR: The structure determined shows that ERG10 shares the characteristic thiolase superfamily fold, with a similar active-site architecture to those of type II thiolases and a similar binding pocket, apart from Ala159 at the entrance to the pantetheine-binding cavity, which appears to be a determinant of the poor binding ability of the substrate.
Heterologous expression and characterisation of a biosynthetic thiolase from Clostridium butyricum DSM 10702
TL;DR: The gene coding for thiolase from C. butyricum DSM 10702 was cloned by genome walking and revealed that the catalytically active enzyme consists of a homotetramer, indicating that CoASH has an important regulatory function in vivo.
3
Structural studies on the enzymatic units of the peroxisomal multifunctional enzyme type 2 (MFE-2)
Kristian Koski
- 01 Jan 2004
TL;DR: The solved three-dimensional structures of the (3R)-hydroxyacyl-CoA dehydrogenase and 2-enoyl- coenzyme A hydratase 2 units were solved by crystallographic methods and provided a molecular basis for understanding the effects of the patient mutations of MFE-2.
OCT1 - a yeast mitochondrial thiolase involved in the 3-oxoadipate pathway.
Romana Vrzoňová,Renáta Tóth,Barbara Sivakova,Anna Moťovská,Katarina Gaplovska-Kysela,Peter Barath,Ľubomír Tomáška,Attila Gácser,Toni Gabaldón,Jozef Nosek,Martina Neboháčová +10 more
TL;DR: It is found that the cells grown on a 3-oxoadipate pathway substrate exhibit increased levels of the OCT1 mRNA, and an intricate evolutionary pattern indicating multiple horizontal gene transfers among different fungal groups is revealed.
3
Patent
METHODS FOR BIOSYNTHESIZING 3-OXOPENT-4-ENOYL-CoA
Alex Van Eck Conradie,Adriana Leonora Botes +1 more
- 29 Jul 2014
TL;DR: This article described biochemical pathways that include the production of 3-oxopent-4-enoyl-CoA by condensation of acryloyl CoA and acetyl CoA using a β-ketothiolase with a SERHIS-HIS catalytic triad.
3
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