Thiolase: A Versatile Biocatalyst Employing Coenzyme A–Thioester Chemistry for Making and Breaking C–C Bonds
RK Harijan, S Dalwani, TR Kiema… - Annual Review of …, 2023 - annualreviews.org
Thiolases are CoA-dependent enzymes that catalyze the thiolytic cleavage of 3-ketoacyl-
CoA, as well as its reverse reaction, which is the thioester-dependent Claisen condensation …
CoA, as well as its reverse reaction, which is the thioester-dependent Claisen condensation …
The 3-ketoacyl-CoA thiolase: an engineered enzyme for carbon chain elongation of chemical compounds
Because of their function of catalyzing the rearrangement of the carbon chains, thiolases
have attracted increasing attentions over the past decades. The 3-ketoacyl-CoA thiolase …
have attracted increasing attentions over the past decades. The 3-ketoacyl-CoA thiolase …
Rational design of the substrate tunnel of β-ketothiolase reveals a local cationic domain modulated rule that improves the efficiency of Claisen Condensation
Formation of carbon–carbon bonds via Claisen condensation catalyzed by thiolase
generates a diverse range of carbon frameworks in biosynthetic chemistry. During catalysis …
generates a diverse range of carbon frameworks in biosynthetic chemistry. During catalysis …
Crystal structure of FadA2 thiolase from Mycobacterium tuberculosis and prediction of its substrate specificity and membrane‐anchoring properties
Tuberculosis (TB) is one of the leading causes of human death caused by Mycobacterium
tuberculosis (Mtb). Mtb can enter into a long‐lasting persistence where it can utilize fatty …
tuberculosis (Mtb). Mtb can enter into a long‐lasting persistence where it can utilize fatty …
Finis tolueni: a new type of thiolase with an integrated Zn‐finger subunit catalyzes the final step of anaerobic toluene metabolism
S Weidenweber, K Schühle, ML Lippert… - The FEBS …, 2022 - Wiley Online Library
Anaerobic toluene degradation involves β‐oxidation of the first intermediate (R)‐2‐
benzylsuccinate to succinyl‐CoA and benzoyl‐CoA. Here, we characterize the last enzyme …
benzylsuccinate to succinyl‐CoA and benzoyl‐CoA. Here, we characterize the last enzyme …
The peroxisomal zebrafish SCP2-thiolase (type-1) is a weak transient dimer as revealed by crystal structures and native mass spectrometry
TR Kiema, CJ Thapa, M Laitaoja, W Schmitz… - Biochemical …, 2019 - portlandpress.com
The SCP2 (sterol carrier protein 2)-thiolase (type-1) functions in the vertebrate peroxisomal,
bile acid synthesis pathway, converting 24-keto-THC-CoA and CoA into choloyl-CoA and …
bile acid synthesis pathway, converting 24-keto-THC-CoA and CoA into choloyl-CoA and …
[HTML][HTML] Structural basis for differentiation between two classes of thiolase: degradative vs biosynthetic thiolase
Thiolases are a well characterized family of enzymes with two distinct categories:
degradative, β-ketoadipyl-CoA thiolases and biosynthetic, acetoacetyl-CoA thiolases. Both …
degradative, β-ketoadipyl-CoA thiolases and biosynthetic, acetoacetyl-CoA thiolases. Both …
Crystal structure of a thiolase from Archaeal Pyrococcus furiosus and its in silico functional annotation
In most of the eukaryotes and archaea, isopentenyl pyrophosphate (IPP) and dimethyl allyl
pyrophosphate (DMAPP) essential building blocks of all isoprenoids synthesized in the …
pyrophosphate (DMAPP) essential building blocks of all isoprenoids synthesized in the …