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Key Documents

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H0261

Sigma-Aldrich

DL-β-Hydroxybutyryl coenzyme A lithium salt

≥90%

Sinónimos:

DL-3- hydroxybutyryl Coenzyme A lithium salt

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About This Item

Fórmula empírica (notación de Hill):
C25H42N7O18P3S
Número de CAS:
103404-51-9
Peso molecular:
853.62
MDL number:
MFCD00079336
UNSPSC Code:
41106305
PubChem Substance ID:
24895396
NACRES:
NA.51

assay

≥90%

storage temp.

−20°C

SMILES string

[Li].CC(O)CC(=O)SCCNC(=O)CCNC(=O)C(O)C(C)(C)COP(O)(=O)OP(O)(=O)OCC1OC(C(O)C1OP(O)(O)=O)n2cnc3c(N)ncnc23

InChI

1S/C25H42N7O18P3S.Li.H/c1-13(33)8-16(35)54-7-6-27-15(34)4-5-28-23(38)20(37)25(2,3)10-47-53(44,45)50-52(42,43)46-9-14-19(49-51(39,40)41)18(36)24(48-14)32-12-31-17-21(26)29-11-30-22(17)32;;/h11-14,18-20,24,33,36-37H,4-10H2,1-3H3,(H,27,34)(H,28,38)(H,42,43)(H,44,45)(H2,26,29,30)(H2,39,40,41);;

Inchi Key

HNPHARRBSFXZAL-UHFFFAOYSA-N

Application

DL-β-Hydroxybutyryl coenzyme A lithium salt has been used:

  • as a substrate in the HSD17B4 protein enzymatic assay
  • as a substrate to determine the specificity and kinetics of Hc-DHS-28 and its mutation proteins
  • as a component of the reaction buffer in S-adenosyl-L-homocysteine hydrolase (AHCY) in vitro acylation

Biochem/physiol Actions

3-Hydroxybutyryl coenzyme A (HBCoA) is converted to bacterial polyhydroxyalkanoates (PHB) by polyhydroxybutyrate (PHB) synthases. 3-Hydroxybutyryl coenzyme A is a substrate used to measure the specificity and kinetics of β-hydroxyacyl CoA dehydrogenase.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Ping Li et al.
Biochemistry, 48(39), 9202-9211 (2009-08-29)
Polyhydroxybutyrate (PHB) synthases catalyze the conversion of 3-hydroxybutyryl coenzyme A (HBCoA) to PHB with a molecular mass of 1.5 MDa. The class III synthase from Allochromatium vinosum is a tetramer of PhaEPhaC (each 40 kDa). The polymerization involves covalent catalysis
Kesaven Bhubalan et al.
Applied and environmental microbiology, 77(9), 2926-2933 (2011-03-15)
The synthesis of bacterial polyhydroxyalkanoates (PHA) is very much dependent on the expression and activity of a key enzyme, PHA synthase (PhaC). Many efforts are being pursued to enhance the activity and broaden the substrate specificity of PhaC. Here, we
An Artemisinin Derivative ART1 Induces Ferroptosis by Targeting the HSD17B4 Protein Essential for Lipid Metabolism and Directly Inducing Lipid Peroxidation
Xie J, et al.
CCS Chemistry, 4(1), 304-317 (2022)
Yi Yang et al.
International journal for parasitology, 50(12), 945-957 (2020-08-29)
Haemonchus contortus could enter the diapause stage to avoid hostile conditions, however the inducing mechanism still remains poorly understood. A similar dauer strategy exists in Caenorhabditis elegans, and dauer phenomones, which are produced through a four step cycle of peroxisomal
Der-Shyan Sheu et al.
Analytical biochemistry, 393(1), 62-66 (2009-06-17)
This study presents a method to detect active polyhydroxyalkanoate (PHA) synthase on a polyacrylamide gel that combines the polyhydroxybutyrate (PHB) polymerization reaction with Sudan Black B staining. After separation of the protein samples on a modified sodium dodecyl sulfate-polyacrylamide gel
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