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Key Documents

C2643

Sigma-Aldrich

Coenzyme A, oxidized lithium salt

≥85%

Sinónimos:

CoA-S-S-CoA

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About This Item

Fórmula empírica (notación de Hill):
C42H70N14O32P6S2 · xLi+
Número de CAS:
Peso molecular:
1533.05 (free acid basis)
UNSPSC Code:
41106305
PubChem Substance ID:
NACRES:
NA.51

Quality Level

assay

≥85%

form

solid

storage temp.

−20°C

InChI

1S/C42H70N14O32P6S2/c1-41(2,15-81-93(75,76)87-91(71,72)79-13-21-29(85-89(65,66)67)27(59)39(83-21)55-19-53-25-33(43)49-17-51-35(25)55)31(61)37(63)47-7-5-23(57)45-9-11-95-96-12-10-46-24(58)6-8-48-38(64)32(62)42(3,4)16-82-94(77,78)88-92(73,74)80-14-22-30(86-90(68,69)70)28(60)40(84-22)56-20-54-26-34(44)50-18-52-36(26)56/h17-22,27-32,39-40,59-62H,5-16H2,1-4H3,(H,45,57)(H,46,58)(H,47,63)(H,48,64)(H,71,72)(H,73,74)(H,75,76)(H,77,78)(H2,43,49,51)(H2,44,50,52)(H2,65,66,67)(H2,68,69,70)/t21-,22-,27-,28-,29-,30-,31+,32+,39-,40-/m1/s1

InChI key

YAISMNQCMHVVLO-ODFVJXNFSA-N

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General description

Coenzyme A (CoA) is a ubiquitous cofactor present in all living organisms. It is synthesized by the enzymatic conjugation of cysteine, pantothenate (Vitamin B5), and adenosine triphosphate (ATP).

Application

Coenzyme A oxidized lithium salt has been used in the preparation of the coenzyme A persulfide (CoASSH) standard to quantify the CoASSH in Staphylococcus aureus strains by tandem mass spectrometry.

Biochem/physiol Actions

Coenzyme A (CoA) plays a role as an acyl-group carrier and carbonyl activator in several biochemical reactions like the tricarboxylic acid cycle and fatty acid metabolism. It acts as a co-factor for several enzymes and is involved in several reactions in intermediary metabolism. CoA contains a thiol group that enables it to take part in several biochemical reactions. Oxidized CoA may be used to study reduction systems (CoA disulfide reductase (CoADR) systems) that regenerate reduced CoA in vivo. Furthermore, oxidized CoA may be used to study the unique functions of this molecule in vivo.

pictograms

Corrosion

signalword

Danger

hcodes

Hazard Classifications

Eye Dam. 1 - Skin Irrit. 2

Storage Class

4.1B - Flammable solid hazardous materials

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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S B delCardayre et al.
The Journal of biological chemistry, 273(10), 5752-5757 (1998-04-16)
The cdr gene encoding coenzyme A disulfide reductase (CoADR) from Staphylococcus aureus 8325-4 was cloned, sequenced, and overexpressed. The gene encodes a 438-amino acid polypeptide that has a calculated molecular weight of 49,200 and sequence similarity to the pyridine nucleotide-disulfide
T Conn Mallett et al.
Biochemistry, 45(38), 11278-11289 (2006-09-20)
Coenzyme A (CoASH) replaces glutathione as the major low molecular weight thiol in Staphylococcus aureus; it is maintained in the reduced state by coenzyme A-disulfide reductase (CoADR), a homodimeric enzyme similar to NADH peroxidase but containing a novel Cys43-SSCoA redox
Ivan Gout
Biochemical Society transactions, 47(1), 469-476 (2019-02-21)
Coenzyme A (CoA) is an indispensable cofactor in all living organisms. It is synthesized in an evolutionarily conserved pathway by enzymatic conjugation of cysteine, pantothenate (Vitamin B5), and ATP. This unique chemical structure allows CoA to employ its highly reactive
Jamie R Wallen et al.
Biochemistry, 47(18), 5182-5193 (2008-04-11)
We have recently reported that CoASH is the major low-molecular weight thiol in Bacillus anthracis [Nicely, N. I. , Parsonage, D., Paige, C., Newton, G. L., Fahey, R. C., Leonardi, R., Jackowski, S., Mallett, T. C., and Claiborne, A. (2007)
Dennis R Harris et al.
The FEBS journal, 272(5), 1189-1200 (2005-02-22)
We have cloned NADH oxidase homologues from Pyrococcus horikoshii and P. furiosus, and purified the recombinant form of the P. horikoshii enzyme to homogeneity from Escherichia coli. Both enzymes (previously referred to as NOX2) have been shown to act as

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