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Key Documents

C2643

Sigma-Aldrich

Coenzyme A, oxidized lithium salt

≥85%

Synonyme(s) :

CoA-S-S-CoA

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About This Item

Formule empirique (notation de Hill):
C42H70N14O32P6S2 · xLi+
Numéro CAS:
31664-36-5
Poids moléculaire :
1533.05 (free acid basis)
Code UNSPSC :
41106305
ID de substance PubChem :
24892510
Nomenclature NACRES :
NA.51

Pureté

≥85%

Forme

solid

Température de stockage

−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

Clé InChI

YAISMNQCMHVVLO-ODFVJXNFSA-N

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Catégories apparentées

Description générale

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.

Actions biochimiques/physiologiques

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.

Pictogrammes

Corrosion
GHS05

Mention d'avertissement

Danger

Mentions de danger

H315,H318

Classification des risques

Eye Dam. 1 - Skin Irrit. 2

Code de la classe de stockage

4.1B - Flammable solid hazardous materials

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Acétyl-coenzyme A lithium salt ≥93% (HPLC)

Sigma-Aldrich

A2181

Acétyl-coenzyme A lithium salt

Acétyl-coenzyme A 85% (Enzymatic and Absorbance), 2% (lithium)

Roche

ACOA-RO

Acétyl-coenzyme A

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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