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G5131

Sigma-Aldrich

Guanosine 5′-diphospho-D-mannose sodium salt from Saccharomyces cerevisiae

Type I, ≥97% (HPLC)

Sinonimo/i:

GDP-Man, GDP-mannose

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About This Item

Formula condensata:
C16H23N5O16P2Na2
Numero CAS:
103301-73-1
Peso molecolare:
649.30
Numero MDL:
MFCD00070120
Codice UNSPSC:
41106305
ID PubChem:
24895196
NACRES:
NA.51

Tipo

Type I

Saggio

≥97% (HPLC)

Temperatura di conservazione

−20°C

Stringa SMILE

[Na].NC1=NC(=O)c2ncn(C3OC(COP(O)(=O)OP(O)(=O)OC4OC(CO)C(O)C(O)C4O)C(O)C3O)c2N1

InChI

1S/C16H25N5O16P2.Na.H/c17-16-19-12-6(13(28)20-16)18-3-21(12)14-10(26)8(24)5(34-14)2-33-38(29,30)37-39(31,32)36-15-11(27)9(25)7(23)4(1-22)35-15;;/h3-5,7-11,14-15,22-27H,1-2H2,(H,29,30)(H,31,32)(H3,17,19,20,28);;
MEXITZOHWLXZKR-UHFFFAOYSA-N

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Descrizione generale

Guanosine 5′-diphospho-D-mannose (GDP-D-mannose) is present in high cytosolic levels in Saccharomyces cerevisiae. It is crucial for protein mannosylation. GDP-D-mannose is an important precursor to produce GDP-l-fucose.

Applicazioni

Guanosine 5′-diphospho-D-mannose sodium salt from Saccharomyces cerevisiae has been used as a nucleotide sugar in transglycosylation enzymatic assay and hydrolysis based catalytic reactions with S-glycosyltransferases (SunS).
Guanosine 5′-diphospho-D-mannose sodium salt has been used as a component of ATP regeneration system for in vitro vesicle formation from Saccharomyces cerevisiae microsomes. It has also been used as a component of the buffer for mannosyl transferase activity assay.

Azioni biochim/fisiol

Guanosine diphosphate mannose (GDP-mannose) is a nucleotide sugar substrate for glycosyltransferase (mannosylation) reactions mediated by mannosyltransferases.

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Certificati d'analisi (COA)

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Articoli

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The presence of multiple functional groups and stereocenters in complex carbohydrates makes them challenging targets for the organic chemist.

Glycosyltransferases

Glycosyltransferases were initially considered to be specific for a single glycosyl donor and acceptor, which led to the one enzyme-one linkage concept. Subsequent observations have refuted the theory of absolute enzymatic specificity by describing the transfer of analogs of some nucleoside mono- or diphosphate sugar donors.

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