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A5298

Sigma-Aldrich

3-Acetylpyridine hypoxanthine dinucleotide

~97%

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Empirical Formula (Hill Notation):
C22H27N5O15P2
CAS Number:
4002-09-9
Molecular Weight:
663.42
MDL number:
MFCD00078884
PubChem Substance ID:
24890966
NACRES:
NA.51

Assay

~97%

form

solid

storage temp.

−20°C

SMILES string

CC(=O)C1=CC=C[N](=C1)C2OC(COP(O)(=O)OP(O)(=O)OCC3OC(C(O)C3O)n4cnc5C(=O)N=CNc45)C(O)C2O

InChI

1S/C22H28N5O15P2/c1-10(28)11-3-2-4-26(5-11)21-17(31)15(29)12(40-21)6-38-43(34,35)42-44(36,37)39-7-13-16(30)18(32)22(41-13)27-9-25-14-19(27)23-8-24-20(14)33/h2-5,8-9,12-13,15-18,21-22,29-32H,6-7H2,1H3,(H,34,35)(H,36,37)(H,23,24,33)

InChI key

CRRQTCXZYOYDAM-UHFFFAOYSA-N

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This Item
772437665851425990
3-Acetylpyridine hypoxanthine dinucleotide ~97%

Sigma-Aldrich

A5298

3-Acetylpyridine hypoxanthine dinucleotide

Fmoc-Thr[GalNAc(Ac)3-α-D]-OH 97%

Sigma-Aldrich

772437

Fmoc-Thr[GalNAc(Ac)3-α-D]-OH

3-(Methylamino)benzoic acid 97%

Sigma-Aldrich

665851

3-(Methylamino)benzoic acid

3-Amino-2-chlorobenzoic acid 97%

Sigma-Aldrich

425990

3-Amino-2-chlorobenzoic acid

form

solid

form

solid

form

solid

form

solid

storage temp.

−20°C

storage temp.

−20°C

storage temp.

-

storage temp.

-

Application

3-Acetylpyridine hypoxanthine dinucleotide is an analogue of nicotinamide adenine dinucleotide (NAD) which may be used in mechanistic studies of NAD-dependent enzymes and enzymes that act upon NAD itself.

Linkage

Analog of β-NAD

Pictograms

Exclamation mark
GHS07

Signal Word

Warning

Hazard Statements

H315 - H319 - H335

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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G G Chang et al.
Archives of biochemistry and biophysics, 284(2), 285-291 (1991-02-01)
Initial velocity, product inhibition, and substrate inhibition studies suggest that the endogenous lactate dehydrogenase activity of duck epsilon-crystallin follows an order Bi-Bi sequential mechanism. In the forward reaction (pyruvate reduction), substrate inhibition by pyruvate was uncompetitive with inhibition constant of
T Gomi et al.
Biochimica et biophysica acta, 994(2), 172-179 (1989-02-02)
Rat liver S-adenosylhomocysteinase, a homotetramer, was resolved by treatment with acid ammonium sulfate into apoenzyme and NAD. The apoenzyme thus prepared retained a tetrameric structure but differed in the mobility on nondenaturing polyacrylamide gel electrophoresis. The inactive apoenzyme was reactivated
H J Lee et al.
The Biochemical journal, 245(2), 407-414 (1987-07-15)
The structural requirements of the NADP+ molecule as a coenzyme in the oxidative decarboxylation reaction catalysed by pigeon liver malic enzyme were studied by kinetic and fluorimetric analyses with various NADP+ analogues and fragments. The substrate L-malate had little effect
S L Oei et al.
FEBS letters, 397(1), 17-21 (1996-11-11)
Poly(ADP-ribosyl) transferase (pADPRT) catalyzes the transfer of the ADP-ribose moiety from NAD+ onto proteins as well as onto protein-bound ADP-ribose. As a result, protein-bound polymers of ADP-ribose are formed. pADPRT itself contains several acceptor sites for ADP-ribose polymers and may

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