1-Deaza-fad

    WARNING: This product is for research use only, not for human or veterinary use.

Hodoodo CAT#: H581638

CAS#: 57818-88-9

Description: 1-Deaza-fad also known as Deazafad. 1-deazaFAD has comparable activity in the mutase reconstituted.

Chemical Structure

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1-Deaza-fad
CAS# 57818-88-9
Instruction

Theoretical Analysis

Hodoodo Cat#: H581638
Name: 1-Deaza-fad
CAS#: 57818-88-9
Chemical Formula: C28H34N8O15P2
Exact Mass: 784.16
Molecular Weight: 784.568
Elemental Analysis: C, 42.87; H, 4.37; N, 14.28; O, 30.59; P, 7.90

Price and Availability

This product is not in stock, which may be available by custom synthesis. For cost-effective reason, minimum order is 1g (price is usually high, lead time is 2~3 months, depending on the technical challenge). Quote less than 1g will not be provided. To request quote, please email to sales @hodoodo.com or click below button.
Note: Price will be listed if it is available in the future.

Request quote for custom synthesis

Synonym: 1-Deaza-fad; Deazafad; 1-deazaFAD ; 5-Deazariboflavin-5'-diphosphate.

IUPAC/Chemical Name: Adenosine 5'-(trihydrogen diphosphate), 5-5'-ester with 1-deoxy-1-(3,4-dihydro-7,8-dimethyl-2,4-dioxopyrimido(4,5-b)quinolin-10(2H)-yl)-D-ribitol

InChi Key: GLDULYQMIPGSPD-AUSFFQRRSA-N

InChi Code: InChI=1S/C28H34N8O15P2/c1-11-3-13-5-14-24(33-28(43)34-26(14)42)35(15(13)4-12(11)2)6-16(37)20(39)17(38)7-48-52(44,45)51-53(46,47)49-8-18-21(40)22(41)27(50-18)36-10-32-19-23(29)30-9-31-25(19)36/h3-5,9-10,16-18,20-22,27,37-41H,6-8H2,1-2H3,(H,44,45)(H,46,47)(H2,29,30,31)(H,34,42,43)/t16-,17+,18+,20-,21+,22+,27+/m0/s1

SMILES Code: C([C@@H]([C@@H]([C@@H](COP(OP(OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N2C=3C(N=C2)=C(N)N=CN3)(=O)O)(=O)O)O)O)O)N4C=5C(=CC=6C4=CC(C)=C(C)C6)C(=O)NC(=O)N5

Appearance: Solid powder

Purity: >98% (or refer to the Certificate of Analysis)

Shipping Condition: Shipped under ambient temperature as non-hazardous chemical. This product is stable enough for a few weeks during ordinary shipping and time spent in Customs.

Storage Condition: Dry, dark and at 0 - 4 C for short term (days to weeks) or -20 C for long term (months to years).

Solubility: Soluble in DMSO

Shelf Life: >3 years if stored properly

Drug Formulation: This drug may be formulated in DMSO

Stock Solution Storage: 0 - 4 C for short term (days to weeks), or -20 C for long term (months).

HS Tariff Code: 2934.99.03.00

More Info:

Biological target:
In vitro activity:
In vivo activity:

Preparing Stock Solutions

The following data is based on the product molecular weight 784.57 Batch specific molecular weights may vary from batch to batch due to the degree of hydration, which will affect the solvent volumes required to prepare stock solutions.

Recalculate based on batch purity %
Concentration / Solvent Volume / Mass 1 mg 5 mg 10 mg
1 mM 1.15 mL 5.76 mL 11.51 mL
5 mM 0.23 mL 1.15 mL 2.3 mL
10 mM 0.12 mL 0.58 mL 1.15 mL
50 mM 0.02 mL 0.12 mL 0.23 mL
Formulation protocol:
In vitro protocol:
In vivo protocol:

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Reconstitution Calculator

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1: Hassan-Abdallah A, Zhao G, Jorns MS. Role of the covalent flavin linkage in monomeric sarcosine oxidase. Biochemistry. 2006 Aug 8;45(31):9454-62. PubMed PMID: 16878980.

2: Hassan-Abdallah A, Bruckner RC, Zhao G, Jorns MS. Biosynthesis of covalently bound flavin: isolation and in vitro flavinylation of the monomeric sarcosine oxidase apoprotein. Biochemistry. 2005 May 3;44(17):6452-62. PubMed PMID: 15850379; PubMed Central PMCID: PMC1993914.

3: Huang Z, Zhang Q, Liu HW. Reconstitution of UDP-galactopyranose mutase with 1-deaza-FAD and 5-deaza-FAD: analysis and mechanistic implications. Bioorg Chem. 2003 Dec;31(6):494-502. PubMed PMID: 14613770.

4: Zhang H, Gruenke L, Arscott D, Shen A, Kasper C, Harris DL, Glavanovich M, Johnson R, Waskell L. Determination of the rate of reduction of oxyferrous cytochrome P450 2B4 by 5-deazariboflavin adenine dinucleotide T491V cytochrome P450 reductase. Biochemistry. 2003 Oct 14;42(40):11594-603. PubMed PMID: 14529269.

5: Zhang H, Gruenke L, Saribas AS, Im SC, Shen AL, Kasper CB, Waskell L. Preparation and characterization of a 5'-deazaFAD T491V NADPH-cytochrome P450 reductase. Biochemistry. 2003 Jun 10;42(22):6804-13. PubMed PMID: 12779335.

6: Poinas A, Gaillard J, Vignais P, Doussiere J. Exploration of the diaphorase activity of neutrophil NADPH oxidase. Eur J Biochem. 2002 Feb;269(4):1243-52. PubMed PMID: 11856358.

7: Rudik I, Thorpe C. Thioester enolate stabilization in the acyl-CoA dehydrogenases: the effect of 5-deaza-flavin substitution. Arch Biochem Biophys. 2001 Aug 15;392(2):341-8. PubMed PMID: 11488611.

8: Dwyer TM, Mortl S, Kemter K, Bacher A, Fauq A, Frerman FE. The intraflavin hydrogen bond in human electron transfer flavoprotein modulates redox potentials and may participate in electron transfer. Biochemistry. 1999 Jul 27;38(30):9735-45. PubMed PMID: 10423253.

9: Harris CM, Sanders SA, Massey V. Role of the flavin midpoint potential and NAD binding in determining NAD versus oxygen reactivity of xanthine oxidoreductase. J Biol Chem. 1999 Feb 19;274(8):4561-9. PubMed PMID: 9988690.

10: Tedeschi G, Chen S, Massey V. Active site studies of DT-diaphorase employing artificial flavins. J Biol Chem. 1995 Feb 10;270(6):2512-6. PubMed PMID: 7531691.

11: Pollegioni L, Ghisla S, Pilone MS. Studies on the active centre of Rhodotorula gracilis D-amino acid oxidase and comparison with pig kidney enzyme. Biochem J. 1992 Sep 1;286 ( Pt 2):389-94. PubMed PMID: 1356333; PubMed Central PMCID: PMC1132910.

12: Chanderkar LP, Jorns MS. Effect of flavin structure and redox state on catalysis by and flavin-pterin energy transfer in Escherichia coli DNA photolyase. Biochemistry. 1991 Jan 22;30(3):745-54. PubMed PMID: 1988061.

13: Prongay AJ, Williams CH Jr. Evidence for direct interaction between cysteine 138 and the flavin in thioredoxin reductase. A study using flavin analogs. J Biol Chem. 1990 Nov 5;265(31):18968-75. PubMed PMID: 2229055.

14: Krauth-Siegel RL, Schirmer RH, Ghisla S. FAD analogues as prosthetic groups of human glutathione reductase. Properties of the modified enzyme species and comparisons with the active site structure. Eur J Biochem. 1985 Apr 15;148(2):335-44. PubMed PMID: 3987692.

15: Ghisla S, Thorpe C, Massey V. Mechanistic studies with general acyl-CoA dehydrogenase and butyryl-CoA dehydrogenase: evidence for the transfer of the beta-hydrogen to the flavin N(5)-position as a hydride. Biochemistry. 1984 Jul 3;23(14):3154-61. PubMed PMID: 6466635.

16: O'Donnell ME, Williams CH Jr. Reconstitution of Escherichia coli thioredoxin reductase with 1-deazaFAD. Evidence for 1-deazaFAD C-4a adduct formation linked to the ionization of an active site base. J Biol Chem. 1984 Feb 25;259(4):2243-51. PubMed PMID: 6365906.

17: Detmer K, Schopfer LM, Massey V. Reactions of 1-deaza-FAD-substituted phenol hydroxylase and melilotate hydroxylase. J Biol Chem. 1984 Feb 10;259(3):1532-8. PubMed PMID: 6693423.

18: Pompon D, Guiard B, Lederer F. Reconstitution of liver NADH: cytochrome b5 oxidoreductase and of Desulfovibvio vulgaris flavodoxin with 1-carba-1-deazaflavin. Eur J Biochem. 1982 Nov 15;128(2-3):377-82. PubMed PMID: 7151784.

19: Entsch B, Husain M, Ballou DP, Massey V, Walsh C. Oxygen reactivity of p-hydroxybenzoate hydroxylase containing 1-deaza-FAD. J Biol Chem. 1980 Feb 25;255(4):1420-9. PubMed PMID: 6766449.