6244-91-3

Basic information

• Product Name: isovaleryl coenzyme a lithium salt hydrate
• Synonyms: isovaleryl coenzyme a lithium salt hydrate;[5-(6-aminopurin-9-yl)-4-hydroxy-2-[[hydroxy-[hydroxy-[3-hydroxy-2,2-dimethyl-3-[2-[2-(3-methylbutanoylsulfanyl)ethylcarbamoyl]ethylcarbamoyl]propoxy]-phosphoryl]oxy-phosphoryl]oxymethyl]oxolan-3-yl]oxyphosphonic acid;Isovaleryl-CoA;isovaleryl-coenzyme A;IV-CoA
• CAS NO: 6244-91-3
• Molecular Formula: C₂₆H₄₄N₇O₁₇P₃S
• Molecular Weight: 851.65
• Mol File: 6244-91-3.mol
• Article Data: 5

Chemical Properties

• Appearance: /
• Density: 1.8g/cm³
• Refractive Index: 1.693
• Storage Temp.: -20°C
• CAS DataBase Reference: isovaleryl coenzyme a lithium salt hydrate(CAS DataBase Reference)
• NIST Chemistry Reference: isovaleryl coenzyme a lithium salt hydrate(6244-91-3)
• EPA Substance Registry System: isovaleryl coenzyme a lithium salt hydrate(6244-91-3)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 6244-91-3(Hazardous Substances Data)

Usage

Uses

Isovaleryl coenzyme A (IV-CoA ) lithium salt hydrate may be used:as substrate for β-Hydroxy-β-methylbutyric acid synthesis in cell-free extracts from G. reessiiin high-performance liquid chromatography (HPLC) for the characterization of IV-CoA from lymphocytesas a substrate in isovaleryl-CoA dehydrogenase assay

Definition

ChEBI: A methylbutanoyl-CoA is the S-isovaleryl derivative of coenzyme A.

General Description

Isovaleryl coenzyme A, an intermediate of the leucine catabolism. It is synthesized from β-methylbutyric acid by the action of enzyme acyl CoA synthetase. The conversion of isovaleryl-CoA to methylcrotonyl-CoA is catalyzed by the enzyme isovaleryl-CoA dehydrogenase in leucine catabolism pathway. The enzyme isovaleryl-CoA oxidase also calalyzes this conversion in fatty acid β-oxidation pathway.

InChI:InChI=1/C26H44N7O17P3S/c1-14(2)9-17(35)54-8-7-28-16(34)5-6-29-24(38)21(37)26(3,4)11-47-53(44,45)50-52(42,43)46-10-15-20(49-51(39,40)41)19(36)25(48-15)33-13-32-18-22(27)30-12-31-23(18)33/h12-15,19-21,25,36-37H,5-11H2,1-4H3,(H,28,34)(H,29,38)(H,42,43)(H,44,45)(H2,27,30,31)(H2,39,40,41)/t15-,19-,20-,21+,25-/m1/s1

Upstream product

• 503-74-2 3-methylbutyric acid 
• 85-61-0 coenzyme A 
• 137415-16-8 2,2-dimethylpropionyl-CoA 
• 816-66-0 4-methyl-2-oxopentanoic acid 
• 10364-92-8 1-(1H-imidazol-1-yl)-3-methylbutan-1-one 

Downstream Products

• 16284-60-9 N-isovaleryl glycine 
• 85-61-0 coenzyme A 

Relevant articles and documents

Identification of an α-Oxoamine Synthase and a One-Pot Two-Step Enzymatic Synthesis of α-Amino Ketones

Alb29, an α-oxoamine synthase involved in albogrisin biosynthesis in Streptomyces albogriseolus MGR072, was characterized and responsible for the incorporation of l-glutamate to acyl-coenzyme A substrates. Combined with Alb29 and Mgr36 (an acyl-coenzyme A ligase), a one-pot enzymatic system was established to synthesize seven α-amino ketones. When these α-amino ketones were fed into the alb29 knockout strain Δalb29, respectively, the albogrisin analogs with different side chains were observed.

Novel coenzyme B12-dependent interconversion of isovaleryl-CoA and pivalyl-CoA

5′-Deoxyadenosylcobalamin (AdoCbl)-dependent isomerases catalyze carbon skeleton rearrangements using radical chemistry. We have recently characterized a fusion protein that comprises the two subunits of the AdoCbl-dependent isobutyryl- CoA mutase flanking a G-protein chaperone and named it isobutyryl-CoA mutase fused (IcmF). IcmF catalyzes the interconversion of isobutyryl-CoA and n-butyryl-CoA, whereas GTPase activity is associated with its G-protein domain. In this study, we report a novel activity associated with IcmF, i.e. the interconversion of isovaleryl-CoA and pivalyl-CoA. Kinetic characterization of IcmF yielded the following values: a Km for isovaleryl-CoA of 62 ± 8 μM and Vmax of 0.021 ± 0.004 μmol min-1 mg-1 at 37 ° C. Biochemical experiments show that an IcmF in which the base specificity loop motif NKXD is modified to NKXE catalyzes the hydrolysis of both GTP and ATP. IcmF is susceptible to rapid inactivation during turnover, and GTP conferred modest protection during utilization of isovaleryl-CoA as substrate. Interestingly, there was no protection from inactivation when either isobutyryl-CoA or n-butyryl-CoA was used as substrate. Detailed kinetic analysis indicated that inactivation is associated with loss of the 5′-deoxyadenosine moiety from the active site, precluding reformation of AdoCbl at the end of the turnover cycle. Under aerobic conditions, oxidation of the cob(II)alamin radical in the inactive enzyme results in accumulation of aquacobalamin. Because pivalic acid found in sludge can be used as a carbon source by some bacteria and isovaleryl- CoA is an intermediate in leucine catabolism, our discovery of a new isomerase activity associated with IcmF expands its metabolic potential.

Biosynthesis of branched-chain fatty acid in bacilli: FabD (malonyl-CoA:ACP transacylase) is not essential for in vitro biosynthesis of branched-chain fatty acids.

It was found that the partially purified beta-ketoacyl-ACP synthase of Bacillus insolitus did not require the addition of FabD (malonyl-CoA:ACP transacylase, MAT) for the activity assay. This study therefore examined the necessity of FabD protein for in vitro branched-chain fatty acid (BCFA) biosynthesis by crude fatty acid synthetases (FAS) of Bacilli. To discover the involvement of FabD in the BCFA biosynthesis, the protein was removed from the crude FAS by immunoprecipitation. The His-tag fusion protein FabD of Bacillus subtilis was expressed in Escherichia coli and used for the preparation of antibody. The rabbit antibody raised against the expressed fusion protein specifically recognized the FabD in the crude FAS of B. subtilis. Evaluation of the efficacy of the immunoprecipitation showed that a trace of FabD protein was present in the antibody-treated crude FAS. However, this complete removal of FabD from the crude FAS did not abolish its BCFA biosynthesis, but only reduced the level to 50-60% of the control level for acyl-CoA primer and to 80% for alpha-keto-beta-methylvalerate primer. Furthermore, the FabD concentration did not necessarily correlate with the MAT specific activity in the enzyme fractions, suggesting the presence of another enzyme source of MAT activity. This study, therefore, suggests that FabD is not the sole enzyme source of MAT for in vitro BCFA biosynthesis, and implies the existence of a functional connection between fatty acid biosynthesis and another metabolic pathway.