Preparation of <i>L</i>(+) β‐hydroxyisobutyric acid by bacterial oxidation of isobutyric acid

Goodhue, C. T.; Schaeffer, J.

doi:10.1002/bit.260130204

Cited by 104 publications

(40 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Separation of the R and S isomers of 3-hydroxyisobutyrate and of 2-(hydroxymethyl)butyrate was achieved using the trifluoroacetyl-/-menthyl derivatives (Kamerling et al, 1977) and a 25 m fused silica capillary column with a polar bonded stationary phase (BPI0, SGE Pty., North Melbourne, Australia). S-3-Hydroxyisobutyrate was obtained by the oxidation of isobutyrate by Pseudomonas putida ATCC 21244 (Goodhue and Schaeffer, 1971). The oxidation of R,S-2-methylbutyrate by this organism gave 2-(hydroxymethyl)butyrate as the enantiomer which on gas chromatography as the/-menthyl-trifluoroacetyl derivative had the shorter retention time.…”

Section: Laboratory Methodsmentioning

confidence: 99%

Excessive excretion of β‐alanine and of 3‐hydroxypropionic,R‐ andS‐3‐aminoisobutyric,R‐ andS‐3‐hydroxyisobutyric andS‐2‐(hydroxymethyl)butyric acids probably due to a defect in the metabolism of the corresponding malonic semialdehydes

Pollitt¹,

Green

Smith

1984

J of Inher Metab Disea

View full text Add to dashboard Cite

A new metabolic disorder characterised by the excessive excretion of beta-alanine, 3-hydroxypropionic acid, R- and S-3-amino- and 3-hydroxyisobutyric acids and S-2-(hydroxymethyl)butyric acid is probably due to deficient activities of malonic, methylmalonic and ethylmalonic semialdehyde dehydrogenases. These dehydrogenation reactions could be mediated by one enzyme, or by enzymes with a common subunit, and both R- and S-methylmalonic semialdehydes seem to be equally affected. The patient is now aged 4 years and has developed normally. He has a persistent gross hypermethioninaemia which is probably unrelated to the other biochemical abnormalities.

show abstract

Section: Laboratory Methodsmentioning

confidence: 99%

Excessive excretion of β‐alanine and of 3‐hydroxypropionic,R‐ andS‐3‐aminoisobutyric,R‐ andS‐3‐hydroxyisobutyric andS‐2‐(hydroxymethyl)butyric acids probably due to a defect in the metabolism of the corresponding malonic semialdehydes

Pollitt¹,

Green

Smith

1984

J of Inher Metab Disea

View full text Add to dashboard Cite

show abstract

“…[19] (ee up to 97%), the asymmetric reduction of ethyl 4,4-dimethoxy-3-methylcrotonate using bakers yeast [20] and the stereoseletive (formal) b-hydroxylation of isobutyric acid using Pseudomonas putida (ATCC 21244). [21] All of these biotransformations were performed using whole (fermenting) microbial cells with several enzymes being involved. Only recently, was it shown that a non-flavin NADH-dependent D 4,5 -steroid 5b-reductase from Arabidopsis thaliana was able to reduce ethyl 2-hydroxymethylacrylate, however, the stereochemistry of the product was not examined in regard to its absolute configuration and enantiomeric composition.…”

mentioning

confidence: 99%

Asymmetric Synthesis of (R)‐3‐Hydroxy‐2‐methylpropanoate (‘Roche Ester’) and Derivatives via Biocatalytic CC‐Bond Reduction

et al. 2010

View full text Add to dashboard Cite

Enoate reductases from the old yellow enzyme family were employed for the asymmetric bioreduction of methyl 2-hydroxymethylacrylate and its O-allyl, O-benzyl and O-TBDMS derivatives to furnish (R)-configurated methyl 3-hydroxy-2-methylpropionate products in up to > 99% ee Variation of the O-protective group had little influence on the stereoselectivity, but a major impact on the reaction rate.Keywords: biocatalysis; C=C-bioreduction; enoate reductase; old yellow enzyme; substrate engineeringThe asymmetric reduction of C=C bonds creates (up to) two chiral carbon centres and is thus one of the most widely employed strategies for the production of chiral materials. The biocatalytic variant, which is applicable to activated alkenes bearing an electron-withdrawing substituent is catalysed by enoate reductases [EC 1.3.1.X], [1,2] which are members of the old yellow enzyme (OYE) family.[3] Over the past few years, increasing attention has been devoted to these flavoproteins [4] in view of their substrate scope, [5] encompassing a,b-unsaturated carbonyl compounds (such as enals and enones), as well as carboxylic acids and derivatives thereof (such as esters, cyclic imides, nitriles, lactones) and nitroalkenes. As a rule of thumb, the degree of activation of the C=C-bond exerted by the electron-withdrawing effect of the activating substituent goes hand in hand with the substrate acceptance, which ensures generally fast reaction rates for enals, enones and nitroalkenes, whereas (di)carboxylic acids and esters are transformed more slowly.To illustrate the importance of this enzyme class for asymmetric synthesis, we aimed at their applicability for an industrially relevant product, that is, (R)-3-hydroxy-2-methylpropanoate, which is commonly denoted as the Roche ester. The latter is a popular chiral building block for the synthesis of vitamins (e.g., a-tocopherol [6] ), fragrance components (e.g., muscone [7] ), and antibiotics (e.g., calcimycin, [8] palinurin, [9] rapamycin, [10] 13-deoxytedanolide, [11] dictyostatin [12] ) and natural products (e.g., spiculoic acid A [13] ). Classical methods for its preparation include the diastereoselective addition of non-racemic alcohols as chiral auxiliaries, [14] the transformation of a chiral homoallylic acetate [15] or involve aldol condensation [16] and -most prominent -the transition metal-catalysed asymmetric hydrogenation of acrylate esters using Rh [17] (ee up to 99%) or Ru [18] (ee up to 94%). For the biocatalytic synthesis of the Roche ester only few examples are reported: the stereoselective oxidation of 2-methyl-1,3-propanediol by Gluconobacter and Acetobacter spp. [19] (ee up to 97%), the asymmetric reduction of ethyl 4,4-dimethoxy-3-methylcrotonate using bakers yeast [20] and the stereoseletive (formal) b-hydroxylation of isobutyric acid using Pseudomonas putida (ATCC 21244).[21] All of these biotransformations were performed using whole (fermenting) microbial cells with several enzymes being involved. Only recently, was it shown that a non-flavin NADH-dependen...

show abstract

“…Reference isobutyric acid SP seudomonas putida 3.7 37 [8] 2-methyl-1,3-propanediol RA cetobacter sp.6 .3 75 [9] isobutyric acid SP seudomonas putida IBA-1 9.0 50 [10] isobutyric acid SY arrowia lipolytica KCCM50506 49.0 n.d. [24] methacrylic acid RC andida rugose 65.0 40 [12] methacrylic acid RC andida rugose 150.0 82 [11] Figure 6. Possible pathways for the synthesis of (S)-3-hydroxyisobutyric acid from glucose using 2-ketoisovalerate as intermediatei nP.…”

Section: Substratementioning

confidence: 99%

“…Goodhue and colleagues utilized the soil isolate Pseudomonas putida IBA-1 for (S)-3-HIBAsynthesis and achieved aspecif- ic activity of about 16 Ug cdw À1 L À1 during the biotransformation of isobutyric acid. [10] Thes train IBA-1 was isolated from enrichment cultures grown on isobutyric acid as ac arbon source. This strategyf inally resulted in high volumetric productivities,b ut lowc onversion yields (< 50%), due to the activity of intrinsic 3-hydroxyisobutyrate dehydrogenase(s).…”

Section: (S)-3-hibasynthesis From Isobutyric Acidmentioning

confidence: 99%

“…Up to now the biological production of this compound via biotransformations starting from isobutyric acid, methacrylic acid or 2-methyl-1,3-propanediol in different hostsw as demonstrated. [2,[8][9][10][11][12] However, conversion yields often sufferf rom product degradation during the reaction, due to the activity of 3-hydroxisobutyric acid converting enzymes in the respective host. Examples for the fermentativep roduction of 3-HIBAd irectly from glucose,t ot he best of our knowledge,d on ot exist.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Multistep Synthesis of (S)‐3‐Hydroxyisobutyric Acid from Glucose usingPseudomonas taiwanensisVLB120 B83 T7 Catalytic Biofilms

2015

View full text Add to dashboard Cite

Thec hiral building block (S)-3-hydroxyisobutyric acid [(S)-3-HIBA] was produced either by conversion of isobutyric acid or directly from glucose utilizing cells of Pseudomonas taiwanensis VLB120 B83 T7 as catalysts.T his strain carriesapoint mutation in the gene encoding 3-hydroxyisobutyrate dehydrogenase (mmsB), leading to its inactivation.T he maximal specific activity in resting-cell biotransformations using isobutyric acid as substrate was 4.9 AE 0.4 Ug cdw À1 .O verexpression of the 2-ketoisovalerate pathwayg enes alsS,i lvC, and ilvD,a nd the introduction of kivd encoding 2-ketoacid decarboxylase resulted in the efficient fermentatives ynthesiso f( S )-3-HIBAd irectly from glucose.U pt o2 2mM( 2.3 g L À1 ) (S)-3-HIBAwere produceda t3 .7 AE 0.3 Ug cdw À1 in repeated batch experiments without observable product degradation. Utilizing ab iofilm reactor it was possible to continuously produce up to.O verall, the conversion of isobutyric acid to (S)-3-HIBAw as found to be the rate-limiting step,l eading to the accumulation of am ixture of (S)-3-hydroxyisobutyric acid andi sobutyric acid. This study demonstratesf or the first time the production of (S)-3-HIBAf rom renewable carbon in shake flasks and biofilm reactors and sets the stage for furthero ptimizations towards the efficient production of 3-HIBAa nd its derivatives in continuous fermentations.

show abstract

Preparation of L(+) β‐hydroxyisobutyric acid by bacterial oxidation of isobutyric acid

Cited by 104 publications

References 7 publications

Excessive excretion of β‐alanine and of 3‐hydroxypropionic,R‐ andS‐3‐aminoisobutyric,R‐ andS‐3‐hydroxyisobutyric andS‐2‐(hydroxymethyl)butyric acids probably due to a defect in the metabolism of the corresponding malonic semialdehydes

Excessive excretion of β‐alanine and of 3‐hydroxypropionic,R‐ andS‐3‐aminoisobutyric,R‐ andS‐3‐hydroxyisobutyric andS‐2‐(hydroxymethyl)butyric acids probably due to a defect in the metabolism of the corresponding malonic semialdehydes

Asymmetric Synthesis of (R)‐3‐Hydroxy‐2‐methylpropanoate (‘Roche Ester’) and Derivatives via Biocatalytic CC‐Bond Reduction

Multistep Synthesis of (S)‐3‐Hydroxyisobutyric Acid from Glucose usingPseudomonas taiwanensisVLB120 B83 T7 Catalytic Biofilms

Contact Info

Product

Resources

About