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L-Lyxose

$52

  • Brand : BIOFRON

  • Catalogue Number : BN-O1301

  • Specification : 98%(HPLC)

  • CAS number : 1949-78-6

  • Formula : C5H10O5

  • Molecular Weight : 150.13

  • PUBCHEM ID : 644176

  • Volume : 20mg

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Catalogue Number

BN-O1301

Analysis Method

Specification

98%(HPLC)

Storage

2-8°C

Molecular Weight

150.13

Appearance

Botanical Source

Structure Type

Category

SMILES

C(C(C(C(C=O)O)O)O)O

Synonyms

D-glyceraldehyde/Lyxose/D-glycerose/Lyxose, L-/rechtsdrehende Lyxose/L-Lyxose/Triose/D-aldotriose/L-(+)-Lyxose/aldehydo-L-lyxose/L-lyxo-2,3,4,5-Tetrahydroxy-valeraldehyd

IUPAC Name

(2R,3R,4S)-2,3,4,5-tetrahydroxypentanal

Density

1.5±0.1 g/cm3

Solubility

Flash Point

219.2±23.3 °C

Boiling Point

415.5±38.0 °C at 760 mmHg

Melting Point

108-112ºC(lit.)

InChl

InChl Key

PYMYPHUHKUWMLA-YUPRTTJUSA-N

WGK Germany

RID/ADR

HS Code Reference

Personal Projective Equipment

Correct Usage

For Reference Standard and R&D, Not for Human Use Directly.

Meta Tag

provides coniferyl ferulate(CAS#:1949-78-6) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

No Technical Documents Available For This Product.

PMID

1650346

Abstract

Escherichia coli cannot grow on L-lyxose, a pentose analog of the 6-deoxyhexose L-rhamnose, which supports the growth of this and other enteric bacteria. L-Rhamnose is metabolized in E. coli by a system that consists of a rhamnose permease, rhamnose isomerase, rhamnulose kinase, and rhamnulose-1-phosphate aldolase, which yields the degradation products dihydroxyacetone phosphate and L-lactaldehyde. This aldehyde is oxidized to L-lactate by lactaldehyde dehydrogenase. All enzymes of the rhamnose system were found to be inducible not only by L-rhamnose but also by L-lyxose. L-Lyxose competed with L-rhamnose for the rhamnose transport system, and purified rhamnose isomerase catalyzed the conversion of L-lyxose into L-xylulose. However, rhamnulose kinase did not phosphorylate L-xylulose sufficiently to support the growth of wild-type E. coli on L-lyxose. Mutants able to grow on L-lyxose were analyzed and found to have a mutated rhamnulose kinase which phosphorylated L-xylulose as efficiently as the wild-type enzyme phosphorylated L-rhamnulose. Thus, the mutated kinase, mapped in the rha locus, enabled the growth of the mutant cells on L-lyxose. The glycolaldehyde generated in the cleavage of L-xylulose 1-phosphate by the rhamnulose-1-phosphate aldolase was oxidized by lactaldehyde dehydrogenase to glycolate, a compound normally utilized by E. coli.

Title

L-lyxose metabolism employs the L-rhamnose pathway in mutant cells of Escherichia coli adapted to grow on L-lyxose.

Author

Badia J1, Gimenez R, Baldoma L, Barnes E, Fessner WD, Aguilar J.

Publish date

1991 Aug

PMID

21946936

Abstract

A critical step in the synthesis of the rare sugars, L-lyxose and L-ribose, from the corresponding D-sugars is the oxidation to the lactone. Instead of conventional oxidizing agents like bromine or pyridinium dichromate, it was found that a heterogeneous catalyst, Pd-Bi/C, could be used for the direct oxidation with molecular oxygen. The composition of the catalyst was optimized and the best results were obtained with 5 : 1 atomic ratio of Pd : Bi. The overall yields of the five-step procedure to L-ribose and L-lyxose were 47% and 50%, respectively. The synthetic procedure is advantageous from the viewpoint of overall yield, reduced number of steps, and mild reaction conditions. Furthermore, the heterogeneous oxidation catalyst can be easily separated from the reaction mixture and reused with no loss of activity.

Title

A heterogeneous Pd-Bi/C catalyst in the synthesis of L-lyxose and L-ribose from naturally occurring D-sugars.

Author

Fan A1, Jaenicke S, Chuah GK.

Publish date

2011 Oct 26

PMID

7961955

Abstract

A silent gene encoding a kinase that specifically phosphorylates L-xylulose was activated and rendered constitutive in mutant cells of Escherichia coli. L-Xylulose kinase was purified to homogeneity and found to be a dimer of two subunits of 55 kDa, highly specific for L-xylulose with a Km of 0.8 mM, a Vmax of 33 mumol/min/mg, and an optimum pH of 8.4. Physical (thin layer chromatography) and spectroscopic (nuclear magnetic resonance and optical rotation) characterization of the product of L-xylulose kinase indicated that the enzyme phosphorylated the sugar at position 5. The gene encoding L-xylulose kinase was mapped in the 80.2 min region of the chromosome by conjugation and transduction. Cloning and comparison of the restriction map with the Kohara map (Kohara, Y., Akiyame, K., and Isono, K. (1987) Cell 50, 495-501) located the gene between positions 3963 and 3965 kilobases. The molecular and functional features of L-xylulose kinase together with the location of the corresponding gene indicate that this enzyme did not derive from mutation of any other known kinase. The new kinase opens a route for the utilization of L-lyxose through the action of rhamnose permease, rhamnose isomerase, and the phosphorylation of the L-xylulose formed to L-xylulose 5-phosphate, which is then introduced into the pentose phosphate pathway for subsequent metabolism.

Title

Activation of a cryptic gene encoding a kinase for L-xylulose opens a new pathway for the utilization of L-lyxose by Escherichia coli.

Author

Sanchez JC1, Gimenez R, Schneider A, Fessner WD, Baldomà L, Aguilar J, Badia J.

Publish date

1994 Nov 25


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