Methods for the production of tyrosine, cinnamic acid and para-hydroxycinnamics acid

a technology of cinnamic acid and tyrosine, which is applied in the field of molecular biology and microbiology, can solve the problems of time-consuming and cumbersome methods, and low supply of tyrosine, and achieves enhanced tal activity and enhanced tal activity

Inactive Publication Date: 2005-07-07
ORMON CORP +1
View PDF2 Cites 9 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

[0034] SEQ ID NO:23 is the nucleotide sequence encoding the mutant or modified R. glutinis PAL enzyme having enhanced TAL activity.
[0035] SEQ I...

Problems solved by technology

These methods are time consuming and cumbersome and a more facile method of production is needed for the large scale syn...

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Methods for the production of tyrosine, cinnamic acid and para-hydroxycinnamics acid

Examples

Experimental program
Comparison scheme
Effect test

example 1

Cloning and Expression of Chromobacterium violaceum Phenylalanine Hydroxylase in Microorganisms

Phenylalanine Hydroxylase for Chromobacterium violaceum DNA Amplification and Cloning:

[0124] In these studies the PAH gene of the Chromobacterium violaceum (SEQ ID NO:1) was cloned into both Pseudomonas aeruginosa (ATCC 15691) and DH5αE. coli. Two oligonucleotide primers, 5′-TCCAGGAGCCCAGGATCCAACGATCGCGCCGA-3′ [SEQ ID NO:5], (designated CVPH168), and 5′-GGACAAGCTTAATGATGCAGCGACACAT-3′ [SEQ ID NO:6], (designated CVPH1170) were synthesized based on the deoxynucleotide sequences flanking the coding region of the C. violaceum phenylalanine hydroxylase gene described previously (A. Onishi, L. J. Liotta, S. J. Benkovic; Cloning and Expression of Chromobacterium violaceum phenylalanine hydroxylase in Escherichia coli and comparison of amino acid sequence with mammalian aromatic amino acid hydroylase J. Biol. Chem. 266: 18454-18459 (1991)). Restriction endonuclease sites (BamHI or HindIII, unde...

example 11

Growth of E. coli AT271 Tyr-Auxotrophic Strain Following its Transformation with C. violaceum PAH and the Various Components of the P. aeruginosa PAH Operon

[0127] Agar plates containing M9 medium plus glucose were prepared. The tyrosine auxotrophic AT271 strain is incapable of growing on this plate in the absence of tyrosine (see Control-1). When a filter disc containing 1.0 mM tyrosine is added to the plate, growth is observed around the disc indicating the dependency of the organism to the presence of tyrosine (see Control-2). The AT271 recombinant strains used in this study included strains containing PhhA, PhhB, PhhC, PhhBC, PhhABC, PAH and PAH / PhhB / PhhC. The tyrosine disc was placed in the middle of each of the plates for these recombinants. For the strains containing PhhA, PhhB, PhhC, and PhhBC growth appeard only around the tyrosine disc indicating that these strains could not synthesize tyrosine and were still dependent on the external supply of this compound for growth. Ho...

example 12

The Effect of Iron on Growth and Tyrosine Production by Transformants of Phenylalanine Overproducing E. coli Containing the PAH Gene

[0128] In order to examine the effect of iron on the activity of PAH and therefore production of tyrosine, E. coli strains containing the PAH gene of the C. violaceum (PAH) [SEQ ID NO:1] and the PhhA component of the Pseudomonas PAH operon were grown in the M9 medium with glucose with and without addition of either FeSO4 or Fe(NH4)2(SO4)2 (1.0 M final conc.). Samples were taken at 2.0, 6.0, 16.0, and 22 hours. The results are shown in the Table 13. Based on the results obtained, it was concluded that addition of neither of the two iron sources had any significant positive effect on the level of the tyrosine produced.

TABLE 13Tyrosine Production of Phenylalanine OverproducingStrain (ATCC31884) Transformed with PAHfrom C. violaceum in the Presence and Absence of Fe+2Time (hour)Presence of Fe+2Absence of Fe+20006132.68146.7616173.79171.7722212.99208.58

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

PUM

PropertyMeasurementUnit
Molar densityaaaaaaaaaa
Molar densityaaaaaaaaaa
Molar densityaaaaaaaaaa
Login to view more

Abstract

Genes encoding phenylalanine ammonia-lyase (PAL), tyrosine ammonia lyase (TAL) and phenylalanine hydroxylase (PAH) have been introduced into a host organism for the production of Para-hydroxycinnamic acid (PHCA). The introduction of these genes results in the redirection of carbon flow in the host, optimizing the flow of carbon from glucose to PHCA. The intermediates, tyrosine and cinnamic acid are also produced.

Description

[0001] This application claims the benefit of U.S. Provisional Application No. 60 / 288,701, filed May 4, 2001.FIELD OF THE INVENTION [0002] The invention relates to the field of molecular biology and microbiology. More specifically, the invention relates to the production of tyrosine and para-hydroxycinnamic acid in a recombinant organism by the conversion of phenylalanine to tyrosine via phenylalanine hydroxylase and the subsequent conversion of tyrosine to para-hydroxycinnamic acid via tyrosine ammonium lyase. BACKGROUND OF THE INVENTION [0003] Production of chemicals from microorganisms has been an important application of biotechnology. Typically, the step in developing such a bio-production method may include 1) selection of a proper microorganism host, 2) elimination of metabolic pathways leading to by-products, 3) deregulation of such pathways at both enzyme activity level and the transcriptional level, and 4) overexpression of appropriate enzymes in the desired pathways. The ...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

Application Information

Patent Timeline
no application Login to view more
IPC IPC(8): C12N15/09C12N1/15C12N1/19C12N1/21C12N5/10C12N9/88C12P7/40C12P7/42C12P7/52C12P13/22
CPCC12N9/88C12P13/225C12P7/42C12P7/40
Inventor QI, WEISARIASLANI, FATEMETANG, XIAO-SONG
Owner ORMON CORP
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap