Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Preparing heterocyclic carbon compound having only o – n – s,...
Reexamination Certificate
2001-02-22
2004-02-10
Patterson, Jr., Charles L. (Department: 1652)
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Preparing heterocyclic carbon compound having only o, n, s,...
C435S006120, C435S194000, C435S320100, C435S252300, C536S023200, C536S024330
Reexamination Certificate
active
06689587
ABSTRACT:
BACKGROUND OF THE INVENTION
1. Field of the Invention
The present invention relates to polynucleotides corresponding to the nadC gene and which encode the nicotinate nucleotide pyrophosphorylase protein, methods of producing nicotinic acid or nicotinic acid derivatives, and methods of screening for polynucleotides which encode proteins having nicotinate nucleotide pyrophosphorylase protein activity.
2. Discussion of the Background
Nicotinic acid and nicotinic acid derivatives are used in human medicine, in the pharmaceuticals industry, in the foodstuffs industry and in animal nutrition. It is known that L-amino acids are prepared by fermentation from strains of coryneform bacteria, in particular
Corynebacterium glutamicum
. Prior to the present invention there were no processes for the preparation of nicotinic acid or nicotinic acid derivatives using coryneform bacteria.
SUMMARY OF THE INVENTION
The inventors had the object of providing processes for the fermentative preparation of nicotinic acid and nicotinic acid derivatives.
Accordingly, one object of the present invention is an isolated polynucleotide which encodes a protein comprising the amino acid sequence of SEQ ID NO:2.
Another object of the present invention is the nucleotide sequence of SEQ ID NO:1.
Another object of the present invention are isolated polynucleotides which are complimentary to SEQ ID NO:1 or a 70%, 80% or 90% identical to SEQ ID NO:1.
Another object of the present invention are isolated polynucleotides which hybridizes under stringent conditions to SEQ ID NO:1.
Another object of the present invention are polynucleotides which comprises at least 15 consecutive nucleotides of SEQ ID NO:1.
Another object of the present invention are vectors and host cells containing the polynucleotides. In a preferred embodiment the host cells are Corynebacterium and are preferably
Corynebacterium glutamicum.
Another object of the present invention is a Coryneform bacterium which has an enhanced nadC gene.
Another object of the present invention is to a process for producing nicotinic acid or a nicotinic acid derivative culturing a host cell in accordance with the invention in a medium suitable for the expression of the polynucleotide; and collecting the nicotinic acid or nicotinic acid derivative. In a preferred embodiment, the nicotinic acid or nicotinic acid derivative is concentrated after it is collected. In another embodiment, the host cell can also contain an pyc, zwa1 and/or prs whose expression is enhanced; and/or an pck, poxB and zwa2 whose expression is attenuated.
Another object of the present invention is a process for screening for polynucleotides which encode a protein having nicotinate nucleotide pyrophosphorylase protein activity by hybridizing one or more of the polynucleotides embodied in this application to the polynucleotide to be screened; expressing the polynucleotide to produce a protein; and detecting the presence or absence of nicotinate nucleotide pyrophosphorylase protein activity in said protein.
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Tettelin, H., et al. (2000) Acc. No. AE002486.*
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Shin-Ichi Fukuoka, et al., Biochimica et Biophysica Acta, vol. 1395, No. 2, pp. 192-201, XP-002192519, “Characterization and Functional Expression of the cDNA Encoding Human Brain Quinolinate Phosphoribosyltransferase”, Jan. 21, 1998.
R. Bhatia, et al., Archives of Biochemistry and Biophysics, vol 325, No. 2, pp. 270-278, XP-002192520, “The Sequencing, Expression, Purification, and Steady-State Kinetic Analysis of Quinolinate Phosphoribosyl Transferase FromEscherichia coli”, Jan. 15, 1996.
Bastuck Christine
Bathe Brigitte
Dusch Nicole
Moeckel Bettina
Thierbach Georg
Degussa - AG
Oblon & Spivak, McClelland, Maier & Neustadt P.C.
Patterson Jr. Charles L.
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