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Title: Isolated spinach ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase and method of inactivating ribulose-1,5-bisphosphatase carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase activity

Abstract

The gene sequence for ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) large subunit (LS) .sup..epsilon. N-methyltransferase (protein methylase III or Rubisco LSMT) from a plant which has a des(methyl) lysyl residue in the LS is disclosed. In addition, the full-length cDNA clones for Rubisco LSMT are disclosed. Transgenic plants and methods of producing same which have the Rubisco LSMT gene inserted into the DNA are also provided. Further, methods of inactivating the enzymatic activity of Rubisco LSMT are also disclosed.

Inventors:
 [1]
  1. (Lexington, KY)
Issue Date:
Research Org.:
University of Kentucky Research Foundation (Lexington, KY)
OSTI Identifier:
872316
Patent Number(s):
5908972
Assignee:
University of Kentucky Research Foundation (Lexington, KY) ORO
DOE Contract Number:  
FG05-92ER26075
Resource Type:
Patent
Country of Publication:
United States
Language:
English
Subject:
isolated; spinach; ribulose-1; 5-bisphosphate; carboxylase; oxygenase; subunit; epsilon; n-methyltransferase; method; inactivating; 5-bisphosphatase; activity; sequence; rubisco; protein; methylase; iii; lsmt; plant; methyl; lysyl; residue; disclosed; addition; full-length; cdna; clones; transgenic; plants; methods; producing; inserted; dna; provided; enzymatic; cdna clones; cdna clone; rubisco lsmt; transgenic plants; protein methylase; methylase iii; full-length cdna; n-methyltransferase activity; enzymatic activity; transgenic plant; spinach ribulose-1; inactivating ribulose-1; isolated spinach; /800/435/999/

Citation Formats

Houtz, Robert L. Isolated spinach ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase and method of inactivating ribulose-1,5-bisphosphatase carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase activity. United States: N. p., 1999. Web.
Houtz, Robert L. Isolated spinach ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase and method of inactivating ribulose-1,5-bisphosphatase carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase activity. United States.
Houtz, Robert L. Fri . "Isolated spinach ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase and method of inactivating ribulose-1,5-bisphosphatase carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase activity". United States. https://www.osti.gov/servlets/purl/872316.
@article{osti_872316,
title = {Isolated spinach ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase and method of inactivating ribulose-1,5-bisphosphatase carboxylase/oxygenase large subunit .sup..epsilon. N-methyltransferase activity},
author = {Houtz, Robert L.},
abstractNote = {The gene sequence for ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) large subunit (LS) .sup..epsilon. N-methyltransferase (protein methylase III or Rubisco LSMT) from a plant which has a des(methyl) lysyl residue in the LS is disclosed. In addition, the full-length cDNA clones for Rubisco LSMT are disclosed. Transgenic plants and methods of producing same which have the Rubisco LSMT gene inserted into the DNA are also provided. Further, methods of inactivating the enzymatic activity of Rubisco LSMT are also disclosed.},
doi = {},
journal = {},
number = ,
volume = ,
place = {United States},
year = {1999},
month = {1}
}

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