CEFOBI   05405
CENTRO DE ESTUDIOS FOTOSINTETICOS Y BIOQUIMICOS
Unidad Ejecutora - UE
capítulos de libros
Título:
Study of the structurefunction relationship in maize
Autor/es:
DETARSIO, E.; ALVAREZ, C.E.; SAIGO, M; DRINCOVICH, M.F.; ANDREO, C.S.
Libro:
Photosynthesis. Energy from the Sun
Editorial:
Allen, Grantt and Osmond, eds. Springer
Referencias:
Año: 2008; p. 841 - 844
Resumen:
Abstract NADP-malic enzyme catalyses the
reversible oxidative decarboxylation of l-malate
to yield carbon dioxide and pyruvate with the
concomitant reduction of NADP. Maize presents
at least three isoforms of this enzyme, and the
photosynthetic isoform is responsible for providing
CO2 to the Calvin Cycle for carbon fixation.
In this work, different aspects of the enzyme were
studied by recombinant protein engineering. The
site directed mutagenesis of the residues A392 and
K435/6 indicated that these residues contribute to
the specificity of NADP over NAD as substrate
of the enzyme. The mutation of the conserved
basic residues K255 and R237 showed that they
are implicated in substrate binding and catalysis,
probably acting as a base. In addition, four
cysteine residues C192, C231, C246 and C270
were shown to affect the catalytic activity when
mutated to alanine.
In this work, different aspects of the enzyme were
studied by recombinant protein engineering. The
site directed mutagenesis of the residues A392 and
K435/6 indicated that these residues contribute to
the specificity of NADP over NAD as substrate
of the enzyme. The mutation of the conserved
basic residues K255 and R237 showed that they
are implicated in substrate binding and catalysis,
probably acting as a base. In addition, four
cysteine residues C192, C231, C246 and C270
were shown to affect the catalytic activity when
mutated to alanine.
to yield carbon dioxide and pyruvate with the
concomitant reduction of NADP. Maize presents
at least three isoforms of this enzyme, and the
photosynthetic isoform is responsible for providing
CO2 to the Calvin Cycle for carbon fixation.
In this work, different aspects of the enzyme were
studied by recombinant protein engineering. The
site directed mutagenesis of the residues A392 and
K435/6 indicated that these residues contribute to
the specificity of NADP over NAD as substrate
of the enzyme. The mutation of the conserved
basic residues K255 and R237 showed that they
are implicated in substrate binding and catalysis,
probably acting as a base. In addition, four
cysteine residues C192, C231, C246 and C270
were shown to affect the catalytic activity when
mutated to alanine.
In this work, different aspects of the enzyme were
studied by recombinant protein engineering. The
site directed mutagenesis of the residues A392 and
K435/6 indicated that these residues contribute to
the specificity of NADP over NAD as substrate
of the enzyme. The mutation of the conserved
basic residues K255 and R237 showed that they
are implicated in substrate binding and catalysis,
probably acting as a base. In addition, four
cysteine residues C192, C231, C246 and C270
were shown to affect the catalytic activity when
mutated to alanine.
reversible oxidative decarboxylation of l-malate
to yield carbon dioxide and pyruvate with the
concomitant reduction of NADP. Maize presents
at least three isoforms of this enzyme, and the
photosynthetic isoform is responsible for providing
CO2 to the Calvin Cycle for carbon fixation.
In this work, different aspects of the enzyme were
studied by recombinant protein engineering. The
site directed mutagenesis of the residues A392 and
K435/6 indicated that these residues contribute to
the specificity of NADP over NAD as substrate
of the enzyme. The mutation of the conserved
basic residues K255 and R237 showed that they
are implicated in substrate binding and catalysis,
probably acting as a base. In addition, four
cysteine residues C192, C231, C246 and C270
were shown to affect the catalytic activity when
mutated to alanine.
In this work, different aspects of the enzyme were
studied by recombinant protein engineering. The
site directed mutagenesis of the residues A392 and
K435/6 indicated that these residues contribute to
the specificity of NADP over NAD as substrate
of the enzyme. The mutation of the conserved
basic residues K255 and R237 showed that they
are implicated in substrate binding and catalysis,
probably acting as a base. In addition, four
cysteine residues C192, C231, C246 and C270
were shown to affect the catalytic activity when
mutated to alanine.
to yield carbon dioxide and pyruvate with the
concomitant reduction of NADP. Maize presents
at least three isoforms of this enzyme, and the
photosynthetic isoform is responsible for providing
CO2 to the Calvin Cycle for carbon fixation.
In this work, different aspects of the enzyme were
studied by recombinant protein engineering. The
site directed mutagenesis of the residues A392 and
K435/6 indicated that these residues contribute to
the specificity of NADP over NAD as substrate
of the enzyme. The mutation of the conserved
basic residues K255 and R237 showed that they
are implicated in substrate binding and catalysis,
probably acting as a base. In addition, four
cysteine residues C192, C231, C246 and C270
were shown to affect the catalytic activity when
mutated to alanine.
In this work, different aspects of the enzyme were
studied by recombinant protein engineering. The
site directed mutagenesis of the residues A392 and
K435/6 indicated that these residues contribute to
the specificity of NADP over NAD as substrate
of the enzyme. The mutation of the conserved
basic residues K255 and R237 showed that they
are implicated in substrate binding and catalysis,
probably acting as a base. In addition, four
cysteine residues C192, C231, C246 and C270
were shown to affect the catalytic activity when
mutated to alanine.
NADP-malic enzyme catalyses the
reversible oxidative decarboxylation of l-malate
to yield carbon dioxide and pyruvate with the
concomitant reduction of NADP. Maize presents
at least three isoforms of this enzyme, and the
photosynthetic isoform is responsible for providing
CO2 to the Calvin Cycle for carbon fixation.
In this work, different aspects of the enzyme were
studied by recombinant protein engineering. The
site directed mutagenesis of the residues A392 and
K435/6 indicated that these residues contribute to
the specificity of NADP over NAD as substrate
of the enzyme. The mutation of the conserved
basic residues K255 and R237 showed that they
are implicated in substrate binding and catalysis,
probably acting as a base. In addition, four
cysteine residues C192, C231, C246 and C270
were shown to affect the catalytic activity when
mutated to alanine.
In this work, different aspects of the enzyme were
studied by recombinant protein engineering. The
site directed mutagenesis of the residues A392 and
K435/6 indicated that these residues contribute to
the specificity of NADP over NAD as substrate
of the enzyme. The mutation of the conserved
basic residues K255 and R237 showed that they
are implicated in substrate binding and catalysis,
probably acting as a base. In addition, four
cysteine residues C192, C231, C246 and C270
were shown to affect the catalytic activity when
mutated to alanine.
to yield carbon dioxide and pyruvate with the
concomitant reduction of NADP. Maize presents
at least three isoforms of this enzyme, and the
photosynthetic isoform is responsible for providing
CO2 to the Calvin Cycle for carbon fixation.
In this work, different aspects of the enzyme were
studied by recombinant protein engineering. The
site directed mutagenesis of the residues A392 and
K435/6 indicated that these residues contribute to
the specificity of NADP over NAD as substrate
of the enzyme. The mutation of the conserved
basic residues K255 and R237 showed that they
are implicated in substrate binding and catalysis,
probably acting as a base. In addition, four
cysteine residues C192, C231, C246 and C270
were shown to affect the catalytic activity when
mutated to alanine.
In this work, different aspects of the enzyme were
studied by recombinant protein engineering. The
site directed mutagenesis of the residues A392 and
K435/6 indicated that these residues contribute to
the specificity of NADP over NAD as substrate
of the enzyme. The mutation of the conserved
basic residues K255 and R237 showed that they
are implicated in substrate binding and catalysis,
probably acting as a base. In addition, four
cysteine residues C192, C231, C246 and C270
were shown to affect the catalytic activity when
mutated to alanine.
l-malate
to yield carbon dioxide and pyruvate with the
concomitant reduction of NADP. Maize presents
at least three isoforms of this enzyme, and the
photosynthetic isoform is responsible for providing
CO2 to the Calvin Cycle for carbon fixation.
In this work, different aspects of the enzyme were
studied by recombinant protein engineering. The
site directed mutagenesis of the residues A392 and
K435/6 indicated that these residues contribute to
the specificity of NADP over NAD as substrate
of the enzyme. The mutation of the conserved
basic residues K255 and R237 showed that they
are implicated in substrate binding and catalysis,
probably acting as a base. In addition, four
cysteine residues C192, C231, C246 and C270
were shown to affect the catalytic activity when
mutated to alanine.
In this work, different aspects of the enzyme were
studied by recombinant protein engineering. The
site directed mutagenesis of the residues A392 and
K435/6 indicated that these residues contribute to
the specificity of NADP over NAD as substrate
of the enzyme. The mutation of the conserved
basic residues K255 and R237 showed that they
are implicated in substrate binding and catalysis,
probably acting as a base. In addition, four
cysteine residues C192, C231, C246 and C270
were shown to affect the catalytic activity when
mutated to alanine.
2 to the Calvin Cycle for carbon fixation.
In this work, different aspects of the enzyme were
studied by recombinant protein engineering. The
site directed mutagenesis of the residues A392 and
K435/6 indicated that these residues contribute to
the specificity of NADP over NAD as substrate
of the enzyme. The mutation of the conserved
basic residues K255 and R237 showed that they
are implicated in substrate binding and catalysis,
probably acting as a base. In addition, four
cysteine residues C192, C231, C246 and C270
were shown to affect the catalytic activity when
mutated to alanine.