Triosephosphate isomerase, cytosolic; Belongs to the triosephosphate isomerase family.

Puromycin-sensitive aminopeptidase; Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. Plays an essential role during prophase I of meiosis. Required for correct meiotic reconbination in both male and female gametophytes.

Triosephosphate isomerase, cytosolic; Belongs to the triosephosphate isomerase family.

Triosephosphate isomerase, chloroplastic; Belongs to the triosephosphate isomerase family.

3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial; Catalyzes all the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Able to elongate saturated acyl chains from 4 to at least 16 carbons. Uses malonyl-CoA but not acetyl-CoA as primer substrate. When expressed in a heterologous system, reveals a bimodal distribution of products, with peaks at C8 and C14-C16. The major product of the reaction (octanoyl-ACP) is required for the lipoylation of essential mitochondrial proteins.

3-oxoacyl-[acyl-carrier-protein] synthase I, chloroplastic; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids (By similarity).

3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial; Catalyzes all the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Able to elongate saturated acyl chains from 4 to at least 16 carbons. Uses malonyl-CoA but not acetyl-CoA as primer substrate. When expressed in a heterologous system, reveals a bimodal distribution of products, with peaks at C8 and C14-C16. The major product of the reaction (octanoyl-ACP) is required for the lipoylation of essential mitochondrial proteins.

Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (By similarity). Together with LIP2 is essential for mitochondrial protein lipoylation during seed development. Required for the lipoylation of mitochondrial pyruvate dehydrogenase component E2 proteins in leaves and roots.

3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial; Catalyzes all the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Able to elongate saturated acyl chains from 4 to at least 16 carbons. Uses malonyl-CoA but not acetyl-CoA as primer substrate. When expressed in a heterologous system, reveals a bimodal distribution of products, with peaks at C8 and C14-C16. The major product of the reaction (octanoyl-ACP) is required for the lipoylation of essential mitochondrial proteins.

Octanoyltransferase LIP2, mitochondrial; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity). Together with LIP1 is essential for mitochondrial protein lipoylation during seed development. Required for the lipoylation of mitochondrial 2-oxoglutarate dehydrogenase component E2 proteins in leaves and roots.

3-oxoacyl-[acyl-carrier-protein] synthase I, chloroplastic; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids (By similarity).

3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial; Catalyzes all the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Able to elongate saturated acyl chains from 4 to at least 16 carbons. Uses malonyl-CoA but not acetyl-CoA as primer substrate. When expressed in a heterologous system, reveals a bimodal distribution of products, with peaks at C8 and C14-C16. The major product of the reaction (octanoyl-ACP) is required for the lipoylation of essential mitochondrial proteins.

3-oxoacyl-[acyl-carrier-protein] synthase I, chloroplastic; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids (By similarity).

Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (By similarity). Together with LIP2 is essential for mitochondrial protein lipoylation during seed development. Required for the lipoylation of mitochondrial pyruvate dehydrogenase component E2 proteins in leaves and roots.

3-oxoacyl-[acyl-carrier-protein] synthase I, chloroplastic; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids (By similarity).

Octanoyltransferase LIP2, mitochondrial; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity). Together with LIP1 is essential for mitochondrial protein lipoylation during seed development. Required for the lipoylation of mitochondrial 2-oxoglutarate dehydrogenase component E2 proteins in leaves and roots.

3-oxoacyl-[acyl-carrier-protein] synthase I, chloroplastic; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids (By similarity).

Triosephosphate isomerase, chloroplastic; Belongs to the triosephosphate isomerase family.

Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (By similarity). Together with LIP2 is essential for mitochondrial protein lipoylation during seed development. Required for the lipoylation of mitochondrial pyruvate dehydrogenase component E2 proteins in leaves and roots.

3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial; Catalyzes all the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Able to elongate saturated acyl chains from 4 to at least 16 carbons. Uses malonyl-CoA but not acetyl-CoA as primer substrate. When expressed in a heterologous system, reveals a bimodal distribution of products, with peaks at C8 and C14-C16. The major product of the reaction (octanoyl-ACP) is required for the lipoylation of essential mitochondrial proteins.

Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (By similarity). Together with LIP2 is essential for mitochondrial protein lipoylation during seed development. Required for the lipoylation of mitochondrial pyruvate dehydrogenase component E2 proteins in leaves and roots.

3-oxoacyl-[acyl-carrier-protein] synthase I, chloroplastic; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids (By similarity).

Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (By similarity). Together with LIP2 is essential for mitochondrial protein lipoylation during seed development. Required for the lipoylation of mitochondrial pyruvate dehydrogenase component E2 proteins in leaves and roots.

Octanoyltransferase LIP2, mitochondrial; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity). Together with LIP1 is essential for mitochondrial protein lipoylation during seed development. Required for the lipoylation of mitochondrial 2-oxoglutarate dehydrogenase component E2 proteins in leaves and roots.

Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (By similarity). Together with LIP2 is essential for mitochondrial protein lipoylation during seed development. Required for the lipoylation of mitochondrial pyruvate dehydrogenase component E2 proteins in leaves and roots.

Triosephosphate isomerase, chloroplastic; Belongs to the triosephosphate isomerase family.

Octanoyltransferase LIP2, mitochondrial; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity). Together with LIP1 is essential for mitochondrial protein lipoylation during seed development. Required for the lipoylation of mitochondrial 2-oxoglutarate dehydrogenase component E2 proteins in leaves and roots.

3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial; Catalyzes all the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Able to elongate saturated acyl chains from 4 to at least 16 carbons. Uses malonyl-CoA but not acetyl-CoA as primer substrate. When expressed in a heterologous system, reveals a bimodal distribution of products, with peaks at C8 and C14-C16. The major product of the reaction (octanoyl-ACP) is required for the lipoylation of essential mitochondrial proteins.

Octanoyltransferase LIP2, mitochondrial; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity). Together with LIP1 is essential for mitochondrial protein lipoylation during seed development. Required for the lipoylation of mitochondrial 2-oxoglutarate dehydrogenase component E2 proteins in leaves and roots.

3-oxoacyl-[acyl-carrier-protein] synthase I, chloroplastic; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids (By similarity).

Octanoyltransferase LIP2, mitochondrial; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity). Together with LIP1 is essential for mitochondrial protein lipoylation during seed development. Required for the lipoylation of mitochondrial 2-oxoglutarate dehydrogenase component E2 proteins in leaves and roots.

Lipoyl synthase, mitochondrial; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives (By similarity). Together with LIP2 is essential for mitochondrial protein lipoylation during seed development. Required for the lipoylation of mitochondrial pyruvate dehydrogenase component E2 proteins in leaves and roots.

Puromycin-sensitive aminopeptidase; Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. Plays an essential role during prophase I of meiosis. Required for correct meiotic reconbination in both male and female gametophytes.

Triosephosphate isomerase, cytosolic; Belongs to the triosephosphate isomerase family.

Puromycin-sensitive aminopeptidase; Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. Plays an essential role during prophase I of meiosis. Required for correct meiotic reconbination in both male and female gametophytes.

Triosephosphate isomerase, chloroplastic; Belongs to the triosephosphate isomerase family.

Triosephosphate isomerase, chloroplastic; Belongs to the triosephosphate isomerase family.

Triosephosphate isomerase, cytosolic; Belongs to the triosephosphate isomerase family.

Triosephosphate isomerase, chloroplastic; Belongs to the triosephosphate isomerase family.

3-oxoacyl-[acyl-carrier-protein] synthase I, chloroplastic; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids (By similarity).