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ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
additional information
?
-
Substrates: the amino acid, S-2-amino-6-(R-3,4-dihydro-2H-pyrrole-2-carboxamido)-hexanoic acid, named pyrroline-carboxy-lysine (Pcl), is only produced in high amounts in the presence of D-ornithine but, like Pyl, is a substrate for PylS for site-specific incorporation into proteins
Products: -
-
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Methanosarcina spp.
-
Substrates: -
Products: -
?
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ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
additional information
?
-
Substrates: the amino acid, S-2-amino-6-(R-3,4-dihydro-2H-pyrrole-2-carboxamido)-hexanoic acid, named pyrroline-carboxy-lysine (Pcl), is only produced in high amounts in the presence of D-ornithine but, like Pyl, is a substrate for PylS for site-specific incorporation into proteins
Products: -
-
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Substrates: -
Products: -
?
ATP + (3R)-3-methyl-D-ornithine + L-lysine
ADP + phosphate + N6-[(3R)-3-methyl-D-ornithinyl]-L-lysine
Methanosarcina spp.
-
Substrates: -
Products: -
?
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evolution
PylC has similarity to members of the carbamoyl phosphate synthetase family, including D-Ala, D-Ala ligase, and amide formation is in keeping with this phylogeny
evolution
PylC has similarity to members of the carbamoyl phosphate synthetase family, including D-Ala, D-Ala ligase, and amide formation is in keeping with this phylogeny
evolution
PylC has similarity to members of the carbamoyl phosphate synthetase family, including D-Ala, D-Ala ligase, and amide formation is in keeping with this phylogeny
evolution
Methanosarcina spp.
-
PylC has similarity to members of the carbamoyl phosphate synthetase family, including D-Ala, D-Ala ligase, and amide formation is in keeping with this phylogeny
evolution
PylC is a member of the carbamoyl phosphate synthetase family of proteins forming amides between carbon dioxide (or carboxyl groups), and ammonia (or amines)
evolution
the overall structure of PylC reveals similarities to the superfamily of ATP-grasp enzymes, but there exist unique structural and functional features for a topological control of successive substrate entry and product release. PylC harbors two adenine nucleotides bound at the active site, what has not been observed in any ATP-grasp protein analyzed to date
evolution
-
PylC is a member of the carbamoyl phosphate synthetase family of proteins forming amides between carbon dioxide (or carboxyl groups), and ammonia (or amines)
-
evolution
-
the overall structure of PylC reveals similarities to the superfamily of ATP-grasp enzymes, but there exist unique structural and functional features for a topological control of successive substrate entry and product release. PylC harbors two adenine nucleotides bound at the active site, what has not been observed in any ATP-grasp protein analyzed to date
-
evolution
-
PylC has similarity to members of the carbamoyl phosphate synthetase family, including D-Ala, D-Ala ligase, and amide formation is in keeping with this phylogeny
-
evolution
-
PylC has similarity to members of the carbamoyl phosphate synthetase family, including D-Ala, D-Ala ligase, and amide formation is in keeping with this phylogeny
-
evolution
-
PylC is a member of the carbamoyl phosphate synthetase family of proteins forming amides between carbon dioxide (or carboxyl groups), and ammonia (or amines)
-
evolution
-
PylC is a member of the carbamoyl phosphate synthetase family of proteins forming amides between carbon dioxide (or carboxyl groups), and ammonia (or amines)
-
evolution
-
PylC has similarity to members of the carbamoyl phosphate synthetase family, including D-Ala, D-Ala ligase, and amide formation is in keeping with this phylogeny
-
evolution
-
PylC has similarity to members of the carbamoyl phosphate synthetase family, including D-Ala, D-Ala ligase, and amide formation is in keeping with this phylogeny
-
evolution
-
the overall structure of PylC reveals similarities to the superfamily of ATP-grasp enzymes, but there exist unique structural and functional features for a topological control of successive substrate entry and product release. PylC harbors two adenine nucleotides bound at the active site, what has not been observed in any ATP-grasp protein analyzed to date
-
evolution
-
PylC has similarity to members of the carbamoyl phosphate synthetase family, including D-Ala, D-Ala ligase, and amide formation is in keeping with this phylogeny
-
evolution
-
PylC has similarity to members of the carbamoyl phosphate synthetase family, including D-Ala, D-Ala ligase, and amide formation is in keeping with this phylogeny
-
metabolism
in the Methanosarcinaceae, and related species such as Methanococcoides burtonii, Methanohalophilus mahii, and Methanohalobium evestigatum, pyrrolysine is synthesized and incorporated into the methylamine methyltransferases, involved in metabolism of trimethylamine, dimethylamine, or monomethylamine, through the combined actions of the products of the pyl genes. The pylT gene encodes tRNAPyl whose CUA anticodon allows for amber codon translation. The pylS gene produces the pyrrolysyl-tRNA synthetase that charges tRNAPyl directly with pyrrolysine. The synthesis of pyrrolysine is carried out by the pylBCD gene products. Metabolism overview
metabolism
in the Methanosarcinaceae, and related species such as Methanococcoides burtonii, Methanohalophilus mahii, and Methanohalobium evestigatum, pyrrolysine is synthesized and incorporated into the methylamine methyltransferases, involved in metabolism of trimethylamine, dimethylamine, or monomethylamine, through the combined actions of the products of the pyl genes. The pylT gene encodes tRNAPyl whose CUA anticodon allows for amber codon translation. The pylS gene produces the pyrrolysyl-tRNA synthetase that charges tRNAPyl directly with pyrrolysine. The synthesis of pyrrolysine is carried out by the pylBCD gene products. Metabolism overview
metabolism
in the Methanosarcinaceae, and related species such as Methanococcoides burtonii, Methanohalophilus mahii, and Methanohalobium evestigatum, pyrrolysine is synthesized and incorporated into the methylamine methyltransferases, involved in metabolism of trimethylamine, dimethylamine, or monomethylamine, through the combined actions of the products of the pyl genes. The pylT gene encodes tRNAPyl whose CUA anticodon allows for amber codon translation. The pylS gene produces the pyrrolysyl-tRNA synthetase that charges tRNAPyl directly with pyrrolysine. The synthesis of pyrrolysine is carried out by the pylBCD gene products. Metabolism overview
metabolism
Methanosarcina spp.
-
in the Methanosarcinaceae, and related species such as Methanococcoides burtonii, Methanohalophilus mahii, and Methanohalobium evestigatum, pyrrolysine is synthesized and incorporated into the methylamine methyltransferases, involved in metabolism of trimethylamine, dimethylamine, or monomethylamine, through the combined actions of the products of the pyl genes. The pylT gene encodes tRNAPyl whose CUA anticodon allows for amber codon translation. The pylS gene produces the pyrrolysyl-tRNA synthetase that charges tRNAPyl directly with pyrrolysine. The synthesis of pyrrolysine is carried out by the pylBCD gene products. Metabolism overview
metabolism
proposed pathway for the biosynthesis of amino acids Pyl and S-2-amino-6-(R-3,4-dihydro-2H-pyrrole-2-carboxamido)-hexanoic acid, named pyrroline-carboxy-lysine (Pcl), overview. PylB does not act on Pcl or L-Lys-D-Orn but rather acts upstream of PylC and PylD. For this to occur, PylC and PylD must tolerate methylated intermediates. D-Ornithine coopts pyrrolysine biosynthesis to make and insert pyrroline-carboxy-lysine
metabolism
proposed pathway of pyrrolysine biosynthesis by the products of pylB, pylC, and pylD from two molecules of lysine. Lysine is first used to make (2R, 3R) 3-methylornithine. After ligation to a second molecule of lysine, the terminal amine of the methylornithyl-Nepsilon-lysine intermediate is oxidized to an aldehyde. Spontaneous elimination of water forms pyrrolysine
metabolism
the second step in the biosynthesis of the 22nd genetically encoded amino acid pyrrolysine (Pyl) is catalyzed by enzyme PylC that forms the pseudopeptide L-lysine-Nepsilon-3R-methyl-D-ornithine
metabolism
-
proposed pathway of pyrrolysine biosynthesis by the products of pylB, pylC, and pylD from two molecules of lysine. Lysine is first used to make (2R, 3R) 3-methylornithine. After ligation to a second molecule of lysine, the terminal amine of the methylornithyl-Nepsilon-lysine intermediate is oxidized to an aldehyde. Spontaneous elimination of water forms pyrrolysine
-
metabolism
-
the second step in the biosynthesis of the 22nd genetically encoded amino acid pyrrolysine (Pyl) is catalyzed by enzyme PylC that forms the pseudopeptide L-lysine-Nepsilon-3R-methyl-D-ornithine
-
metabolism
-
in the Methanosarcinaceae, and related species such as Methanococcoides burtonii, Methanohalophilus mahii, and Methanohalobium evestigatum, pyrrolysine is synthesized and incorporated into the methylamine methyltransferases, involved in metabolism of trimethylamine, dimethylamine, or monomethylamine, through the combined actions of the products of the pyl genes. The pylT gene encodes tRNAPyl whose CUA anticodon allows for amber codon translation. The pylS gene produces the pyrrolysyl-tRNA synthetase that charges tRNAPyl directly with pyrrolysine. The synthesis of pyrrolysine is carried out by the pylBCD gene products. Metabolism overview
-
metabolism
-
in the Methanosarcinaceae, and related species such as Methanococcoides burtonii, Methanohalophilus mahii, and Methanohalobium evestigatum, pyrrolysine is synthesized and incorporated into the methylamine methyltransferases, involved in metabolism of trimethylamine, dimethylamine, or monomethylamine, through the combined actions of the products of the pyl genes. The pylT gene encodes tRNAPyl whose CUA anticodon allows for amber codon translation. The pylS gene produces the pyrrolysyl-tRNA synthetase that charges tRNAPyl directly with pyrrolysine. The synthesis of pyrrolysine is carried out by the pylBCD gene products. Metabolism overview
-
metabolism
-
proposed pathway of pyrrolysine biosynthesis by the products of pylB, pylC, and pylD from two molecules of lysine. Lysine is first used to make (2R, 3R) 3-methylornithine. After ligation to a second molecule of lysine, the terminal amine of the methylornithyl-Nepsilon-lysine intermediate is oxidized to an aldehyde. Spontaneous elimination of water forms pyrrolysine
-
metabolism
-
proposed pathway of pyrrolysine biosynthesis by the products of pylB, pylC, and pylD from two molecules of lysine. Lysine is first used to make (2R, 3R) 3-methylornithine. After ligation to a second molecule of lysine, the terminal amine of the methylornithyl-Nepsilon-lysine intermediate is oxidized to an aldehyde. Spontaneous elimination of water forms pyrrolysine
-
metabolism
-
in the Methanosarcinaceae, and related species such as Methanococcoides burtonii, Methanohalophilus mahii, and Methanohalobium evestigatum, pyrrolysine is synthesized and incorporated into the methylamine methyltransferases, involved in metabolism of trimethylamine, dimethylamine, or monomethylamine, through the combined actions of the products of the pyl genes. The pylT gene encodes tRNAPyl whose CUA anticodon allows for amber codon translation. The pylS gene produces the pyrrolysyl-tRNA synthetase that charges tRNAPyl directly with pyrrolysine. The synthesis of pyrrolysine is carried out by the pylBCD gene products. Metabolism overview
-
metabolism
-
in the Methanosarcinaceae, and related species such as Methanococcoides burtonii, Methanohalophilus mahii, and Methanohalobium evestigatum, pyrrolysine is synthesized and incorporated into the methylamine methyltransferases, involved in metabolism of trimethylamine, dimethylamine, or monomethylamine, through the combined actions of the products of the pyl genes. The pylT gene encodes tRNAPyl whose CUA anticodon allows for amber codon translation. The pylS gene produces the pyrrolysyl-tRNA synthetase that charges tRNAPyl directly with pyrrolysine. The synthesis of pyrrolysine is carried out by the pylBCD gene products. Metabolism overview
-
metabolism
-
the second step in the biosynthesis of the 22nd genetically encoded amino acid pyrrolysine (Pyl) is catalyzed by enzyme PylC that forms the pseudopeptide L-lysine-Nepsilon-3R-methyl-D-ornithine
-
metabolism
-
in the Methanosarcinaceae, and related species such as Methanococcoides burtonii, Methanohalophilus mahii, and Methanohalobium evestigatum, pyrrolysine is synthesized and incorporated into the methylamine methyltransferases, involved in metabolism of trimethylamine, dimethylamine, or monomethylamine, through the combined actions of the products of the pyl genes. The pylT gene encodes tRNAPyl whose CUA anticodon allows for amber codon translation. The pylS gene produces the pyrrolysyl-tRNA synthetase that charges tRNAPyl directly with pyrrolysine. The synthesis of pyrrolysine is carried out by the pylBCD gene products. Metabolism overview
-
metabolism
-
in the Methanosarcinaceae, and related species such as Methanococcoides burtonii, Methanohalophilus mahii, and Methanohalobium evestigatum, pyrrolysine is synthesized and incorporated into the methylamine methyltransferases, involved in metabolism of trimethylamine, dimethylamine, or monomethylamine, through the combined actions of the products of the pyl genes. The pylT gene encodes tRNAPyl whose CUA anticodon allows for amber codon translation. The pylS gene produces the pyrrolysyl-tRNA synthetase that charges tRNAPyl directly with pyrrolysine. The synthesis of pyrrolysine is carried out by the pylBCD gene products. Metabolism overview
-
physiological function
enzyme Pylc catalyzes the biosynthesis of pyrrolysine C by formation of the pseudopeptide L-lysine-Nepsilon-3R-methyl-D-ornithine. Pyrrolysine (Pyl) is the 22nd genetically encoded amino acid, and has been discovered as a building block of three proteins (MtmB, MtbB, and MttB) that are all involved in the catabolism of methylamines in the Methanosarcina family of methanogenic archaea and in some eubacteria
physiological function
PylC ligates the epsilonN of lysine to the carboxyl of D-ornithine as a first step in forming desmethylpyrrolysine
physiological function
synthesis of pyrrolysine is carried out by the pylBCD gene products. Formation of desmethylpyrrolysine (dmPyl) requires only PylC and PylD. PylC carries out ligation of D-ornithine to the terminal amine of lysine, as cells transformed with pylC produce D-ornithyl-epsilonN-lysine dependent on exogenous D-ornithine
physiological function
synthesis of pyrrolysine is carried out by the pylBCD gene products. Formation of desmethylpyrrolysine (dmPyl) requires only PylC and PylD. PylC carries out ligation of D-ornithine to the terminal amine of lysine, as cells transformed with pylC produce D-ornithyl-epsilonN-lysine dependent on exogenous D-ornithine
physiological function
synthesis of pyrrolysine is carried out by the pylBCD gene products. Formation of desmethylpyrrolysine (dmPyl) requires only PylC and PylD. PylC carries out ligation of D-ornithine to the terminal amine of lysine, as cells transformed with pylC produce D-ornithyl-epsilonN-lysine dependent on exogenous D-ornithine
physiological function
Methanosarcina spp.
-
synthesis of pyrrolysine is carried out by the pylBCD gene products. Formation of desmethylpyrrolysine (dmPyl) requires only PylC and PylD. PylC carries out ligation of D-ornithine to the terminal amine of lysine, as cells transformed with pylC produce D-ornithyl-epsilonN-lysine dependent on exogenous D-ornithine
physiological function
-
PylC ligates the epsilonN of lysine to the carboxyl of D-ornithine as a first step in forming desmethylpyrrolysine
-
physiological function
-
enzyme Pylc catalyzes the biosynthesis of pyrrolysine C by formation of the pseudopeptide L-lysine-Nepsilon-3R-methyl-D-ornithine. Pyrrolysine (Pyl) is the 22nd genetically encoded amino acid, and has been discovered as a building block of three proteins (MtmB, MtbB, and MttB) that are all involved in the catabolism of methylamines in the Methanosarcina family of methanogenic archaea and in some eubacteria
-
physiological function
-
synthesis of pyrrolysine is carried out by the pylBCD gene products. Formation of desmethylpyrrolysine (dmPyl) requires only PylC and PylD. PylC carries out ligation of D-ornithine to the terminal amine of lysine, as cells transformed with pylC produce D-ornithyl-epsilonN-lysine dependent on exogenous D-ornithine
-
physiological function
-
synthesis of pyrrolysine is carried out by the pylBCD gene products. Formation of desmethylpyrrolysine (dmPyl) requires only PylC and PylD. PylC carries out ligation of D-ornithine to the terminal amine of lysine, as cells transformed with pylC produce D-ornithyl-epsilonN-lysine dependent on exogenous D-ornithine
-
physiological function
-
PylC ligates the epsilonN of lysine to the carboxyl of D-ornithine as a first step in forming desmethylpyrrolysine
-
physiological function
-
PylC ligates the epsilonN of lysine to the carboxyl of D-ornithine as a first step in forming desmethylpyrrolysine
-
physiological function
-
synthesis of pyrrolysine is carried out by the pylBCD gene products. Formation of desmethylpyrrolysine (dmPyl) requires only PylC and PylD. PylC carries out ligation of D-ornithine to the terminal amine of lysine, as cells transformed with pylC produce D-ornithyl-epsilonN-lysine dependent on exogenous D-ornithine
-
physiological function
-
synthesis of pyrrolysine is carried out by the pylBCD gene products. Formation of desmethylpyrrolysine (dmPyl) requires only PylC and PylD. PylC carries out ligation of D-ornithine to the terminal amine of lysine, as cells transformed with pylC produce D-ornithyl-epsilonN-lysine dependent on exogenous D-ornithine
-
physiological function
-
enzyme Pylc catalyzes the biosynthesis of pyrrolysine C by formation of the pseudopeptide L-lysine-Nepsilon-3R-methyl-D-ornithine. Pyrrolysine (Pyl) is the 22nd genetically encoded amino acid, and has been discovered as a building block of three proteins (MtmB, MtbB, and MttB) that are all involved in the catabolism of methylamines in the Methanosarcina family of methanogenic archaea and in some eubacteria
-
physiological function
-
synthesis of pyrrolysine is carried out by the pylBCD gene products. Formation of desmethylpyrrolysine (dmPyl) requires only PylC and PylD. PylC carries out ligation of D-ornithine to the terminal amine of lysine, as cells transformed with pylC produce D-ornithyl-epsilonN-lysine dependent on exogenous D-ornithine
-
physiological function
-
synthesis of pyrrolysine is carried out by the pylBCD gene products. Formation of desmethylpyrrolysine (dmPyl) requires only PylC and PylD. PylC carries out ligation of D-ornithine to the terminal amine of lysine, as cells transformed with pylC produce D-ornithyl-epsilonN-lysine dependent on exogenous D-ornithine
-
additional information
analysis of the incorporation of Pcl and Pyl at TAG codons, tandem mass spectrometry
additional information
the enzyme structure analysis of the active site containing LysNepsilon-D-Orn, two ADP molecules, and phosphate, functional role of the nucleotide bound at the D1 domain, mutational analysis, overview. The active site of PylC appears as a crescent shaped cavity with a length of about 35 A
additional information
-
the enzyme structure analysis of the active site containing LysNepsilon-D-Orn, two ADP molecules, and phosphate, functional role of the nucleotide bound at the D1 domain, mutational analysis, overview. The active site of PylC appears as a crescent shaped cavity with a length of about 35 A
-
additional information
-
the enzyme structure analysis of the active site containing LysNepsilon-D-Orn, two ADP molecules, and phosphate, functional role of the nucleotide bound at the D1 domain, mutational analysis, overview. The active site of PylC appears as a crescent shaped cavity with a length of about 35 A
-
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Gaston, M.; Jiang, R.; Krzycki, J.
Functional context, biosynthesis, and genetic encoding of pyrrolysine
Curr. Opin. Microbiol.
14
342-349
2011
Methanosarcina spp., no activity in Desulfobacterium autotrophicum, Methanohalophilus mahii (D5E9G2), Methanohalobium evestigatum (D7E781), Methanococcoides burtonii (Q12UB8), Methanococcoides burtonii OCM 468 (Q12UB8), Methanococcoides burtonii ACE-M (Q12UB8), Methanococcoides burtonii NBRC 107633 (Q12UB8), Methanohalobium evestigatum DSM 3721 (D7E781), Methanohalophilus mahii ATCC 35705 (D5E9G2), Methanococcoides burtonii DSM 6242 (Q12UB8)
brenda
Quitterer, F.; List, A.; Beck, P.; Bacher, A.; Groll, M.
Biosynthesis of the 22nd genetically encoded amino acid pyrrolysine structure and reaction mechanism of PylC at 1.5 A resolution
J. Mol. Biol.
424
270-282
2012
Methanosarcina barkeri (Q46E79), Methanosarcina barkeri Fusaro (Q46E79), Methanosarcina barkeri DSM 804 (Q46E79)
brenda
Cellitti, S.; Ou, W.; Chiu, H.; Gruenewald, J.; Jones, D.; Hao, X.; Fan, Q.; Quinn, L.; Ng, K.; Anfora, A.; Lesley, S.; Uno, T.; Brock, A.; Geierstanger, B.
D-Ornithine coopts pyrrolysine biosynthesis to make and insert pyrroline-carboxy-lysine
Nat. Chem. Biol.
7
528-530
2011
Methanosarcina mazei (A0A4P8QYJ1)
brenda
Gaston, M.; Zhang, L.; Green-Church, K.; Krzycki, J.
The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine
Nature
471
647-650
2011
Methanosarcina acetivorans (Q8TUC0), Methanosarcina acetivorans ATCC 35395 (Q8TUC0), Methanosarcina acetivorans DSM 2834 (Q8TUC0), Methanosarcina acetivorans JCM 12185 (Q8TUC0)
brenda