Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Mörl, M.; Betat, H.; Rammelt, C.
    TRNA nucleotidyltransferases: ancient catalysts with an unusual mechanism of polymerization (2010), Cell. Mol. Life Sci., 67, 1447-1463.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.7.72 protein Hfq the multifunctional protein Hfq, originally discovered as a host factor for phage Qb, can stimulate the CCA-adding activity, Hfq facilitates the release of the reaction product, after CCA addition has taken place Thermus thermophilus
2.7.7.72 protein Hfq the multifunctional protein Hfq, originally discovered as a host factor for phage Qb, can stimulate the CCA-adding activity, Hfq facilitates the release of the reaction product, after CCA addition has taken place Escherichia coli
2.7.7.72 protein Hfq the multifunctional protein Hfq, originally discovered as a host factor for phage Qb, can stimulate the CCA-adding activity, Hfq facilitates the release of the reaction product, after CCA addition has taken place Homo sapiens
2.7.7.72 protein Hfq the multifunctional protein Hfq, originally discovered as a host factor for phage Qb, can stimulate the CCA-adding activity, Hfq facilitates the release of the reaction product, after CCA addition has taken place Geobacillus stearothermophilus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.72 crystal structure analysis Escherichia coli
2.7.7.72 crystal structure analysis Archaeoglobus fulgidus
2.7.7.72 crystal structure analysis Thermotoga maritima

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.72 Mg2+ two metal ions are bound to the two catalytically important carboxylates. The first metal ion deprotonates the 3'-OH group of the tRNA primer and activates the resulting 3'-O for an attack at the a-phosphate of the incoming nucleotide. The second metal ion stabilizes the triphosphate moiety of the NTP and facilitates the leaving of the pyrophosphate group, overview Archaeoglobus fulgidus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.72 additional information Thermus thermophilus CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview ?
-
 ?
2.7.7.72 additional information Escherichia coli CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview ?
-
 ?
2.7.7.72 additional information Homo sapiens CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview ?
-
 ?
2.7.7.72 additional information Geobacillus stearothermophilus CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview ?
-
 ?
2.7.7.72 additional information Saccharolobus shibatae CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview ?
-
 ?
2.7.7.72 additional information Archaeoglobus fulgidus CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview ?
-
 ?
2.7.7.72 additional information Thermotoga maritima CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.72 Archaeoglobus fulgidus
-
-
-
2.7.7.72 Escherichia coli
-
-
-
2.7.7.72 Geobacillus stearothermophilus
-
-
-
2.7.7.72 Homo sapiens
-
-
-
2.7.7.72 Saccharolobus shibatae
-
-
-
2.7.7.72 Thermotoga maritima
-
-
-
2.7.7.72 Thermus thermophilus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.7.72 a tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate catalytic core and reaction mechanism of class I CCA-adding enzymes, overview Saccharolobus shibatae
a
2.7.7.72 a tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate catalytic core and reaction mechanism of class I CCA-adding enzymes, overview Archaeoglobus fulgidus
a
2.7.7.72 a tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate catalytic core and reaction mechanism of class II CCA-adding enzymes, overview Thermus thermophilus
a
2.7.7.72 a tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate catalytic core and reaction mechanism of class II CCA-adding enzymes, overview Homo sapiens
a
2.7.7.72 a tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate catalytic core and reaction mechanism of class II CCA-adding enzymes, overview Geobacillus stearothermophilus
a
2.7.7.72 a tRNA precursor + 2 CTP + ATP = a tRNA with a 3' CCA end + 3 diphosphate catalytic core and reaction mechanism of class II CCA-adding enzymes, overview Thermotoga maritima
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.72 additional information CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview Thermus thermophilus ?
-
 ?
2.7.7.72 additional information CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview Escherichia coli ?
-
 ?
2.7.7.72 additional information CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview Homo sapiens ?
-
 ?
2.7.7.72 additional information CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview Geobacillus stearothermophilus ?
-
 ?
2.7.7.72 additional information CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview Saccharolobus shibatae ?
-
 ?
2.7.7.72 additional information CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview Archaeoglobus fulgidus ?
-
 ?
2.7.7.72 additional information CCA-adding enzymes recognize tRNA and tRNA-like structures as substrates, select and discriminate the correct nucleotides CTP and ATP against UTP and GTP, and, after incorporation of two C residues, the nucleotide specificity has to switch towards ATP without the help of a nucleic acid template. The enzymes have to stop polymerization exactly after three positions and recognize partial CCA-ends and add only the missing residues for completion, instead of stubbornly adding CCA-ends to their substrates, overview Thermotoga maritima ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.7.72 CCA-adding enzyme
-
 Thermus thermophilus
2.7.7.72 CCA-adding enzyme
-
 Escherichia coli
2.7.7.72 CCA-adding enzyme
-
 Homo sapiens
2.7.7.72 CCA-adding enzyme
-
 Geobacillus stearothermophilus
2.7.7.72 CCA-adding enzyme
-
 Saccharolobus shibatae
2.7.7.72 CCA-adding enzyme
-
 Archaeoglobus fulgidus
2.7.7.72 CCA-adding enzyme
-
 Thermotoga maritima
2.7.7.72 class I CCA-adding enzyme
-
 Saccharolobus shibatae
2.7.7.72 class I CCA-adding enzyme
-
 Archaeoglobus fulgidus
2.7.7.72 class II CCA-adding enzyme
-
 Thermus thermophilus
2.7.7.72 class II CCA-adding enzyme
-
 Homo sapiens
2.7.7.72 class II CCA-adding enzyme
-
 Geobacillus stearothermophilus
2.7.7.72 class II CCA-adding enzyme
-
 Thermotoga maritima

General Information

EC Number General Information Comment Organism
2.7.7.72 evolution a class I CCA-adding enzyme. CCA-adding enzymes are essential RNA polymerases that emerged twice in evolution leading to different structural characteristics and unusual mechanistic solutions for an error-free and sequence-specific CCA polymerization reaction. The catalytic cleft is formed by the head, neck, and body domains. Evolution of class I and class II CCA-adding enzymes as well as poly(A) polymerases, overview Saccharolobus shibatae
2.7.7.72 evolution a class I CCA-adding enzyme. CCA-adding enzymes are essential RNA polymerases that emerged twice in evolution leading to different structural characteristics and unusual mechanistic solutions for an error-free and sequence-specific CCA polymerization reaction. The catalytic cleft is formed by the head, neck, and body domains. Evolution of class I and class II CCA-adding enzymes as well as poly(A) polymerases, overview Archaeoglobus fulgidus
2.7.7.72 evolution a class II CCA-adding enzyme. Compared to class I, class II CCA-adding enzymes show a much higher evolutionary conservation of individual catalytic core motifs. Evolution of class I and class II CCA-adding enzymes as well as poly(A) polymerases, overview Thermus thermophilus
2.7.7.72 evolution a class II CCA-adding enzyme. Compared to class I, class II CCA-adding enzymes show a much higher evolutionary conservation of individual catalytic core motifs. Evolution of class I and class II CCA-adding enzymes as well as poly(A) polymerases, overview Homo sapiens
2.7.7.72 evolution a class II CCA-adding enzyme. Compared to class I, class II CCA-adding enzymes show a much higher evolutionary conservation of individual catalytic core motifs. Evolution of class I and class II CCA-adding enzymes as well as poly(A) polymerases, overview Geobacillus stearothermophilus
2.7.7.72 evolution a class II CCA-adding enzyme. Compared to class I, class II CCA-adding enzymes show a much higher evolutionary conservation of individual catalytic core motifs. The templating motif carries the sequence DDxxR, a slight deviation from the usual EDxxR motif. Evolution of class I and class II CCA-adding enzymes as well as poly(A) polymerases, overview Thermotoga maritima
2.7.7.72 evolution CCA-adding enzymes are essential RNA polymerases that emerged twice in evolution leading to different structural characteristics and unusual mechanistic solutions for an error-free and sequence-specific CCA polymerization reaction. Evolution of class I and class II CCA-adding enzymes as well as poly(A) polymerases, overview Escherichia coli
2.7.7.72 malfunction mutations around the active site of the Sulfolobus shibatae enzyme interfere with CCA-addition, but have only a minor affect on tRNA binding Thermus thermophilus
2.7.7.72 malfunction mutations around the active site of the Sulfolobus shibatae enzyme interfere with CCA-addition, but have only a minor affect on tRNA binding Homo sapiens
2.7.7.72 malfunction mutations around the active site of the Sulfolobus shibatae enzyme interfere with CCA-addition, but have only a minor affect on tRNA binding Geobacillus stearothermophilus
2.7.7.72 malfunction mutations around the active site of the Sulfolobus shibatae enzyme interfere with CCA-addition, but have only a minor affect on tRNA binding Saccharolobus shibatae
2.7.7.72 malfunction mutations around the active site of the Sulfolobus shibatae enzyme interfere with CCA-addition, but have only a minor affect on tRNA binding Thermotoga maritima
2.7.7.72 malfunction the enzyme knockout phenotype is a dramatic growth impairment, indicating the repair function of the CCA-adding enzyme on defective tRNAs lacking CCA ends due to hydrolytic damage Escherichia coli
2.7.7.72 additional information structure-function relationship, overview Escherichia coli
2.7.7.72 additional information structure-function relationship, overview Saccharolobus shibatae
2.7.7.72 additional information structure-function relationship, overview. The active site is located in the N-terminal part of the enzyme and consists of five elements that are involved in metal ion binding, catalysis, ribose recognition, nucleotide selection, and templating. Motif A is located in the head domain and includes the general signature motif of all nucleotidyltransferases with the two metal-binding carboxylates DxD that are involved in catalysis and binding of the triphosphate moiety of the incoming nucleotides. The head domain carries motif B, where highly conserved residues play a critical role in discriminating between NTPs and dNTPs. The neck domain contains motif D, a single nucleotide-binding pocket that is specific for binding of CTP and ATP. Head and neck domain form a cleft that binds the incoming nucleotide as well as the 3'-end of the tRNA primer. The body and tail domains at the enzyme's C-terminus recognize the top-half region of the tRNA primer. The CCA-enzyme does not move along the tRNA during synthesis but remains at a fixed position Thermus thermophilus
2.7.7.72 additional information structure-function relationship, overview. The active site is located in the N-terminal part of the enzyme and consists of five elements that are involved in metal ion binding, catalysis, ribose recognition, nucleotide selection, and templating. Motif A is located in the head domain and includes the general signature motif of all nucleotidyltransferases with the two metal-binding carboxylates DxD that are involved in catalysis and binding of the triphosphate moiety of the incoming nucleotides. The head domain carries motif B, where highly conserved residues play a critical role in discriminating between NTPs and dNTPs. The neck domain contains motif D, a single nucleotide-binding pocket that is specific for binding of CTP and ATP. Head and neck domain form a cleft that binds the incoming nucleotide as well as the 3'-end of the tRNA primer. The body and tail domains at the enzyme's C-terminus recognize the top-half region of the tRNA primer. The CCA-enzyme does not move along the tRNA during synthesis but remains at a fixed position Homo sapiens
2.7.7.72 additional information structure-function relationship, overview. The active site is located in the N-terminal part of the enzyme and consists of five elements that are involved in metal ion binding, catalysis, ribose recognition, nucleotide selection, and templating. Motif A is located in the head domain and includes the general signature motif of all nucleotidyltransferases with the two metal-binding carboxylates DxD that are involved in catalysis and binding of the triphosphate moiety of the incoming nucleotides. The head domain carries motif B, where highly conserved residues play a critical role in discriminating between NTPs and dNTPs. The neck domain contains motif D, a single nucleotide-binding pocket that is specific for binding of CTP and ATP. Head and neck domain form a cleft that binds the incoming nucleotide as well as the 3'-end of the tRNA primer. The body and tail domains at the enzyme's C-terminus recognize the top-half region of the tRNA primer. The CCA-enzyme does not move along the tRNA during synthesis but remains at a fixed position Geobacillus stearothermophilus
2.7.7.72 additional information structure-function relationship, overview. The active site is located in the N-terminal part of the enzyme and consists of five elements that are involved in metal ion binding, catalysis, ribose recognition, nucleotide selection, and templating. Motif A is located in the head domain and includes the general signature motif of all nucleotidyltransferases with the two metal-binding carboxylates DxD that are involved in catalysis and binding of the triphosphate moiety of the incoming nucleotides. The head domain carries motif B, where highly conserved residues play a critical role in discriminating between NTPs and dNTPs. The neck domain contains motif D, a single nucleotide-binding pocket that is specific for binding of CTP and ATP. Head and neck domain form a cleft that binds the incoming nucleotide as well as the 3'-end of the tRNA primer. The body and tail domains at the enzyme's C-terminus recognize the top-half region of the tRNA primer. The CCA-enzyme does not move along the tRNA during synthesis but remains at a fixed position Thermotoga maritima
2.7.7.72 additional information structure-function relationship, overview. The enzyme binds the tRNA top half in the correct orientation for CCA-addition in a cleft, the tRNA acceptor stem interacts with a highly conserved long alpha-helical element in an almost parallel orientation. In the position of nucleotide addition, the 3'-end is bound to the active site located in the enzyme's head domain, while the T loop of the tRNA contacts the tail domain. The bound tRNA substrate remains fixed at its binding site in the enzyme during the complete nucleotide incorporation process Archaeoglobus fulgidus
2.7.7.72 physiological function CCA-adding enzymes represent vital components of the cell's tRNA maturation and maintenance system. The CCA end, added to the tRNA by the CCA tRNA nucleotidyltransferase, is the site of aminoacylation, and aminoacyl tRNA synthetases fuse the individual amino acids to the ribose moiety of the terminal A residue. Second, the CCA terminus is required for the correct positioning of the aminoacyl-tRNA in the ribosome's A- and P-site in order to guarantee an efficient peptidyl transfer reaction. The CCA-adding enzyme represents an essential activity in the majority of organisms Archaeoglobus fulgidus
2.7.7.72 physiological function CCA-adding enzymes represent vital components of the cell's tRNA maturation and maintenance system. The CCA end, added to the tRNA by the CCA tRNA nucleotidyltransferase, is the site of aminoacylation, and aminoacyl tRNA synthetases fuse the individual amino acids to the ribose moiety of the terminal A residue. Second, the CCA terminus is required for the correct positioning of the aminoacyl-tRNA in the ribosome's A- and P-site in order to guarantee an efficient peptidyl transfer reaction. The CCA-adding enzyme represents an essential activity in the majority of organisms, but in Escherichia coli, on the other hand, where CCA ends are encoded, this enzyme is dispensable, and a corresponding gene knockout is not lethal, but the repair function of the CCA-adding enzyme on defective tRNAs lacking CCA ends due to hydrolytic damage is required Escherichia coli
2.7.7.72 physiological function CCA-adding enzymes represent vital components of the cell's tRNA maturation and maintenance system. The CCA end, added to the tRNA by the CCA tRNA nucleotidyltransferase, is the site of aminoacylation, and aminoacyl tRNA synthetases fuse the individual amino acids to the ribose moiety of the terminal A residue. Secondly, the CCA terminus is required for the correct positioning of the aminoacyl-tRNA in the ribosome's A- and P-site in order to guarantee an efficient peptidyl transfer reaction. The CCA-adding enzyme represents an essential activity in the majority of organisms Thermus thermophilus
2.7.7.72 physiological function CCA-adding enzymes represent vital components of the cell's tRNA maturation and maintenance system. The CCA end, added to the tRNA by the CCA tRNA nucleotidyltransferase, is the site of aminoacylation, and aminoacyl tRNA synthetases fuse the individual amino acids to the ribose moiety of the terminal A residue. Secondly, the CCA terminus is required for the correct positioning of the aminoacyl-tRNA in the ribosome's A- and P-site in order to guarantee an efficient peptidyl transfer reaction. The CCA-adding enzyme represents an essential activity in the majority of organisms Homo sapiens
2.7.7.72 physiological function CCA-adding enzymes represent vital components of the cell's tRNA maturation and maintenance system. The CCA end, added to the tRNA by the CCA tRNA nucleotidyltransferase, is the site of aminoacylation, and aminoacyl tRNA synthetases fuse the individual amino acids to the ribose moiety of the terminal A residue. Secondly, the CCA terminus is required for the correct positioning of the aminoacyl-tRNA in the ribosome's A- and P-site in order to guarantee an efficient peptidyl transfer reaction. The CCA-adding enzyme represents an essential activity in the majority of organisms Geobacillus stearothermophilus
2.7.7.72 physiological function CCA-adding enzymes represent vital components of the cell's tRNA maturation and maintenance system. The CCA end, added to the tRNA by the CCA tRNA nucleotidyltransferase, is the site of aminoacylation, and aminoacyl tRNA synthetases fuse the individual amino acids to the ribose moiety of the terminal A residue. Secondly, the CCA terminus is required for the correct positioning of the aminoacyl-tRNA in the ribosome's A- and P-site in order to guarantee an efficient peptidyl transfer reaction. The CCA-adding enzyme represents an essential activity in the majority of organisms Saccharolobus shibatae
2.7.7.72 physiological function CCA-adding enzymes represent vital components of the cell's tRNA maturation and maintenance system. The CCA end, added to the tRNA by the CCA tRNA nucleotidyltransferase, is the site of aminoacylation, and aminoacyl tRNA synthetases fuse the individual amino acids to the ribose moiety of the terminal A residue. Secondly, the CCA terminus is required for the correct positioning of the aminoacyl-tRNA in the ribosome's A- and P-site in order to guarantee an efficient peptidyl transfer reaction. The CCA-adding enzyme represents an essential activity in the majority of organisms Thermotoga maritima