Any feedback?
Information on EC 2.7.7.72 - CCA tRNA nucleotidyltransferase and Organism(s) Escherichia coli and UniProt Accession P06961
for references in articles please use BRENDA:EC2.7.7.72Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.7.72 CCA tRNA nucleotidyltransferaseIUBMB Comments
The acylation of all tRNAs with an amino acid occurs at the terminal ribose of a 3' CCA sequence. The CCA sequence is added to the tRNA precursor by stepwise nucleotide addition performed by a single enzyme that is ubiquitous in all living organisms. Although the enzyme has the option of releasing the product after each addition, it prefers to stay bound to the product and proceed with the next addition .
Specify your search results
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(3 overall reactions are displayed. Show all (4)>>)
a tRNA precursor
+
=
a tRNA with a 3' cytidine end
+
a tRNA with a 3' cytidine
+
=
a tRNA with a 3' CC end
+
a tRNA with a 3' CC end
+
=
a tRNA with a 3' CCA end
+
Synonyms
cca-adding enzyme, trnt1, cca enzyme, cca1p, atp(ctp):trna nucleotidyltransferase, trna-nt, class i cca-adding enzyme, ccase, afcca, ctp(atp):trna nucleotidyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
-C-C-A pyrophosphorylase
-
-
-
-
ATP(CTP)-tRNA nucleotidyltransferase
-
-
-
-
ATP:tRNA adenylyltransferase
-
-
-
-
ATP:tRNA nucleotidyltransferase (CTP)
-
-
-
-
CTP(ATP):tRNA nucleotidyltransferase
-
-
-
-
CTP:tRNA cytidylyltransferase
-
-
-
-
ribonucleic cytidylic cytidylic adenylic pyrophosphorylase
-
-
-
-
ribonucleic cytidylyltransferase
-
-
-
-
transfer ribonucleate adenyltransferase
-
-
-
-
transfer ribonucleate adenylyltransferase
-
-
-
-
transfer ribonucleate adenylyltransferase,
-
-
-
-
transfer ribonucleate cytidylyltransferase
-
-
-
-
transfer ribonucleate nucleotidyltransferase
-
-
-
-
transfer ribonucleic acid nucleotidyl transferase
-
-
-
-
transfer ribonucleic adenylyl (cytidylyl) transferase
-
-
-
-
transfer ribonucleic-terminal trinucleotide nucleotidyltransferase
-
-
-
-
transfer RNA adenylyltransferase
-
-
-
-
transfer-RNA nucleotidyltransferase
-
-
-
-
tRNA adenylyl(cytidylyl)transferase
-
-
-
-
tRNA adenylyltransferase
-
-
-
-
tRNA CCA-pyrophosphorylase
-
-
-
-
tRNA cytidylyltransferase
-
-
-
-
tRNA-nucleotidyltransferase
-
-
-
-
additional information
-
the CCA-adding enzymes belong to the nucleotidyltransferase superfamily
SYSTEMATIC NAME
IUBMB Comments
CTP,CTP,ATP:tRNA cytidylyl,cytidylyl,adenylyltransferase
The acylation of all tRNAs with an amino acid occurs at the terminal ribose of a 3' CCA sequence. The CCA sequence is added to the tRNA precursor by stepwise nucleotide addition performed by a single enzyme that is ubiquitous in all living organisms. Although the enzyme has the option of releasing the product after each addition, it prefers to stay bound to the product and proceed with the next addition [5].
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
tRNAAsp with a 3' CC end + ATP
tRNAAsp with a 3' CCA end + diphosphate
-
usage of tRNAAsp of Bacillus subtilis as substrate, and 5'-labeled tRNA-C and 3'-labeled tRNA-CC alkylated by ethylnitrosourea
-
-
?
tRNAAsp with a 3' cytidine + CTP
tRNAAsp with a 3' CC end + diphosphate
-
usage of tRNAAsp of Bacillus subtilis as substrate, and 5'-labeled tRNA-C and 3'-labeled tRNA-CC alkylated by ethylnitrosourea
-
-
?
tRNAX1 + ATP + 2 CTP
tRNAXCCA + 3 diphosphate
-
only one protein is responsible for both AMP and CMP incorporation
-
-
r
yeast tRNAPhe + 2 CTP + ATP
yeast tRNAPhe with 3'-CCA end + 3 diphosphate
-
preparation of substrate lacking the CCA-terminus or ending with a partial CCA-end
-
-
?
a tRNA precursor + 2 CTP + ATP
a tRNA with a 3' CCA end + 3 diphosphate
-
-
-
-
r
a tRNA precursor + 2 CTP + ATP
a tRNA with a 3' CCA end + 3 diphosphate
-
substrate is synthetic DNA templates based on the sequence of Escherichia coli tRNAVal. Overall reaction, class II CCA-adding enzymes also perform the reverse reaction, mechanism, overview. The enzyme catalyzes diphosphorolysis slowly relative to the forward nucleotide addition and that it exhibits weak binding affinity to diphosphate relative to NTP
-
-
r
a tRNA with a 3' CCA end + 3 diphosphate
a tRNA precursor + 2 CTP + ATP
-
-
-
-
r
a tRNA with a 3' CCA end + 3 diphosphate
a tRNA precursor + 2 CTP + ATP
-
substrate is synthetic DNA templates based on the sequence of Escherichia coli tRNAVal. Overall reaction, class II CCA-adding enzymes also perform the reverse reaction, mechanism, overview. The enzyme catalyzes diphosphorolysis slowly relative to the forward nucleotide addition and that it exhibits weak binding affinity to diphosphate relative to NTP
-
-
r
additional information
?
-
the HD domain of the enzyme also exhibits 2',3'-cyclic phosphodiesterase, 2'-nucleotidase, and Ni2+-dependent phosphatase activities, overview
-
-
?
additional information
?
-
-
the HD domain of the enzyme also exhibits 2',3'-cyclic phosphodiesterase, 2'-nucleotidase, and Ni2+-dependent phosphatase activities, overview
-
-
?
additional information
?
-
-
the CCA-adding enzymes can use three different substrates: tRNAs lacking one, i.e. tRNA-CC, two, i.e. tRNA-C, or all three 3'-terminal nucleotides, tRNA. The CCA-adding enzyme recognizes primarily the top half tRNA minihelix
-
-
?
additional information
?
-
-
the tRNA substrate must remain fixed on the enzyme surface during CA addition. Both CTP addition to tRNA-C and ATP addition to tRNA-CC are dramatically inhibited by alkylation of the same tRNA phosphates in the acceptor stem and TPsiC stem-loop
-
-
?
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
-
-
?
additional information
?
-
-
the specific enzyme incorporates only a highly restricted number of nucleotides in a tRNA primer and then stops polymerization at a high efficiency and accuracy. It selects exclusively CTP and ATP for incorporation and discriminates strongly against the other two nucleotide triphosphates. It does not require a nucleic acid template for directing order and nature of nucleotides to be inserted and is highly selective for tRNA-like structures as a polymerization substrate. The enzyme fulfills both functions in maintenance/repair as well as de novo polymerization
-
-
?
additional information
?
-
-
class 2 enzymes select the nucleotides to be incorporated by a true amino acid template that consists of the three highly conserved residues glutamic acid, aspartic acid and arginine (EDxxR). The arginine residue forms hydrogen bonds with ATP (1 bond) and CTP (2 bonds), assisted by aspartate that contributes one hydrogen bond
-
-
?
additional information
?
-
-
only class II CCA enzymes catalyze diphosphorolysis, the reaction can initiate from all three CCA positions and proceed processively until the removal of nucleotide C74. Diphosphorolysis enables class II enzymes to efficiently remove an incorrect A75 nucleotide from the 3' end, at a rate much faster than the rate of A75 incorporation, suggesting the ability to perform a previously unexpected quality control mechanism for CCA synthesis. No activity with non-tRNA substrate U2 snRNA, but EcCCA is active with non-tRNA substrate BMV TLSTyr and removes the terminalA nucleotide without proceeding further. The enzyme shows a robust activity with tRNA-A75, degrading it down to tRNA-A73 (by 50%) while showing a minor activity with tRNA-C76 (less than 5% substrate conversion) and no activity with tRNA-A74. The incorrect A75 is more readily removed than it is synthesized, suggesting a quality control mechanism that can improve the overall accuracy of CCA synthesis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a tRNA precursor + 2 CTP + ATP
a tRNA with a 3' CCA end + 3 diphosphate
-
-
-
-
r
a tRNA with a 3' CCA end + 3 diphosphate
a tRNA precursor + 2 CTP + ATP
-
-
-
-
r
additional information
?
-
the HD domain of the enzyme also exhibits 2',3'-cyclic phosphodiesterase, 2'-nucleotidase, and Ni2+-dependent phosphatase activities, overview
-
-
?
additional information
?
-
-
the HD domain of the enzyme also exhibits 2',3'-cyclic phosphodiesterase, 2'-nucleotidase, and Ni2+-dependent phosphatase activities, overview
-
-
?
additional information
?
-
-
the CCA-adding enzymes can use three different substrates: tRNAs lacking one, i.e. tRNA-CC, two, i.e. tRNA-C, or all three 3'-terminal nucleotides, tRNA. The CCA-adding enzyme recognizes primarily the top half tRNA minihelix
-
-
?
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
-
-
?
additional information
?
-
-
the specific enzyme incorporates only a highly restricted number of nucleotides in a tRNA primer and then stops polymerization at a high efficiency and accuracy. It selects exclusively CTP and ATP for incorporation and discriminates strongly against the other two nucleotide triphosphates. It does not require a nucleic acid template for directing order and nature of nucleotides to be inserted and is highly selective for tRNA-like structures as a polymerization substrate. The enzyme fulfills both functions in maintenance/repair as well as de novo polymerization
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
-
while Mn2+ is incompetent for diphosphorolysis of tRNA-A76, it promotes a more rapid forward synthesis of tRNA-A76 than even the Mg2+ ion
Zn2+
-
it is inert for diphosphorolysis of tRNAA76, but it is active in the forward synthesis of this tRNA
additional information
Mg2+
-
essentially required, two metal ions are coordinated by highly conserved carboxylates and fulfill specific roles in catalyzing the reaction. Metal ion A activates the 3'-hydroxyl group of the primer for a nucleophilic in-line attack on the alpha-phosphate of the incoming NTP, while metal ion B promotes the leaving of the diphosphate group that is released during this reaction
Mg2+
-
essentially required, two metal ions are coordinated by highly conserved carboxylates and fulfill specific roles in catalyzing the reaction. Metal ion A activates the 3'-hydroxyl group of the primer for a nucleophilic in-line attack on the alpha-phosphate of the incoming NTP, while metal ion B promotes the leaving of the diphosphate group that is released during this reaction. The Mg2+ ions are also required for the diposphorolysis reaction, overview. With tRNA-A76 as the substrate in the reverse reacction, only Mg2+ is catalytically competent
additional information
-
the nature of the divalent metal ions can influence the positioning of diphosphate in the active site. tRNAs ending in C75 and C74, in contrast to tRNA A76, are also active with other divalent metal ions tan Mg2+, albeit less efficient due to accumulation of unreacted tRNA substrate. Diphosphorolysis of tRNA-C75 proceeds the farthest with Mg2+, followed by Co2+, and by Mn2+ and Ni2+. Pyrophosphorolysis of tRNA-C74 also proceeds the farthest with Mg2+, but it is followed by Mn2+ and Co2+ and followed by Ni2+. While the preference of divalent metal ions varies among the three reactions, it also differs from that required for the forward A76 addition. While Ca2+ and Pb2+ fail to promote diphosphorolysis of all three tRNA substrates, they also fail to promote forward synthesis of tRNA-A76 for EcCCA
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
inhibition of AMP incorporating activity only, the CMP incorporating activity is much less sensitive
2,2,2-Terpyridyl
-
inhibition of AMP incorporating activity only, the CMP incorporating activity is much less sensitive
2,2-dipyridyl
-
at high concentrations, inhibition of AMP incorporating activity only, the CMP incorporating activity is much less sensitive
bathophenanthroline
-
inhibition of AMP incorporating activity only, the CMP incorporating activity is much less sensitive
ethylnitrosourea
-
both CTP addition to tRNA-C and ATP addition to tRNA-CC are dramatically inhibited by alkylation of the same tRNA phosphates in the acceptor stem and TPsiC stem-loop
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic parameters of diphosphorolysis from A76, C75, and C74, overview
-
0.5
diphosphate
-
pH not specified in the publication, 37°C, diphosphorolysis reaction with substrate tRNA-C75
0.6
diphosphate
-
pH not specified in the publication, 37°C, diphosphorolysis reaction with substrate tRNA-C74
1
diphosphate
-
pH not specified in the publication, 37°C, diphosphorolysis reaction with substrate tRNA-A76
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
diphosphate
-
pH not specified in the publication, 37°C, diphosphorolysis reaction with substrate tRNA-A76
1.9
diphosphate
-
pH not specified in the publication, 37°C, diphosphorolysis reaction with substrate tRNA-C75
3.1
diphosphate
-
pH not specified in the publication, 37°C, diphosphorolysis reaction with substrate tRNA-C74
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
diphosphate
-
pH not specified in the publication, 37°C, diphosphorolysis reaction with substrate tRNA-A76
3.8
diphosphate
-
pH not specified in the publication, 37°C, diphosphorolysis reaction with substrate tRNA-C75
5.2
diphosphate
-
pH not specified in the publication, 37°C, diphosphorolysis reaction with substrate tRNA-C74
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
280
-
purified enzyme, pH not specified in the publication, 37°C, column peak fraction
67.1
-
purified enzyme, pH not specified in the publication, 37°C, pooled column fraction
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
in all mature tRNAs, the 3'-terminal CCA sequence is synthesized or repaired by the template-independent nucleotidyltransferase ATP(CTP):tRNA nucleotidyltransferase. The phosphohydrolase activities of the HD domain of the tRNA nucleotidyltransferase are involved in the repair of the 3'-CCA end of tRNA, modeling, overview
evolution
malfunction
metabolism
-
under exponential growth conditions, a significant fraction of tRNAs with damaged CCA-tails is found and this fraction decreases upon transition into stationary phase. tRNAs bearing guanine as a discriminator base are generally unaffected by CCA-tail damage. The knockout of the repairing CCA-adding enzyme significantly reduces tRNA integrity, and tRNACys integrity is reduced from 82% in wild-type to 40% in the knockout strain. Even slight reduction of CCA integrity in exponential phase tRNA results in reduced protein synthesis
physiological function
additional information
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
evolution
-
diphosphorolysis of class II enzymes establishes a fundamental difference from class I enzymes, and it is achieved only with the tRNA structure and with specific divalent metal ions
evolution
-
with a possible origin of ancient telomerase-like activity, the CCA-adding enzymes obviously emerged twice during evolution, leading to structurally different, but functionally identical enzymes. While the enzyme class 1 is exclusively found in archaea, class 2 tRNA-nucleotidyltransferases are present in eukaryotes and bacteria. In class 2 enzymes, only the head domain carries a beta sheet and forms the nucleotidyltransferase core, while neck, body and tail consist exclusively of alpha helices, giving the enzyme a hook- or seahorse-like overall structure. The chemical mechanism underlying the polymerization appears conserved in all polymerases across the three kingdoms of life
malfunction
-
CCA ends with misincorporated nucleotides are only rarely detected. Only under rather artificial in vitro conditions, e.g. in the presence of Mn2+ ions instead of Mg2+ or deviating NTP concentrations, incorporation of CCC as well as poly(C) tails can be observed
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
physiological function
-
CCA enzymes catalyze stepwise CCA addition to the tRNA 3' end at positions 7476 as an obligatory sequence for tRNA activity in the cell. Only class II CCA enzymes catalyze pyrophosphorolysis, the reaction can initiate from all three CCA positions and proceed processively until the removal of nucleotide C74. Diphosphorolysis enables class II enzymes to efficiently remove an incorrect A75 nucleotide from the 3' end, at a rate much faster than the rate of A75 incorporation, suggesting the ability to perform a previously unexpected quality control mechanism for CCA synthesis
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
physiological function
-
tRNA-nucleotidyltransferases are RNA polymerases responsible for the synthesis of the nucleotide triplet CCA at the 3'-terminus of tRNAs. As this CCA end represents an essential functional element for aminoacylation and translation, the CCA-adding enzymes are of vital importance in all organisms. The enzyme fulfills both functions in maintenance/repair as well as de novo polymerization
additional information
-
in class 2 enzymes, only the head domain carries a beta-sheet and forms the nucleotidyltransferase core, while neck, body and tail consist exclusively of alpha helices, giving the enzyme a hook- or seahorse-like overall structure, structure-function relationship, overview
additional information
-
the CCA enzymes are unusual RNA polymerases, which catalyze CCA addition to positions 74-76 at the tRNA 3' end without using a nucleic acid template, reaction mechanism of CCA addition and reverse phosphorolysis reaction, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme comprises two domains: an N-terminal domain containing the nucleotidyltransferase activity and a C-terminal HD domain
additional information
-
the enzyme comprises two domains: an N-terminal domain containing the nucleotidyltransferase activity and a C-terminal HD domain
additional information
-
in class 2 enzymes, only the head domain carries a beta-sheet and forms the nucleotidyltransferase core, while neck, body and tail consist exclusively of alpha helices, giving the enzyme a hook- or seahorse-like overall structure, structure-function relationship, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
replacement of residues 100-117 in the human enzyme by the corresponding part of the Escherichia coli enzyme, positions 66-87, leading to the chimera HEH with human enzyme N-terminus, Escherichia coli flexible loop, human enzyme C-terminus. Replacement of the region in the Escherichia coli enzyme by either the human loop element, representing the reciprocal experiment, chimera EHE, or by the Bacillus stearothermophilus part, resulting in chimera EBE. Whereas the wild-type enzymes incorporate the complete CCA sequence, the chimeric enzymes EHE, HEH and EBE show a reduced activity and add only 2 C residues to the tRNA substrate. The chimeras EHE, HEH show a 45-to 145fold reduced kcat for A-incorporation. The corresponding KM values are consistent with the KM values of the loop donor enzymes
additional information
-
replacement of the highly conserved residues glutamic acid, aspartic acid and arginine o f the EDxxR motif aabolishes nucleotide specificity of the enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged HD domain from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography
native enzyme 11800fold by ammonium sulfate fractionation, anion exchange and hydroxylapatite chromatography, and tRNA affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of the isolated His-tagged HD domain in Escherichia coli strain BL21 (DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
development of a tRNA sequencing method that is specifically tailored to assess the 3'-termini of Escherichia coli tRNA
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schofield, P.; Williams, K.R.
Purification and some properties of Escherichia coli tRNA nucleotidyltransferase
J. Biol. Chem.
252
5584-5588
1977
Escherichia coli, Escherichia coli B / ATCC 11303
Shi, P.Y.; Maizels, N.; Weiner, A.M.
CCA addition by tRNA nucleotidyltransferase: polymerization without translocation?
EMBO J.
17
3197-3206
1998
Escherichia coli, Saccharolobus shibatae
Yakunin, A.F.; Proudfoot, M.; Kuznetsova, E.; Savchenko, A.; Brown, G.; Arrowsmith, C.H.; Edwards, A.M.
The HD domain of the E. coli tRNA nucleotidyltransferase has 2',3'-cyclic phosphodiesterase, 2'-nucleotidase, and phosphatase activities
J. Biol. Chem.
279
36819-36827
2004
Escherichia coli (P06961), Escherichia coli
Hoffmeier, A.; Betat, H.; Bluschke, A.; Gunther, R.; Junghanns, S.; Hofmann, H.J.; Morl, M.
Unusual evolution of a catalytic core element in CCA-adding enzymes
Nucleic Acids Res.
38
4436-4447
2010
Geobacillus stearothermophilus, Escherichia coli, Homo sapiens (Q96Q11)
Mrl, M.; Betat, H.; Rammelt, C.
TRNA nucleotidyltransferases: ancient catalysts with an unusual mechanism of polymerization
Cell. Mol. Life Sci.
67
1447-1463
2010
Archaeoglobus fulgidus, Escherichia coli, Geobacillus stearothermophilus, Homo sapiens, Saccharolobus shibatae, Thermotoga maritima, Thermus thermophilus
Vrtler, S.; Mrl, M.
tRNA-nucleotidyltransferases: Highly unusual RNA polymerases with vital functions
FEBS Lett.
584
297-302
2010
Aquifex aeolicus, Archaea, Caldanaerobacter subterraneus subsp. tengcongensis, Deinococcus radiodurans, Escherichia coli, Halalkalibacterium halodurans, Homo sapiens, Thermus thermophilus
Igarashi, T.; Liu, C.; Morinaga, H.; Kim, S.; Hou, Y.
Pyrophosphorolysis of CCA addition: implication for fidelity
J. Mol. Biol.
414
28-43
2011
Archaeoglobus fulgidus, Escherichia coli, Homo sapiens
EXTERNAL LINKS (specific for EC-Number 2.7.7.72)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
