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(A)15 + n ATP
(A)15+n + n diphosphate
in the presence of ATP, the incorporation of several nucleotides into the RNA substrate is observed
-
-
?
(A)n + ATP
(A)n+1 + diphosphate
-
-
-
?
(A)n + CTP
(A)n-C + diphosphate
-
-
-
?
(A)n + diphosphate
(A)n-1 + ATP
-
-
-
?
(A)n + GTP
(A)n-G + diphosphate
-
-
-
?
2-aminopurine riboside triphosphate + RNA
?
-
-
-
?
adenosine 5'-O-(1-thiotriphosphate) + RNA
diphosphate + ?
-
SP-diastereomer
-
-
?
ATP + 3' untranslated region of mRNA
diphosphate + ?
-
-
-
?
ATP + adenosine(5')diphospho(5')adenosine
diphosphate + ?
-
i.e. AP2A
-
-
?
ATP + adenosine(5')pentaphospho(5')adenosine
diphosphate + ?
-
i.e. AP5A
-
-
?
ATP + adenosine(5')tetraphospho(5')adenosine
diphosphate + ?
-
i.e. AP4A
-
-
?
ATP + adenosine(5')triphospho(5')adenosine
diphosphate + ?
-
i.e. AP3A
-
-
?
ATP + AMP
diphosphate + ?
-
-
-
-
?
ATP + CMP
diphosphate + ?
-
-
-
-
?
ATP + CTP
diphosphate + ?
-
-
-
-
?
ATP + dGTP
diphosphate + ?
-
-
-
-
?
ATP + GDP
diphosphate + ?
-
-
-
-
?
ATP + GLUT1 mRNA poly(A) tail
?
-
-
-
?
ATP + GTP
diphosphate + ?
-
-
-
-
?
ATP + guanosine
diphosphate + ?
-
-
-
-
?
ATP + guanosine(5')diphospho(5')guanosine
diphosphate + ?
-
i.e. GP2G
-
-
?
ATP + guanosine(5')pentaphospho(5')guanosine
diphosphate + ?
-
i.e. GP5G
-
-
?
ATP + guanosine(5')tetraphospho(5')guanosine
diphosphate + ?
-
i.e. GP4G
-
-
?
ATP + guanosine(5')triphospho(5')guanosine
diphosphate + ?
-
i.e. GP3G
-
-
?
ATP + IMP
diphosphate + ?
-
-
-
-
?
ATP + miR-21-5p
?
enzyme isoform PAPD5 adenylates the 3'-end of miR-21-5p, marking it for 3'-to-5'-trimming by the poly(A) specific ribonuclease PARN
-
-
?
ATP + myosin short poly(A)
?
-
-
-
-
?
ATP + nucleotide
?
-
-
-
-
?
ATP + oligo(A)12
diphosphate + oligo(A)13
ATP + oligo(A)14
diphosphate + oligo(A)15
-
-
-
-
?
ATP + oligo(A)15
diphosphate + oligo(A)16
ATP + oligo(A)17C
diphosphate + oligo(A)18C
-
-
-
-
?
ATP + oligo(A)18
diphosphate + oligo(A)19
ATP + oligo(A)n
diphosphate + oligo(A)n+1
ATP + oligo(U)n
diphosphate + ?
-
-
-
?
ATP + oligoadenylate
?
-
-
-
-
?
ATP + poly(A)n
diphosphate + poly(A)n+1
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
ATP + RNA (A)15
diphosphate + RNA (A)16
-
-
-
-
?
ATP + RNA (A)15
diphosphate + RNA(A)16
ATP + RNA primer
?
-
-
-
-
?
ATP + RNA primer
diphosphate + RNA primer-A
ATP + RNA(A)15
diphosphate + RNA(A)16
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
ATP + rRNA
diphosphate + ?
-
-
-
?
ATP + XTP
diphosphate + ?
-
-
-
-
?
ATP + yeast tRNAiMet
diphosphate + ?
in vitro-synthesized yeast tRNAiMet, but not the native tRNA is substrate
-
-
?
CTP + RNA
diphosphate + ?
-
12% of the activity with ATP, adenylyltransferase A
-
-
?
CTP + RNA primer
diphosphate + RNA primer-C
enzyme can use UTP, CTP and GTP as co-substrates in vitro
enzyme can use UTP, CTP and GTP as co-substrates in vitro
-
?
CTP + RNAn
diphosphate + RNAn+1
dATP + RNA
diphosphate + ?
-
15% of the activity with ATP
-
-
?
GTP + RNA primer
diphosphate + RNA primer-G
-
enzyme can use UTP, CTP and GTP as co-substrates in vitro
-
?
mRNA of isoform gld-1 + ATP
polyadenylated mRNA of isoform gld-1 + diphosphate
-
reaction catalyzed by enzyme isoform GLD-2
-
-
?
UTP + RNA
diphosphate + RNA(U)n
-
recombinant Cid1 shows a preference for UTP over ATP, the poly(U) polymerase activity of recombinant Cid1 out-competes its PAP activity under physiologically relevant conditions
-
-
?
UTP + RNA primer
diphosphate + RNA primer-U
-
enzyme can use UTP, CTP and GTP as co-substrates in vitro
-
?
additional information
?
-
ATP + oligo(A)12
diphosphate + oligo(A)13
-
-
-
-
?
ATP + oligo(A)12
diphosphate + oligo(A)13
-
-
-
?
ATP + oligo(A)15
diphosphate + oligo(A)16
-
-
-
?
ATP + oligo(A)15
diphosphate + oligo(A)16
-
-
-
?
ATP + oligo(A)18
diphosphate + oligo(A)19
-
-
-
?
ATP + oligo(A)18
diphosphate + oligo(A)19
-
-
-
-
?
ATP + oligo(A)n
diphosphate + oligo(A)n+1
-
-
-
-
?
ATP + oligo(A)n
diphosphate + oligo(A)n+1
-
-
-
?
ATP + RNA
?
-
processing and activation of stored mRNAs after resumption of development
-
-
?
ATP + RNA
?
-
overview of biological function
-
-
?
ATP + RNA
?
-
involved in the 3'-end processing of mRNA
-
-
?
ATP + RNA
?
Coturnix sp.
-
overview of biological function
-
-
?
ATP + RNA
?
-
overview of biological function
-
-
?
ATP + RNA
?
-
overview of biological function
-
-
?
ATP + RNA
?
-
overview of biological function
-
-
?
ATP + RNA
?
-
the enzymatic machinery that catalyzes formation of 3'-ends of polyadenylated mRNAs consists of two distinct factors: a poly(A) polymerase and a cleavage/specificity factor required for the correct cleavage at the poly(A) site of pre-mRNA
-
-
?
ATP + RNA
?
-
involved in the 3'-end processing of mRNA
-
-
?
ATP + RNA
?
-
overview of biological function
-
-
?
ATP + RNA
?
-
overview of biological function
-
-
?
ATP + RNA
?
-
synthetic and hydrolytic activities are functions of the same molecule, the level of adenine nucleotides regulates synthesis and degradation of poly(A), the hydrolytic reaction is responsible for poly(A) shortening or turnover, poly(A) itself is a storage form of adenine nucleotides
-
-
?
ATP + RNA
?
-
2 enzymes participate in the polyadenylation of chromosomal RNA, by a coupled mechanism, the chromatin bound enzyme adds 120-130 adenosine nucleotides to chromosomal RNA, the nucleoplasmic enzyme completes the polyadenylation by adding 80-90 more AMP units to the polyadenylated end
-
-
?
ATP + RNA
?
-
overview of biological function
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
length of the poly(A) tail is dependent on incubation time and RNA primer concentration
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
length of the poly(A) tail is dependent on incubation time and RNA primer concentration
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
enzyme also has cleavage activity
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: poly(A)
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: dephosphorylated poly(A), tRNA
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
elongation of the primer is distributive
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: viral RNA MS-2 and QB
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no primer: mixture of tRNA
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: short poly(U)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mg2+-activated enzyme from calf thymus or HeLa cells prefers either longer poly(A) or RNAs rather than shorter oligomers of AMP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mn2+-activated enzymes are indifferent to primer length
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
polyadenylate sequences of 100-200 AMP residues
?
ATP + RNA
diphosphate + RNA(A)n
-
enzyme has no ATPase or poly(A) degrading activity
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: poly(G,U)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides when poly(C) and poly(I), but not poly(U), primes poly(A) synthesis with the Mg2+-activated enzyme
-
?
ATP + RNA
diphosphate + RNA(A)n
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: rRNA 16S, E. coli
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: rRNA 23S, E. coli
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no primer: phage RNA
-
?
ATP + RNA
diphosphate + RNA(A)n
-
poly(A) is the most effective primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
influence of shape and size on priming efficiency
polyadenylate sequences of 100-200 AMP residues
?
ATP + RNA
diphosphate + RNA(A)n
-
Mg2+-activated calf thymus enzyme uses poly(A), tRNA, small RNA fragments from calf thymus RNA well, but HeLa 18 and 28S rRNA and MS-1 RNA poorly if at all
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: poly(A)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: variety of oligoribonucleotides having free 3'-OH
-
?
ATP + RNA
diphosphate + RNA(A)n
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no primer: poly(G)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no primer: poly(C)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
enzyme catalyzes both polyadenylic acid synthesis in absence of a template and DNA-dependent RNA synthesis
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
enzyme catalyzes both polyadenylic acid synthesis in absence of a template and DNA-dependent RNA synthesis
-
?
ATP + RNA
diphosphate + RNA(A)n
Coturnix sp.
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
Coturnix sp.
-
Mn2+-activated enzymes are indifferent to primer length
-
?
ATP + RNA
diphosphate + RNA(A)n
Coturnix sp.
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
Coturnix sp.
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
Coturnix sp.
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
Coturnix sp.
-
adenosine 5'-(beta,gamma-methylene)triphosphate is efficiently polymerized into poly(A) with a polymerase from quail oviduct
-
?
ATP + RNA
diphosphate + RNA(A)n
Coturnix sp.
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mn2+-activated enzymes are indifferent to primer length
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primers: poly(U), poly(C), poly(A), not poly(G)
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mn2+-activated enzymes are indifferent to primer length
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
enzyme uses all four nucleoside triphosphates
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
-
enzyme is unable to catalyze pyrophosphorolysis or phosphorolysis reaction
-
?
ATP + RNA
diphosphate + RNA(A)n
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
highly specific for ATP
-
-
r
ATP + RNA
diphosphate + RNA(A)n
-
Mg2+-activated enzyme from calf thymus or HeLa cells prefers either longer poly(A) or RNAs rather than shorter oligomers of AMP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mn2+-activated enzymes are indifferent to primer length
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
enzyme also has cleavage activity
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
-
human nuclear enzyme and Vaccinia virus enzyme are able to use both RNA and oligo(A) as primer, human cytoplasmic enzyme is able to use RNA but not oligo(A)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mg2+-activated calf thymus enzyme uses poly(A), tRNA, small RNA fragments from calf thymus RNA well, but HeLa 18 and 28S rRNA and MS-1 RNA poorly if at all
-
?
ATP + RNA
diphosphate + RNA(A)n
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Hs2 complexes have very little PAP activity, Hs2 also displays efficient poly(U) polymerase activity
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
polymerase IIa: chain length of the product synthesized is independent of the primer concentration, polymerase IIb: the length of the product decreases when RNA concentration increases
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
polymerase IIa: chain length of the product synthesized is independent of the primer concentration, polymerase IIb: the length of the product decreases when RNA concentration increases
?
ATP + RNA
diphosphate + RNA(A)n
-
polymerase IIa and IIb utilize a variety of natural and synthetic RNAs as well as DNA as primer
polymerase IIa: chain length of the product synthesized is independent of the primer concentration, polymerase IIb: the length of the product decreases when RNA concentration increases
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mn2+-activated enzymes are indifferent to primer length
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: mixture of tRNA
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
poly(A) and poly(C) minimally effective
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no primer: poly(dT)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: oligonucleotides A-A-A-A and A-A-A
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no primer: poly(U)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
average length of poly(A) formed is 600 nucleotides
?
ATP + RNA
diphosphate + RNA(A)n
-
chromatin enzyme uses chromosomal RNA as primer, enzyme from nucleoplasm uses poly(A) and hnRNA isolated from chromatin as primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: mixture of tRNA
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mn2+-activated enzymes are indifferent to primer length
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
AMP is the predominant product of the hydrolysis, ADP and ATP are also formed
r
ATP + RNA
diphosphate + RNA(A)n
-
primer required
average length of poly(A) formed is 600 nucleotides
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
catalyzes the synthesis of polyadenylate linked to the 3'-hydroxyl end of the terminal nucleoside of an RNA primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: tRNA lacking terminal adenosine
-
?
ATP + RNA
diphosphate + RNA(A)n
-
ATP is utilized 2000-fold more than any other nucleoside triphosphate tested
-
?
ATP + RNA
diphosphate + RNA(A)n
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
-
enzyme also catalyzes hydrolysis of poly(A)
AMP is the predominant product of the hydrolysis, ADP and ATP are also formed
r
ATP + RNA
diphosphate + RNA(A)n
-
does not degrade poly(A) associated with poly(A)*poly(U) helical structure
AMP is the predominant product of the hydrolysis, ADP and ATP are also formed
r
ATP + RNA
diphosphate + RNA(A)n
-
poly(A) is the most effective primer
average length of poly(A) formed is 600 nucleotides
?
ATP + RNA
diphosphate + RNA(A)n
-
mitochondrial RNA at least five times more efficiently used than nuclear RNA
average length of poly(A) formed is 600 nucleotides
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: methionyl-tRNA
-
?
ATP + RNA
diphosphate + RNA(A)n
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
no apparent length limitation for the poly(A) tail synthesized
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: various E. coli tRNAs or rRNAs
no apparent length limitation for the poly(A) tail synthesized
?
ATP + RNA
diphosphate + RNA(A)n
-
elongation of the primer is distributive
no apparent length limitation for the poly(A) tail synthesized
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
no apparent length limitation for the poly(A) tail synthesized
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: RNA homopolymers
no apparent length limitation for the poly(A) tail synthesized
?
ATP + RNA
diphosphate + RNA(A)n
PAP catalyzes the synthesis of poly(A) tails on the 3'-end of pre-mRNA
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
Mn2+-activated enzymes are indifferent to primer length
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
no specificity for the 3'-terminal nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
other nucleotides polymerized at less than 1% of the ATP rate
-
?
ATP + RNA
diphosphate + RNA(A)n
-
human nuclear enzyme and Vaccinia virus enzyme are able to use both RNA and oligo(A) as primer, human cytoplasmic enzyme is able to use RNA but not oligo(A)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
minimum effective primer length is 4 to 6 nucleotides
-
?
ATP + RNA
diphosphate + RNA(A)n
-
rather low specificity for primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: dinucleoside phosphates having 3'-OH
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: poly(A)
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
-
-
?
ATP + RNA
diphosphate + RNA(A)n
-
highly specific for ATP
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: mixture of tRNA
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer required
-
?
ATP + RNA
diphosphate + RNA(A)n
-
catalyzes the synthesis of polyadenylate linked to the 3'-hydroxyl end of the terminal nucleoside of an RNA primer
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: tRNA lacking terminal adenosine
-
?
ATP + RNA
diphosphate + RNA(A)n
-
ATP is utilized 2000-fold more than any other nucleoside triphosphate tested
-
?
ATP + RNA
diphosphate + RNA(A)n
-
primer: methionyl-tRNA
-
?
ATP + RNA (A)15
diphosphate + RNA(A)16
-
-
-
?
ATP + RNA (A)15
diphosphate + RNA(A)16
-
-
-
?
ATP + RNA primer
diphosphate + RNA primer-A
in absence of ATP: no activity with 8-Cl-ATP, and 8-amino-ATP results in chain termination, in presence of ATP: polyadenylation of the primer is blocked (inhibited) by 8-amino-ATP and 8-Cl-ATP
-
-
?
ATP + RNA primer
diphosphate + RNA primer-A
isoform GLD-2 shows specificity in vitro for single-stranded RNAs with at least one adenosine at the 3'-end
-
-
?
ATP + RNA primer
diphosphate + RNA primer-A
-
-
-
?
ATP + RNA primer
diphosphate + RNA primer-A
-
isoform PAPD7 displays strong nucleotidyl transferase activity
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
in the assay ATP is added to a final concentration of 0.25 mM
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
adenine can bind in two different configurations in the PAP active site
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
preferentially elongates RNA harbouring poly(A) tails bound by Hfq
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
-
-
-
?
additional information
?
-
in Aquifex aeolicus, 3'-terminal CCA (CCA-3' at positions 7476) of tRNA is synthesized by CC-adding and A-adding enzymes collaboratively. CC addition onto tRNA is catalyzed by poly A polymerase. After C74 addition in an enclosed active pocket and diphosphate release, the tRNA translocates and rotates relative to the enzyme, and C75 addition occurs in the same active pocket as C74 addition. At both the C74-adding and C75-adding stages, CTP is selected by Watson-Crick-like hydrogen bonds between the cytosine of CTP and conserved Asp and Arg residues in the pocket. After C74C75 addition and diosphate release, the tRNA translocates further and drops off the enzyme
-
-
?
additional information
?
-
-
in Aquifex aeolicus, 3'-terminal CCA (CCA-3' at positions 7476) of tRNA is synthesized by CC-adding and A-adding enzymes collaboratively. CC addition onto tRNA is catalyzed by poly A polymerase. After C74 addition in an enclosed active pocket and diphosphate release, the tRNA translocates and rotates relative to the enzyme, and C75 addition occurs in the same active pocket as C74 addition. At both the C74-adding and C75-adding stages, CTP is selected by Watson-Crick-like hydrogen bonds between the cytosine of CTP and conserved Asp and Arg residues in the pocket. After C74C75 addition and diosphate release, the tRNA translocates further and drops off the enzyme
-
-
?
additional information
?
-
-
overview on substrates and primers
-
-
?
additional information
?
-
-
enzyme isoform GLD-2 enhances entry into the meiotic cell cycle at least in part by activating oisoform GLD-1 expression
-
-
?
additional information
?
-
-
dATP is not used efficiently by the PAP protein, neither CTP nor UTP is an effective substrate, GTP is used at 6.3% of the rate of ATP
-
-
?
additional information
?
-
Coturnix sp.
-
overview on substrates and primers
-
-
?
additional information
?
-
-
overview on substrates and primers
-
-
?
additional information
?
-
-
overview on substrates and primers
-
-
?
additional information
?
-
-
rRNA fragments and tRNA precursors originating from the internal spacer regions of the rrn operons, in particular, rrnB are abundant poly(A) polymerase targets. Glu tRNA precursors originating from the rrnB and rrnG transcripts exhibit long 3' trailers that are primarily removed by polyribonucleotide nucleotidyltransferase and to a lesser extent by RNase II and poly(A) polymerase. Glu tRNA precursors still harbouring the 5' leader can be degraded by a 3' to 5' quality control pathway involving poly(A) polymerase
-
-
?
additional information
?
-
-
overview on substrates and primers
-
-
?
additional information
?
-
-
the enzyme is responsible for the synthesis of the poly(A) tail at the 3'-end of eukaryotic mRNA
-
-
?
additional information
?
-
isoform PapD1 can utilize all four nucleotides as substrates, although it is more active with ATP or UTP. the lowest activity is observed with GTP
-
-
?
additional information
?
-
-
isoform PapD1 can utilize all four nucleotides as substrates, although it is more active with ATP or UTP. the lowest activity is observed with GTP
-
-
?
additional information
?
-
isoform PapD5 catalyzes the polyadenylation of different types of RNA substrates in vitro. PAPD5 is active without a protein cofactor. The C terminus of PpaD5 contains a stretch of basic amino acids that is involved in binding the RNA substrate. Incorporation of UTP, GTP, CTP is low and limited to single residues, showing a strong preference of isoform PAPD5 for ATP. No substrates: dNTPs
-
-
?
additional information
?
-
-
isoform PapD5 catalyzes the polyadenylation of different types of RNA substrates in vitro. PAPD5 is active without a protein cofactor. The C terminus of PpaD5 contains a stretch of basic amino acids that is involved in binding the RNA substrate. Incorporation of UTP, GTP, CTP is low and limited to single residues, showing a strong preference of isoform PAPD5 for ATP. No substrates: dNTPs
-
-
?
additional information
?
-
-
overview on substrates and primers
-
-
?
additional information
?
-
-
enzyme may act in the ooplasm on the progression of metaphase I to metaphase II during oocyte maturation
-
-
?
additional information
?
-
-
PAP is a substrate for extracellular signal-regulated kinase
-
-
?
additional information
?
-
-
overview on substrates and primers
-
-
?
additional information
?
-
-
overview on substrates and primers
-
-
?