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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.7.31 - DNA nucleotidylexotransferase and Organism(s) Homo sapiens and UniProt Accession P04053

for references in articles please use BRENDA:EC2.7.7.31
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Catalyses template-independent extension of the 3'- end of a DNA strand by one nucleotide at a time. Cannot initiate a chain de novo. Nucleoside may be ribo- or 2'-deoxyribo-.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P04053
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
terminal deoxynucleotidyl transferase, terminal deoxynucleotidyl transferase (tdt), deoxynucleotidyl transferase, terminal deoxynucleotidyltransferase, terminal deoxynucleotide transferase, terminal deoxyribonucleotidyl transferase, rep75, terminal deoxyribonucleotidyltransferase, dna nucleotidylexotransferase, deoxynucleotidyl terminal transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
addase
-
-
-
-
deoxynucleotidyl terminal transferase
-
-
-
-
deoxyribonucleic acid nucleotidyltransferase
-
-
-
-
deoxyribonucleic nucleotidyltransferase
-
-
-
-
hTdT
-
-
hTdTL1
-
long isoform
hTdTL2
-
long isoform
hTdTS
-
short isoform
nucleotidyltransferase, terminal deoxyribo-
-
-
-
-
terminal addition enzyme
-
-
-
-
terminal deoxynucleotide transferase
-
-
-
-
terminal deoxynucleotidyl transferase
-
-
terminal deoxynucleotidyltransferase
terminal deoxyribonucleotidyl transferase
-
-
terminal deoxyribonucleotidyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn = diphosphate + DNAn+1
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
polymerization
-
of deoxyribonucleoside triphosphate
SYSTEMATIC NAME
IUBMB Comments
nucleoside-triphosphate:DNA deoxynucleotidylexotransferase
Catalyses template-independent extension of the 3'- end of a DNA strand by one nucleotide at a time. Cannot initiate a chain de novo. Nucleoside may be ribo- or 2'-deoxyribo-.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-67-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
a 2'-deoxyribonucleoside 5'-triphosphate + single stranded DNAn
diphosphate + single stranded DNAn+1
show the reaction diagram
-
the enzyme catalyzes the elongation of a DNA with the length of three or more nucleotides by the isothermal and repetitive addition of deoxyribonucleotides to the 3'-OH terminus of DNA molecules
-
-
?
alpha-[2-N-(9-fluorenylmethoxycarbonyl)aminoethylphosphonyl]-beta,gamma-difluoromethylenediphosphonate + DNAn
diphosphate + ?
show the reaction diagram
-
synthetic substrate
-
-
?
alpha-[2-N-(9-fluorenylmethoxycarbonyl)aminoethylphosphonyl]-beta,gamma-diphosphate + DNAn
diphosphate + ?
show the reaction diagram
-
synthetic substrate
-
-
?
dATP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
dATP + poly(dA)50
diphosphate + poly(dA)51
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNA
diphosphate + DNAn+1
show the reaction diagram
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
dGTP + DNA
diphosphate + DNA
show the reaction diagram
-
-
-
-
?
dNTP + homopolymer primers
?
show the reaction diagram
-
-
-
-
?
dNTP + oligonucleotide primers
?
show the reaction diagram
-
-
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
alternative splicing seems to regulate TdT isoform expression. Both long isoforms, hTdTL1 and hTdTL2 have 3'-5' exonuclease activity. Overexpression of the short isoform hTdTS or the long isoform hTdTL2 greatly reduces the efficiency of recombinantion, which is reverted to normal levels by simultaneous expression of both enzymes
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
a 2'-deoxyribonucleoside 5'-triphosphate + single stranded DNAn
diphosphate + single stranded DNAn+1
show the reaction diagram
-
the enzyme catalyzes the elongation of a DNA with the length of three or more nucleotides by the isothermal and repetitive addition of deoxyribonucleotides to the 3'-OH terminus of DNA molecules
-
-
?
deoxynucleoside triphosphate + DNA
diphosphate + DNAn+1
show the reaction diagram
additional information
?
-
-
alternative splicing seems to regulate TdT isoform expression. Both long isoforms, hTdTL1 and hTdTL2 have 3'-5' exonuclease activity. Overexpression of the short isoform hTdTS or the long isoform hTdTL2 greatly reduces the efficiency of recombinantion, which is reverted to normal levels by simultaneous expression of both enzymes
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R,2S)-1-(6-aminopurin-9-yl)-2-(Hydroxymethyl)cyclopentane
-
-
3'-azido-TTP
-
-
Ap5A
-
-
aurintricarboxylic acid
-
-
Baicalin
-
competitive versus the DNA primer and non-competitive versus the dNTP substrate, IC50: 0.0186 mM
cordycepin
-
selectively cytotoxic against TdT+ leukemic cells, particularly in combination with the adenosine deaminase inhibitor deoxycoformycin
D-/L-carbocyclic dideoxynucleoside triphosphates
-
-
-
ddATP
-
-
ddCTP
-
-
ddGTP
-
-
ddTTP
-
-
diphosphate
-
-
genistein
-
competitive versus the DNA primer and non-competitive versus the dNTP substrate, IC50: 0.0287 mM
NH4+
-
-
Oligo(dA)
-
product inhibition
P1,P5-diadenosine 5'-pentaphosphate
-
-
phosphate
-
-
pyran
-
-
Streptolydigin
-
does not significantly inhibit DNA polymerase alpha, beta, and gamma, or RNA polymerase, non-competitive to (dA)12-18 and dGTP
TdT interacting factor 1
-
negatively regulates TdT activity, TdT interacting factor 1 binds to the Pol beta-like region in TdT and blocks TdT access to DNA ends
-
Tris
-
above 50 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
TdT interacting factor 1
-
releases TdT in the presence of dsDNA to exhibit TdT activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000009
alpha-[2-N-(9-fluorenylmethoxycarbonyl)aminoethylphosphonyl]-beta,gamma-difluoromethylenediphosphonate
-
37°C, pH 7.2
0.000033
alpha-[2-N-(9-fluorenylmethoxycarbonyl)aminoethylphosphonyl]-beta,gamma-diphosphate
-
37°C, pH 7.2
0.01
dATP
-
dGTP
0.1
dGTP
-
-
0.00008 - 0.0002
DNA
0.000032 - 0.5
dTTP
1
homopolymer primers
-
-
-
0.001
oligonucleotide primers
-
-
-
0.0003 - 0.0025
poly(dA)50
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0005
(1R,2S)-1-(6-aminopurin-9-yl)-2-(Hydroxymethyl)cyclopentane
-
-
0.01
3'-azido-TTP
-
-
0.00025
Ap5A
-
-
0.00981 - 0.0152
Baicalin
0.0009 - 0.006
cordycepin
-
-
0.005 - 0.01
D-/L-carbocyclic dideoxynucleoside triphosphates
-
-
-
0.0013
ddATP
-
-
0.0028
ddCTP
-
-
0.0013
ddGTP
-
-
0.0175
ddTTP
-
-
0.0231 - 0.0338
genistein
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00053
aurintricarboxylic acid
Homo sapiens
-
at pH 7.2 and 37°C
0.0186
Baicalin
Homo sapiens
-
competitive versus the DNA primer and non-competitive versus the dNTP substrate, IC50: 0.0186 mM
1.27
diphosphate
Homo sapiens
-
at pH 7.2 and 37°C
0.0287
genistein
Homo sapiens
-
competitive versus the DNA primer and non-competitive versus the dNTP substrate, IC50: 0.0287 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
precursor
Manually annotated by BRENDA team
-
exclusively express hTdTS and hTdTl2
Manually annotated by BRENDA team
-
transformed, hTdTL2 expression is restricted to transformed lymphoid cell lines
Manually annotated by BRENDA team
-
precursor
Manually annotated by BRENDA team
-
exclusively express hTdTS and hTdTl2
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the genetic variations generated by the hTdT single-nucleotide polymorphisms will vary the human immune repertoire and thus its responses. In vitro, six natural variants of TdT differ from wild-type TdT in polymerization ability, with four having significantly lower activity. In vivo, the presence of TdT varies both the efficiency of recombination and N-addition, with two variants generating coding joints with significantly fewer N-additions
physiological function
-
in cells overexpressing terminal deoxynucleotidyltransferase, the enzyme suppresses DNA repair that is based on short (one- or two-base) homology regions, to efficiently add deoxynucleotides during VDJ recombination in lymphoid cells
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TDT_HUMAN
509
0
58536
Swiss-Prot
Mitochondrion (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
-
ternary complex of enzyme with TdT interacting factor 2, i.e. TdIF2, and with core histone, reduction of enzyme activity in complex
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
may contain a small amount of carbohydrate
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A445T
natural variant of TdT, decrease in polymerase ability
D280H
natural variant of TdT
L397S
natural variant of TdT, impaired polymerase activity in vitro and impaired N-additions in an in vivo V(D)J assay
R431C
natural variant of TdT, loss of polymerase activity
R460Q
natural variant of TdT
T450S
natural variant of TdT. Mutation leads to a decrease in the amount of product
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
-
the enzyme is inactivated after heating to 75°C for 10 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
transfection of U2OS cell
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
construction of a nonhomologous end-joining assay vector NAV, containing mKate2, Venus and ccdB genes. Cotransfection of NAV with a construct expressing the restriction enzyme I-SceI generates a double-strand break in NAV that excises mKate2 and ccdB. Repair of this double-strand break produces an intact vector that expresses Venus, a green fluorescent protein. Cells bearing the repaired NAV lack the ccdB gene which slows cell proliferation, the cultures are enriched in cells containing repaired double-strand breaks
biotechnology
-
use in production of synthetic homo- and heteropolymers, N-acetylation or N-alkylation of derivatives of dNTPs
medicine
-
little reliability of enzyme as marker of lymphoblastic lymphoma and leukemia
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Deibel, M.R.; Coleman, M.S.; Hutton, J.J.
Purification and characterization of multiple forms of terminal transferase from human leukemic cells
Adv. Exp. Med. Biol.
145
37-60
1982
Homo sapiens
Manually annotated by BRENDA team
Deibel, M.R.; Coleman, M.S.; Acree, K.; Hutton, J.J.
Biochemical and immunological properties of human terminal deoxynucleotidyl transferase purified from blasts of acute lymphoblastic and chronic myelogenous leukemia
J. Clin. Invest.
67
725-734
1981
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Grosse, F.; Manns, A.
Terminal deoxyribonucleotidyl transferase
Methods Mol. Biol.
16
95-105
1993
Homo sapiens
Manually annotated by BRENDA team
Ratliff, R.L.
Terminal deoxyribonucleotidyl transferase
The Enzymes,3rd Ed. (Boyer,P. D. ,ed. )
14
105-118
1981
Bos taurus, Homo sapiens, Mus musculus
-
Manually annotated by BRENDA team
DiCioccio, R.A.; Sahai Srivastava, B.I.S.
Inhibition of deoxyribonucleic acid polymerases from human cells and from simian sarcoma virus by pyran
Biochem. J.
175
519-524
1978
Homo sapiens
Manually annotated by BRENDA team
Coleman, M.S.
Terminal deoxynucleotidyl transferase: characterization of extraction and assay conditions from human and calf tissue
Arch. Biochem. Biophys.
182
525-532
1977
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
DiCioccio, R.A.; Srivastava, B.I.S.
Selective inhibition of terminal deoxynucleotidyl transferase from leukemic cells by streptolydigin
Biochem. Biophys. Res. Commun.
72
1343-1349
1976
Homo sapiens
Manually annotated by BRENDA team
Okamura, S.; Crane, F.; Messner, H.A.; Mak, T.W.
Purification of terminal deoxynucleotidyltransferase by oligonucleotide affinity chromatography
J. Biol. Chem.
253
3765-3767
1978
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Deibel, M.R.; Coleman, M.S.
Biochemical properties of purified human terminal deoxynucleotidyltransferase
J. Biol. Chem.
255
4206-4212
1980
Homo sapiens
Manually annotated by BRENDA team
Deibel, M.R.; Coleman, M.S.
Purification of a high molecular weight human terminal deoxynucleotidyl transferase
J. Biol. Chem.
254
8634-8649
1979
Homo sapiens
Manually annotated by BRENDA team
Fujita, K.; Shimazaki, N.; Ohta, Y.; Kubota, T.; Ibe, S.; Toji, S.; Tamai, K.; Fujisaki, S.; Hayano, T.; Koiwai, O.
Terminal deoxynucleotidyltransferase forms a ternary complex with a novel chromatin remodeling protein with 82 kDa and core histone
Genes Cells
8
559-571
2003
Homo sapiens
Manually annotated by BRENDA team
Arzumanov, A.A.; Victorova, L.S.; Jasko, M.V.
Synthesis of non-nucleoside triphosphate analogues, a new type of substrates for terminal deoxynucleotidyl transferase
Nucleosides Nucleotides Nucleic Acids
19
1787-1793
2000
Homo sapiens
Manually annotated by BRENDA team
Ramadan, K.; Maga, G.; Shevelev, I.V.; Villani, G.; Blanco, L.; Hubscher, U.
Human DNA polymerase lambda possesses terminal deoxyribonucleotidyl transferase activity and can elongate RNA primers: implications for novel functions
J. Mol. Biol.
328
63-72
2003
Homo sapiens
Manually annotated by BRENDA team
Mathewson, R.C.; Kjeldsberg, C.R.; Perkins, S.L.
Detection of terminal deoxynucleotidyl transferase (TdT) in nonhematopoietic small round cell tumors of children
Pediatr. Pathol. Lab. Med.
17
835-844
1997
Homo sapiens
Manually annotated by BRENDA team
Thai, T.H.; Kearney, J.F.
Isoforms of terminal deoxynucleotidyltransferase: Developmental aspects and function
Adv. Immunol.
86
113-136
2005
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Uchiyama, Y.; Tagami, J.; Kamisuki, S.; Kasai, N.; Oshige, M.; Chiku, H.; Ibe, S.; Koiwai, O.; Sugawara, F.; Sakaguchi, K.
Selective inhibitors of terminal deoxyribonucleotidyltransferase (TdT): baicalin and genistin
Biochim. Biophys. Acta
1725
298-304
2005
Homo sapiens
Manually annotated by BRENDA team
Thai, T.H.; Kearney, J.F.
Distinct and opposite activities of human terminal deoxynucleotidyltransferase splice variants
J. Immunol.
173
4009-4019
2004
Homo sapiens
Manually annotated by BRENDA team
Ramadan, K.; Shevelev, I.V.; Maga, G.; Huebscher, U.
De novo DNA synthesis by human DNA polymerase l, DNA polymerase m and terminal deoxyribonucleotidyl transferase
J. Mol. Biol.
339
395-404
2004
Homo sapiens
Manually annotated by BRENDA team
Di Santo, R.; Maga, G.
Human terminal deoxynucleotidyl transferases as novel targets for anticancer chemotherapy
Curr. Med. Chem.
13
2353-2368
2006
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Tian, C.; Luskin, G.K.; Dischert, K.M.; Higginbotham, J.N.; Shepherd, B.E.; Crowe, J.E.
Evidence for preferential Ig gene usage and differential TdT and exonuclease activities in human naive and memory B cells
Mol. Immunol.
44
2173-2183
2007
Homo sapiens
Manually annotated by BRENDA team
Kubota, T.; Maezawa, S.; Koiwai, K.; Hayano, T.; Koiwai, O.
Identification of functional domains in TdIF1 and its inhibitory mechanism for TdT activity
Genes Cells
12
941-959
2007
Homo sapiens
Manually annotated by BRENDA team
Maezawa, S.; Nakano, S.; Kuniya, T.; Koiwai, O.; Koiwai, K.
Double-strand break repair based on short-homology regions is suppressed under terminal deoxynucleotidyltransferase expression, as revealed by a novel vector system for analysing DNA repair by nonhomologous end joining
FEBS open bio
6
16-23
2016
Homo sapiens
Manually annotated by BRENDA team
Troshchynsky, A.; Dzneladze, I.; Chen, L.; Sheng, Y.; Saridakis, V.; Wu, G.E.
Functional analyses of polymorphic variants of human terminal deoxynucleotidyl transferase
Genes Immun.
16
388-398
2015
Homo sapiens (P04053), Homo sapiens
Manually annotated by BRENDA team
Zhou, F.; Cui, X.; Shang, A.; Lian, J.; Yang, L.; Jin, Y.; Li, B.
Fluorometric determination of the activity and inhibition of terminal deoxynucleotidyl transferase via in-situ formation of copper nanoclusters using enzymatically generated DNA as template
Microchim. Acta
184
773-779
2017
Homo sapiens
Manually annotated by BRENDA team