Information on EC 6.5.1.3 - RNA ligase (ATP):
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EC NUMBERCOMMENTARY
6.5.1.3-

RECOMMENDED NAMEGeneOntology No.
RNA ligase (ATP)GO:0003972

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
ATP + (ribonucleotide)n + (ribonucleotide)m = AMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		----
ATP + (ribonucleotide)n + (ribonucleotide)m = AMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		mechanismTriticum aestivum-1984

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
adenylylationBranchiostoma floridaeC3YGD8-716756
esterification--phosphodiester-

PATHWAYKEGG LinkMetaCyc Link
No entries in this field

SYSTEMATIC NAMEIUBMB Comments
Poly(ribonucleotide):poly(ribonucleotide) ligase (AMP-forming)Converts linear RNA to a circular form by transfer of the 5'-phosphate to the 3'-hydroxy terminus.

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
b1-10tsynthetic construct--653882
bacteriophage RNA ligaseRhodothermus phage RM378--653392
band IV proteinTrypanosoma brucei--650982
class I ligasesynthetic construct--650172, 653882
class I RNA ligase ribozymesynthetic construct--649963
DraRnIDeinococcus radiodurans--662304
DraRnlDeinococcus radiodurans--676230
DRELTrypanosoma brucei--653217
gp24.1Enterobacteria phage T4--653679
P52Trypanosoma brucei--653217
phage Rnl2Vibrio phage KVP40--654015
Polynucleotide synthetase----
Polyribonucleotide ligase----
Polyribonucleotide synthase (ATP)----
REL1Trypanosoma bruceiP86927-694881, 716670
Ribonucleic ligase----
ribonucleprotein editing complexTrypanosoma brucei--653869
RM378 RNA ligaseRhodothermus phage RM378--653392
RNA editing ligase 1Trypanosoma brucei--662636, 716670
RNA ligase----
RNA ligaseEnterobacteria phage T4--707449
RNA ligaseTrypanosoma brucei--708449
RNA ligase (ATP)Vibrio phage KVP40--654015
RNA ligase 1Enterobacteria phage T4--652429, 674568, 677101
RNA ligase 1Phage TS2126--662976
RNA ligase 2Enterobacteria phage T4--662241, 672949
RNA ligase ribozymesynthetic construct--650172, 653368
RNA-editing ligase 1Trypanosoma brucei--694881
RNLBranchiostoma floridaeC3YGD8-716756
Rnl1Enterobacteria phage T4--652429, 677101
Rnl2Enterobacteria phage T4--652387, 653679, 653915, 654015, 662241, 672949
Rnl2Vibrio phage KVP40--654015
RnlARhodothermus phage RM378--653392
Synthetase, polyribonucleotide----
T4 RNA ligaseEnterobacteria phage T4--650653, 651051, 651061, 652246, 653234, 653369, 707449
T4 RNA ligase 2Enterobacteria phage T4--652387, 653679, 653915, 654015, 713745
T4Rnl2Enterobacteria phage T4--713745
TbMP52Trypanosoma brucei--653217
TbMP52Trypanosoma brucei-macromolecular complex with RNA ligase activity653889
TbREL1Trypanosoma brucei--662636
thermostable RNA ligase 1Rhodothermus phage RM378--653392
Trl1Saccharomyces cerevisiae--676215

CAS REGISTRY NUMBERCOMMENTARY
37353-39-2-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Anabaena sp.strain PCC 7120694311--Manually annotated by BRENDA team
Branchiostoma floridae-716756C3YGD8UniProtManually annotated by BRENDA team
Deinococcus radiodurans-662304, 676230--Manually annotated by BRENDA team
Enterobacteria phage L1-677128--Manually annotated by BRENDA team
Enterobacteria phage T4-1910, 1986, 1989, 1992, 1993, 1994, 1995, 1998, 2000, 2001, 650653, 651051, 651061, 652246, 652387, 652429, 653234, 653369, 653679, 654015, 662241, 673669, 674568, 677096, 677101, 694461, 707449, 713745--Manually annotated by BRENDA team
Enterobacteria phage T4-653915, 672949P32277UniprotManually annotated by BRENDA team
Enterobacteria phage T4am N821990--Manually annotated by BRENDA team
Homo sapiens-1985--Manually annotated by BRENDA team
Leishmania tarentolae-1997, 663245--Manually annotated by BRENDA team
Methanothermobacter thermautotrophicus-694452--Manually annotated by BRENDA team
Phage TS2126-662976--Manually annotated by BRENDA team
Rhodothermus phage RM378thermophilic bacteriophage that infects the thermophilic eubacterium Rhodothermus marinus653392--Manually annotated by BRENDA team
Saccharomyces cerevisiae-676215--Manually annotated by BRENDA team
synthetic constructgenerated using chemical synthesis653368--Manually annotated by BRENDA team
synthetic constructisolated from random RNA sequences653882--Manually annotated by BRENDA team
synthetic constructisolated from random sequence650172--Manually annotated by BRENDA team
synthetic constructisolated from random sequences, pool of random sequences based on their ability to join a substrate oligonucleotide to their own 5'-terminus649963--Manually annotated by BRENDA team
Triticum aestivum-1983, 1984, 1987, 1988, 1991, 1999, 714026, 714046--Manually annotated by BRENDA team
Trypanosoma brucei-1996, 651858, 653217, 653869, 653889, 662636, 663245, 708449--Manually annotated by BRENDA team
Trypanosoma brucei-694881, 716670P86927UniProtManually annotated by BRENDA team
Trypanosoma bruceiprocyclic strain 427650982--Manually annotated by BRENDA team
Vibrio phage KVP40-654015--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
physiological functionTrypanosoma brucei-RNA editing ligase 1 is a key component of the trypanosomatid editosome716670
physiological functionBranchiostoma floridaeC3YGD8the combined activities of RNA ligase and polynucleotide kinase/cyclic phosphodiesterase constitute the 5'-phosphate RNA ligation pathway716756

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
(deoxyribonucleotide)ncircular (deoxyribonucleotide)n
show the reaction diagram		Methanothermobacter thermautotrophicus--694452--?
(ribonucleotide)ncircular (ribonucleotide)n
show the reaction diagram		Methanothermobacter thermautotrophicus--694452--?
5'-adenylated cytidine 5',3'-bisphosphate + diguanosine tetraphosphateGp4GpCp + pCpGp4GpCp
show the reaction diagram		Enterobacteria phage T4--651061-651061?
8-Bromoadenosine 5'-triphosphate + (ribonucleotide)n + (ribonucleotide)m8-Bromoadenosine monophosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--2001---
8-Sulfoadenosine 5'-triphosphate + (ribonucleotide)n + (ribonucleotide)m8-Sulfoadenosinemonophosphate + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--2001---
ATP + (2E,6E)-farnesyl diphosphate(2E,6E)-farnesyl-triphospho(5')adenosine + diphosphate
show the reaction diagram		Enterobacteria phage T4-assay contains pyruvate kinase, phosphoenolpyruvate and pyrophosphatase to recover ATP707449--ir
ATP + (2E,6E)-farnesyl triphosphate(2E,6E)-farnesyl-tetraphospho(5')adenosine + diphosphate
show the reaction diagram		Enterobacteria phage T4-assay contains pyruvate kinase, phosphoenolpyruvate and pyrophosphatase to recover ATP707449--ir
ATP + (deoxyribonucleotide)nadenylyl-(deoxyribonucleotide)n + diphosphate
show the reaction diagram		Methanothermobacter thermautotrophicus--694452--?
ATP + (ribonucleotide)nadenylyl-(ribonucleotide)n + diphosphate
show the reaction diagram		Methanothermobacter thermautotrophicus--694452--?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Homo sapiens--1985-1985-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Triticum aestivum--1983-1983-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Triticum aestivum--1999-1999-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei--1996-1996-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--1910-1910-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--1986-1986-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--1989-1989-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--1990-1990-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--1992-1992-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--1998-1998-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--2000-2000-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--2001-2001-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Leishmania tarentolae--1997-1997-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Triticum aestivum-poly(A) containing 5'-P-2,3-cyclic P termini1984-1984-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Triticum aestivum-RNA substrates containing a 5'-phosphate terminus at one end and either a 2',3'-cyclic phosphate or a 2'-phosphate terminus at the other end. In the latter case the reaction is about 30% as active as with the cyclic derivative1987-1987-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Triticum aestivum-participates in an in vitro splicing of yeast transfer RNA precursors containing intervening sequences. Covalently ligates tRNA5' and 3' half-molecules produced by a yeast endonuclease1988-1988-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Triticum aestivum-conversion of linear polyribonucleotides into covalently closed circles, formation of a 2'-phosphomonoester,3',5'-phosphodiester linkage1991-1991-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4-converts linear molecules of polyriboadenylate to circular form by the intramolecular covalent linkage of the 5'-phosphate end to the 3'-hydroxyl terminus1995-1995-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4-formation of a phosphodiester bond between a 5'-PO4-terminated oligonucleotide and a 3'-OH terminated oligonucleotide. Intramolecular formation of single-stranded circles with longer oligonucleotides of the type pAp(Ap)nAOH, where n is about 15 or greater. Intermolecular joining of pAp(Ap)3AOH, where the 5'-PO4-terminated oligonucleotide is short enough to prevent apposition of its 3' and 5' ends, to UpUpUOH1994-1994-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4-cylization of poly(A)1993-1993-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4-the best substrate is [5'-P]polyriboadenylate1995-1995-
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage L1-the L1 ligase is regioselective for formation of the biologically relevant 5' to 3' phosphodiester bond rather than a 5' to 2' bond677128--?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Saccharomyces cerevisiae-Trl1 executes the end-healing and end-sealing steps of tRNA splicing, requires a 2'-PO4 end for tRNA splicing in vivo676215--?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4-Rnl1 has an inherent specificity for sealing tRNA with a break in the anticodon loop. The tRNA specificity is imparted by the C domain677101--?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Triticum aestivum--714026, 714046--?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei--650982-650982?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei--651858-651858?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei--653217-653217?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei--653869-653869?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei--653889-653889?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei--662636, 663245--?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--650653-650653?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--651051-651051?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--651061-651061?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--652387-652387?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--652429-652429?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--653234-653234?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--653369-653369?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--653679-653679?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4P32277-653915-653915?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--654015-654015?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--652246-652246r
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Leishmania tarentolae--663245--?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		synthetic construct--650172-650172?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		synthetic construct--653368-653368?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		synthetic construct--653882-653882?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Rhodothermus phage RM378--653392-653392?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Vibrio phage KVP40--654015-654015?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Branchiostoma floridaeC3YGD8-716756--?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei--716670--?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		synthetic construct-ligates two substrate RNAs, promoting the attack of the 3'-hydroxyl of one substrate upon the 5'-triphosphate of the other substrate with release of diphosphate, reverse of ligation has been detected, but very inefficient, not saturable by soluble amounts of diphosphate649963-649963?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4-only the di-magnesium-coordinated form Mg2ATP0 reacts with the enzyme, forming the covalent complex E-AMP, the reverse reaction, ATP synthesis, occurs between the mono-magnesium-coordinated diphosphate from MgP2O72- and the enzyme-MgAMP complex652246-652246r
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Vibrio phage KVP40-catalyzes RNA end-joining654015-654015?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4-catalyzes the transfer of AMP from the E-AMP complex to diverse compounds, generating the product indicated between parentheses, ATP(Ap4A), NTP (Ap4N), P3 or P4 (p4A or p5A), ADP (Ap3A)651051-651051?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4-participates in repair, splicing and editing pathways, reseals broken RNAs or alters their primary structure, catalyzes intramolecular and intermolecular RNA strand joining through ligase-adenylate and RNA adenylate intermediates653679-653679?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei-RNA editing, essential for proliferation of Trypanosoma brucei653889-653889?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei-RNA editing, posttranscriptional insertion and deletion of uridylate residues in mitochondrial transcripts651858-651858?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei-RNA editing, posttranscriptional process by which uridine residues are added and deleted from mitochondrial mRNAs653869-653869?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei-RNA editing, posttranscriptional RNA processing in which uridylate residues are inserted into and deleted from pre-mRNAs to create start and stop codons, also acts to reseal mRNAs cleaved at incorrect sites650982-650982?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei-RNA editing, unique U insertion and U deletion process, involves cycles of pre-mRNA cleavage, terminal U addition or U removal, and religation, band IV is the RNA editing ligase needed to seal in U deletion653217-653217?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4-RNA-editing652387-652387?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei-the enzyme is essential for survival of both insect and bloodstream forms of the parasite662636--?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Deinococcus radiodurans-DraRnl seals 3'-OH/5'-PO4 RNA nicks in either a duplex RNA or an RNA:DNA hybrid, but it cannot seal 3'-OH/5'-PO4 DNA nicks662304--?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4-neither dATP, GTP, CTP, nor UTP can substitute for ATP. RNA ligation at a 3'-OH/5'-PO4 nick in a double-stranded RNA or an RNA-DNA hybrid662241--?
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Phage TS2126-the TS2126 RNA ligase catalyzes both inter- and intra-molecular single-stranded DNA ligation to more than 50% completion in not more than a few hours at an elevated temperature, although favoring intramolecular ligation on RNA and single-stranded DNA substrates662976--?
ATP + (ribonucleotide)n + (ribonucleotide)m?
show the reaction diagram		Leishmania tarentolae-possibly involved in posttranscriptional RNA editing process of mitochondrial transcripts1997---
ATP + 5'-aaaCCAGUCAMP + diphosphate + ?
show the reaction diagram		synthetic construct-RNA-DNA hybrid as substrate, chemical step is represented as irreversible, because reverse reaction, pyrophosphorolysis with formation of a triphosphate is 10000000-times slower than the forward reaction650172-650172ir
ATP + ATPP1,P4-bis(5'-adenosyl) tetraphosphate + diphosphate
show the reaction diagram		Enterobacteria phage T4--651051-651051?
ATP + ATPP1,P3-bis(5'-adenosyl) triphosphate + ?
show the reaction diagram		Enterobacteria phage T4--651051-651051?
ATP + clodronateadenosine 5'-(beta,gamma-dichloromethylenetriphosphate) + ?
show the reaction diagram		Enterobacteria phage T4--673669--?
ATP + dimethylallyl diphosphatedimethylallyl-triphospho(5')adenosine + diphosphate
show the reaction diagram		Enterobacteria phage T4-assay contains pyruvate kinase, phosphoenolpyruvate and pyrophosphatase to recover ATP707449--ir
ATP + etidronate?
show the reaction diagram		Enterobacteria phage T4-weak activity673669--?
ATP + geranyl diphosphategeranyl-triphospho(5')adenosine + diphosphate
show the reaction diagram		Enterobacteria phage T4-assay contains pyruvate kinase, phosphoenolpyruvate and pyrophosphatase to recover ATP707449--ir
ATP + geranyl triphosphategeranyl-tetraphospho(5')adenosine + diphosphate
show the reaction diagram		Enterobacteria phage T4-assay contains pyruvate kinase, phosphoenolpyruvate and pyrophosphatase to recover ATP707449--ir
ATP + isopentenyl diphosphateisopentenyl-tetraphospho(5')adenosine + diphosphate
show the reaction diagram		Enterobacteria phage T4-assay contains pyruvate kinase, phosphoenolpyruvate and pyrophosphatase to recover ATP707449--ir
ATP + isopentenyl triphosphateisopentenyl-triphospho(5')adenosine + diphosphate
show the reaction diagram		Enterobacteria phage T4-assay contains pyruvate kinase, phosphoenolpyruvate and pyrophosphatase to recover ATP707449--ir
ATP + methylenebisphosphonateadenosine 5'-(beta,gamma-methylenetriphosphate) + ?
show the reaction diagram		Enterobacteria phage T4--673669--?
ATP + RNA + 5'-aaCCAGUCAMP + diphosphate + ?
show the reaction diagram		synthetic construct-DNA-RNA hybrid649963-649963?
ATPgammaS + ATPP1,P4-bis(5'-adenosyl) tetraphosphate + thiodiphosphate
show the reaction diagram		Enterobacteria phage T4--651051-651051?
dATP + (ribonucleotide)n + (ribonucleotide)mdAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Homo sapiens--1985---
dATP + (ribonucleotide)n + (ribonucleotide)mdAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Triticum aestivum--1984---
dATP + (ribonucleotide)n + (ribonucleotide)mdAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Leishmania tarentolae--1997---
dATP + (ribonucleotide)n + (ribonucleotide)mdAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4-at 20% the activity relative to ATP1995---
dATP + (ribonucleotide)n + (ribonucleotide)mdAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4-acts on single-stranded or double-stranded DNA molecules. Acts on very small pieces of ribonucleic acid, with 40mers being the probable upper size limit. The minimum size of the 5'-moiety is a ribonucleoside 3',5'-bisphosphate1910---
GTP + ATPP1-(5'-adenosyl),P4-(5'-guanosyl) tetraphosphate + diphosphate
show the reaction diagram		Enterobacteria phage T4--651051-651051?
ITP + (ribonucleotide)n + (ribonucleotide)mIMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--2001---
additional information?-Enterobacteria phage T4-joins single-stranded DNA molecules much less efficiently. Many of them approximate a well-defined consensus sequence2000---
additional information?-Triticum aestivum-RNA-stimulated exchange reaction between ATP and diphosphate1984---
additional information?-Enterobacteria phage T4-efficient ligation of single-stranded DNAs and RNAs653234-653234?
additional information?-Enterobacteria phage T4-synthesizes circular hammerhead ribozymes from oligonucleotides, small RNA molecules resistant to circuarization by other means can be efficiently circularized on a preparative scale using a suitable DNA template653369-653369?
additional information?-Enterobacteria phage T4-no activity with alendronate nor pamidronate673669---
additional information?-Anabaena sp.-the group I intron from cyanobacterium Anabaena sp. catalyzes phosphodiester bond formation using a triphosphate on the 5'-terminal nucleotide, much like protein polymerases and engineered ribozymes. In the process, this ribozyme forms a unique circular RNA that incorporates the exogenous guanosine cofactor added during self-splicing694311---
additional information?-Methanothermobacter thermautotrophicus-enzyme does not discriminate between RNA and DNA for phosphodiester bond formation, intramolecular ligation of 5'-PO4 single-strand RNA to form a covalently closed circular RNA molecule through ligase-adenylylate and RNA-adenylylate intermediates AppRNA. At the optimal temperature of 65°C, AppRNA is predominantly ligated to a circular product. At 35°C, phosphodiester bond formation is suppressed and the majority of the AppRNA is deadenylylated694452---
additional information?-Enterobacteria phage T4-T4 RNA ligase possesses nick-joining activity in RNA/DNA hybrids against junctional matches/mismatches complementary to the RNA strand as a ligation template. When a junctional mismatch is present at the 30-terminal of RNA probe, the nick-joining activity of T4Rnl2 is inhibited713745---
additional information?-Branchiostoma floridaeC3YGD8the RNA ligase has a a strict requirement for RNA substrates with a 2'-phosphate terminus for the ligation of RNAs with 5'-phosphate and 3'-hydroxyl ends. RNA ligase forms a 2'-phosphomonoester-3',5'-phosphodiester junction716756---
additional information?-Triticum aestivum-wheat RNA ligase can be dissected into three isolated domain enzymes that are responsible for its core ligase, 5'-kinase, and 2',3'-cyclic phosphate 3'-phosphodiesterase activities, respectively. A side reaction on 5'-tri/diphosphate RNAs is dependent on ATP, a 2'-phosphate-3'-hydroxyl end, and the ligase domain. Two RNA molecules having 5'-hydroxyl and 2',3'-cyclic monophosphate groups are ligated almost stoichiometrically after separate conversion of respective terminal phosphate states into reactive ones714046---
additional information?-Triticum aestivum-wheat RNA ligase contains 5'-hydroxyl kinase, 2',3'-cyclic phosphate 3'-phosphodiesterase, and 5'-phosphate 2'-phosphate-3'-hydroxyl RNA ligase activities714026---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage L1-the L1 ligase is regioselective for formation of the biologically relevant 5' to 3' phosphodiester bond rather than a 5' to 2' bond677128--
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + phosphate + (ribonucleotide)n+m
show the reaction diagram		Saccharomyces cerevisiae-Trl1 executes the end-healing and end-sealing steps of tRNA splicing, requires a 2'-PO4 end for tRNA splicing in vivo676215--
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--650653-650653
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--651061-651061
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--652429-652429
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--653234-653234
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--653369-653369
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4P32277-653915-653915
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--654015-654015
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4--652246-652246
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		synthetic construct--650172-650172
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		synthetic construct--653368-653368
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		synthetic construct--653882-653882
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Rhodothermus phage RM378--653392-653392
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Vibrio phage KVP40-catalyzes RNA end-joining654015-654015
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4-catalyzes the transfer of AMP from the E-AMP complex to diverse compounds, generating the product indicated between parentheses, ATP(Ap4A), NTP (Ap4N), P3 or P4 (p4A or p5A), ADP (Ap3A)651051-651051
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4-participates in repair, splicing and editing pathways, reseals broken RNAs or alters their primary structure, catalyzes intramolecular and intermolecular RNA strand joining through ligase-adenylate and RNA adenylate intermediates653679-653679
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei-RNA editing, essential for proliferation of Trypanosoma brucei653889-653889
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei-RNA editing, posttranscriptional insertion and deletion of uridylate residues in mitochondrial transcripts651858-651858
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei-RNA editing, posttranscriptional process by which uridine residues are added and deleted from mitochondrial mRNAs653869-653869
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei-RNA editing, posttranscriptional RNA processing in which uridylate residues are inserted into and deleted from pre-mRNAs to create start and stop codons, also acts to reseal mRNAs cleaved at incorrect sites650982-650982
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei-RNA editing, unique U insertion and U deletion process, involves cycles of pre-mRNA cleavage, terminal U addition or U removal, and religation, band IV is the RNA editing ligase needed to seal in U deletion653217-653217
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Enterobacteria phage T4-RNA-editing652387-652387
ATP + (ribonucleotide)n + (ribonucleotide)mAMP + diphosphate + (ribonucleotide)n+m
show the reaction diagram		Trypanosoma brucei-the enzyme is essential for survival of both insect and bloodstream forms of the parasite662636--
ATP + (ribonucleotide)n + (ribonucleotide)m?
show the reaction diagram		Leishmania tarentolae-possibly involved in posttranscriptional RNA editing process of mitochondrial transcripts1997--
additional information?-Anabaena sp.-the group I intron from cyanobacterium Anabaena sp. catalyzes phosphodiester bond formation using a triphosphate on the 5'-terminal nucleotide, much like protein polymerases and engineered ribozymes. In the process, this ribozyme forms a unique circular RNA that incorporates the exogenous guanosine cofactor added during self-splicing694311--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Mg2+Enterobacteria phage T4-required1910
Mg2+Triticum aestivum-required1983
Mg2+Homo sapiens-divalent cation required1985
Mg2+Triticum aestivum--1987
Mg2+Enterobacteria phage T4-Km: 0.4 mM, inhibition above 10 mM; required1995
Mg2+Leishmania tarentolae--1997
Mg2+synthetic construct-requires metal ions for structure and catalysis650172
Mg2+Enterobacteria phage T4-nucleotidyl transfer Mg2+ dependent652246
Mg2+Rhodothermus phage RM378-optimum activity at 5 mM653392
Mg2+Enterobacteria phage T4-Mg2+ or Mn2+ required662241
Mg2+Trypanosoma brucei-magnesium ion interacts with the beta and gamma-phosphate groups and is almost perfectly octahedrally coordinated by six phosphate and water oxygen atoms662636
Mg2+Phage TS2126-activates, optimum: 5-10 mM662976
Mg2+Enterobacteria phage T4-the active site contains two metal ions, consistent with the two-magnesium ion catalytic mechanism674568
Mg2+Enterobacteria phage L1-L1 ligase is an obligate metalloenzyme that is highly specific for Mg2+. It is selected in the presence of 60 mM MgCl2 and functions optimally in Mg2+ concentrations as high as 100 mM677128
Mn2+synthetic construct-only marginal activity650172
Mn2+Rhodothermus phage RM378-optimum activity at 1 mM653392
Mn2+Enterobacteria phage T4-Mg2+ or Mn2+ required662241
Mn2+Phage TS2126-activates, showing slightly higher activity than Mg2+662976
additional informationsynthetic construct-no detectable activity with Ca2+, Sr2+, Ba2+, Zn2+, Co2+, Cd2+, Pb2+, Co(NH3)6 3+, or spermine650172

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1,N6-Ethenoadenosine 5'-triphosphateEnterobacteria phage T4--2001 2D-image
1-amino-4-(3-(aminosulfonyl)anilino)-9,10-dioxo-9,10-dihydro-2-anthracenesulfonic acidTrypanosoma brucei-68.5% residual activity at 0.01 mM, presence of Triton X-100. Molecular dynamics simulations694881 2D-image
2',5'-ADPEnterobacteria phage T4-poly(A) cyclization1993 2D-image
2-naphthoic acidTrypanosoma brucei--716670 2D-image
2-nitronaphthaleneTrypanosoma brucei--716670-
3-((4-(ethylamino)phenyl)diazenyl)-4,5-dihydroxy-2,7-naphthalenedisulfonic acidTrypanosoma brucei-4.1% residual activity at 0.01 mM, presence of Triton X-100. Molecular dynamics simulations694881 2D-image
3-((5-chloro-2-hydroxyphenyl)diazenyl)-4,5-dihydroxy-2,7-naphthalenedisulfonic acidTrypanosoma brucei-8.6% residual activity at 0.01 mM, presence of Triton X-100. Molecular dynamics simulations694881 2D-image
4,5-dihydroxy-3-(1-naphthyldiazenyl)-2,7-naphthalenedisulfonic acidTrypanosoma brucei-43.1% residual activity at 0.01 mM, presence of Triton X-100. Molecular dynamics simulations694881 2D-image
4,5-dihydroxynaphthalene-2,7-disulfonateTrypanosoma brucei--716670-
4-hydroxy-3-[(E)-(5-hydroxy-7-sulfonaphthalen-2-yl)diazenyl]-7-[(1-phenylethenyl)amino]naphthalene-2-sulfonic acidTrypanosoma brucei--716670 2D-image
6-Chloropurine riboside 5'-triphosphateEnterobacteria phage T4--2001 2D-image
6-hydroxy-5-[(E)-[3-[(E)-(2-hydroxynaphthalen-1-yl)diazenyl]-5-sulfophenyl]diazenyl]naphthalene-2-sulfonic acidTrypanosoma brucei--716670 2D-image
6-mercaptopurine riboside 5'-triphosphateEnterobacteria phage T4--2001 2D-image
7,7'-iminobis(4-hydroxynaphthalene-2-sulfonic acid)Trypanosoma brucei--716670 2D-image
7-amino-4-hydroxy-3-[(E)-(5-hydroxy-7-sulfonaphthalen-2-yl)diazenyl]naphthalene-2-sulfonic acidTrypanosoma brucei--716670 2D-image
8-bromoadenosine 5'-triphosphateEnterobacteria phage T4--2001 2D-image
8-Sulfoadenosine 5'-triphosphateEnterobacteria phage T4--2001 2D-image
adenosine 5'-tetraphosphateEnterobacteria phage T4--1998 2D-image
Adenosine-N'-oxide 5'-triphosphateEnterobacteria phage T4--2001 2D-image
ADPEnterobacteria phage T4--1998 2D-image
AMPEnterobacteria phage T4--1998 2D-image
ATPPhage TS2126-above 2.5 mM, complete inhibition at 10 mM. The inhibition can be partially rescued by adding more Mg2+ to the reaction662976 2D-image
Ba2+synthetic construct--650172 2D-image
beta,gamma-imine-ATPEnterobacteria phage T4--1998 2D-image
beta,gamma-Methylene-ATPEnterobacteria phage T4--1998 2D-image
Ca2+synthetic construct--650172 2D-image
Cd2+synthetic construct--650172 2D-image
Co(NH3)63+synthetic construct--650172 2D-image
Co2+synthetic construct--650172 2D-image
gamma-Thio-ATPEnterobacteria phage T4--1998 2D-image
ITPEnterobacteria phage T4--2001 2D-image
Mg2+Homo sapiens-inhibits above 10 mM, required at lower concentrations1985 2D-image
NaClRhodothermus phage RM378--653392 2D-image
naphthalene-2-sulfonic acidTrypanosoma brucei--716670-
P1,P3-di(adenosine-5')triphosphateEnterobacteria phage T4--1998 2D-image
P1,P4-di(adenosine-5')tetraphosphateEnterobacteria phage T4--1998 2D-image
Pb2+synthetic construct--650172 2D-image
sperminesynthetic construct--650172 2D-image
Sr2+synthetic construct--650172 2D-image
tripolyphosphateEnterobacteria phage T4--651051 2D-image
Zn2+synthetic construct--650172 2D-image
Mn2+synthetic construct--650172 2D-image
additional informationTrypanosoma brucei-inhibitors in infectious microorganisms708449-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
RNATriticum aestivum-stimulates exchange reaction between ATP and diphosphate1984 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.24-(2E,6E)-farnesyl diphosphateEnterobacteria phage T4--707449 2D-image
0.07-(2E,6E)-farnesyl triphosphateEnterobacteria phage T4--707449-
0.009-(ribonucleotide)n+msynthetic construct-pH 8.0, 22°C653882 2D-image
0.4-5'-adenylated cytidine 5',3'-bisphosphateEnterobacteria phage T4-pH 7.4, 30°C651061 2D-image
1e-05-5'-phosphate termini of RNATriticum aestivum--1987-
0.0002-ATPTriticum aestivum--1987 2D-image
0.0002-ATPEnterobacteria phage T4--1995 2D-image
0.007-ATPPhage TS2126-activity with RNA662976 2D-image
0.04-ATPPhage TS2126-activity with DNA662976 2D-image
0.54-clodronateEnterobacteria phage T4--673669 2D-image
4-diguanosine tetraphosphateEnterobacteria phage T4-pH 7.4, 30°C651061 2D-image
0.86-dimethylallyl diphosphateEnterobacteria phage T4--707449 2D-image
4.3-etidronateEnterobacteria phage T4--673669 2D-image
0.29-geranyl diphosphateEnterobacteria phage T4--707449 2D-image
0.23-geranyl triphosphateEnterobacteria phage T4--707449-
4.9-isopentenyl diphosphateEnterobacteria phage T4--707449 2D-image
3.6-isopentenyl triphosphateEnterobacteria phage T4--707449-
0.26-methylenebisphosphonateEnterobacteria phage T4--673669-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
12.1-(2E,6E)-farnesyl diphosphateEnterobacteria phage T4--707449 2D-image
11.6-(2E,6E)-farnesyl triphosphateEnterobacteria phage T4--707449-
1.66-(ribonucleotide)n+msynthetic construct-pH 8.0, 22°C653882 2D-image
2.94-(ribonucleotide)n+msynthetic construct-pH 8.0, 22°C653882 2D-image
0.05-(RNA)nsynthetic construct-pH 6.0, 22°C, multiple-turnover derivatives 210t and 207t, engineered by changing the arrangement of the base pairs in the P2 stem649963 2D-image
0.266-(RNA)nsynthetic construct-pH 8.0, 22°C, multiple-turnover derivative 207t, engineered by changing the arrangement of the base pairs in the P2 stem649963 2D-image
0.583-(RNA)nsynthetic construct-pH 9.0, 22°C, multiple-turnover derivative 207t, engineered by changing the arrangement of the base pairs in the P2 stem649963 2D-image
2.33-(RNA)nsynthetic construct-pH 8.0, 22°C, multiple-turnover derivative 210t, engineered by changing the arrangement of the base pairs in the P2 stem649963 2D-image
2.94-(RNA)nsynthetic construct-pH 8.0, 22°C, multiple-turnover derivative 210t, engineered by changing the arrangement of the base pairs in the P2 stem649963 2D-image
6-(RNA)nsynthetic construct-pH 9.0, 22°C, multiple-turnover derivative 210t, engineered by changing the arrangement of the base pairs in the P2 stem649963 2D-image
6.08-(RNA)nsynthetic construct-pH 9.0, 22°C, multiple-turnover derivative 207t, engineered by changing the arrangement of the base pairs in the P2 stem649963 2D-image
0.055-ATPEnterobacteria phage T4-pH 7.4, 30°C, ATP as acceptor of AMP, Ap4A synthesis651051 2D-image
0.29-clodronateEnterobacteria phage T4--673669 2D-image
3.1-dimethylallyl diphosphateEnterobacteria phage T4--707449 2D-image
0.028-etidronateEnterobacteria phage T4--673669 2D-image
8.6-geranyl diphosphateEnterobacteria phage T4--707449 2D-image
52.2-geranyl triphosphateEnterobacteria phage T4--707449-
0.017-GTPEnterobacteria phage T4-pH 7.4, 37°C651051 2D-image
0.9-isopentenyl diphosphateEnterobacteria phage T4--707449 2D-image
6.7-isopentenyl triphosphateEnterobacteria phage T4--707449-
0.28-methylenebisphosphonateEnterobacteria phage T4--673669-

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
2.9-(2E,6E)-farnesyl diphosphateEnterobacteria phage T4--707449263972
166-(2E,6E)-farnesyl triphosphateEnterobacteria phage T4--7074490
2.7-dimethylallyl diphosphateEnterobacteria phage T4--7074499892
2.5-geranyl diphosphateEnterobacteria phage T4--70744910850
12-geranyl triphosphateEnterobacteria phage T4--7074490
4.5-isopentenyl diphosphateEnterobacteria phage T4--70744911832
24-isopentenyl triphosphateEnterobacteria phage T4--7074490

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.00216-4-hydroxy-3-[(E)-(5-hydroxy-7-sulfonaphthalen-2-yl)diazenyl]-7-[(1-phenylethenyl)amino]naphthalene-2-sulfonic acidTrypanosoma brucei-pH and temperature not specified in the publication716670 2D-image
0.00159-6-hydroxy-5-[(E)-[3-[(E)-(2-hydroxynaphthalen-1-yl)diazenyl]-5-sulfophenyl]diazenyl]naphthalene-2-sulfonic acidTrypanosoma brucei-pH and temperature not specified in the publication716670 2D-image
0.00836-7,7'-iminobis(4-hydroxynaphthalene-2-sulfonic acid)Trypanosoma brucei-pH and temperature not specified in the publication716670 2D-image
0.00153-7-amino-4-hydroxy-3-[(E)-(5-hydroxy-7-sulfonaphthalen-2-yl)diazenyl]naphthalene-2-sulfonic acidTrypanosoma brucei-pH and temperature not specified in the publication716670 2D-image

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.00152-Triticum aestivum--1999
0.0034-Enterobacteria phage T4-with geranyl diphosphate as substrate707449
0.0037-Enterobacteria phage T4-with dimethylallyl diphosphate as substrate707449
0.004-Enterobacteria phage T4-with (2E,6E)-farnesyl diphosphate as substrate707449
0.0062-Enterobacteria phage T4-with isopentenyl diphosphate as substrate707449
0.016-Enterobacteria phage T4-with (2E,6E)-farnesyl triphosphate as substrate707449
0.0166-Enterobacteria phage T4-with geranyl triphosphate as substrate707449
0.0335-Enterobacteria phage T4-with isopentenyl triphosphate as substrate707449
0.0383-Enterobacteria phage T4-5'-phosphate terminus rendered resistant to phosphatase1995
0.06-Enterobacteria phage T4--651051
additional information-Triticum aestivum--1983
additional information-Homo sapiens--1985
additional information-Triticum aestivum--1987
additional information-Enterobacteria phage T4--1989, 1990, 1992, 1993

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
5.57Enterobacteria phage T4--653679
67Enterobacteria phage T4--652387
6-Rhodothermus phage RM378-Tris buffer653392
6.5-Enterobacteria phage T4-adenylyltransferase activity653679, 653915
7-Rhodothermus phage RM378-MOPS buffer653392
7-Vibrio phage KVP40-adenylyltransferase activity654015
7.4-Enterobacteria phage T4--651051
7.58Phage TS2126-MOPS buffer662976
7.58.2Enterobacteria phage T4--1995
99.5Enterobacteria phage T4--653915

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
59.5Vibrio phage KVP40-activity is virtually nil at pH below 5.0 or above 9.5654015
5.58Enterobacteria phage T4-adenylyltransferase activity653679
5.77synthetic construct--650172
6.58Enterobacteria phage T4-around 70% of the maximum at pH 8.0651051
78.5Phage TS2126-pH 7.0: about 40% of maximal activity, pH 8.5: about 30% of maximal activity662976

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
64-Rhodothermus phage RM378--653392
6570Phage TS2126--662976
65-Methanothermobacter thermautotrophicus-RNA-adenylylate intermediates AppRNA are predominantly ligated to a circular product694452

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
35-Methanothermobacter thermautotrophicus-phosphodiester bond formation is suppressed and the majority of the RNA-adenylylate intermediates AppRNA are deadenylylated694452
5075Phage TS2126-50°C: about 35% of maximal activity, 75°C: about 60% of maximal activity662976

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
germTriticum aestivum--1983, 1984, 1987, 1988, 1991, 1999Manually annotated by BRENDA team
HeLa cellHomo sapiens--1985Manually annotated by BRENDA team
infected cellEnterobacteria phage T4--1990, 1992, 1993Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
kinetoplastLeishmania tarentolae--200231997Manually annotated by BRENDA team
mitochondrionTrypanosoma brucei--57391996, 650982, 651858, 653217, 653869, 653889Manually annotated by BRENDA team
mitochondrionLeishmania tarentolae--57391997Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
3ty5, downloadSCOP (3ty5)CATH (3ty5)Clostridium thermocellum (strain ATCC 27405 / DSM 1237)
3ty8, downloadSCOP (3ty8)CATH (3ty8)Clostridium thermocellum (strain ATCC 27405 / DSM 1237)
3ty9, downloadSCOP (3ty9)CATH (3ty9)Clostridium thermocellum (strain ATCC 27405 / DSM 1237)
2c5u, downloadSCOP (2c5u)CATH (2c5u)Enterobacteria phage T4
1vdx, downloadSCOP (1vdx)CATH (1vdx)Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
42000-Enterobacteria phage T4-SDS-PAGE651061
42000-Enterobacteria phage T4-recombinant protein, adsorption to Ni-agarose and step-elution with imidazole653679
42000-Vibrio phage KVP40-adsorption to Ni-agarose and step-elution with imidazole654015
4700048200Enterobacteria phage T4-gel filtration, high-speed sedimentation equilibrium centrifugation1910, 1994
48000-Trypanosoma brucei-SDS-PAGE653869
50000-Trypanosoma brucei-immunoblotting653869
51300-Rhodothermus phage RM378-calculated from the putative RNA ligase 1 gene653392
52000-Enterobacteria phage T4-gel filtration1995
52000-Trypanosoma brucei--653217

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Enterobacteria phage T4-x * 43000, SDS-PAGE1992
dimerMethanothermobacter thermautotrophicus-2 * 45000, calculated and sedimentation analysis694452
monomerEnterobacteria phage T4-1 * 45000, SDS-PAGE after reduction with 2-mercaptoethanol1994
monomerVibrio phage KVP40-1 * 42000, SDS-PAGE654015
additional informationTrypanosoma brucei-complex with 4 activities predicted to catalyze RNA editing: gRNA-directed endonuclease, terminal uridyl transferase, 3' U-specific endonuclease, RNA ligase. The complex is composed of 8 major polypeptides, three of which represent RNA ligase1996
additional informationMethanothermobacter thermautotrophicus-the C-terminal 127 amino acid segment is required for dimerization694452

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
2.6 A crystal structureEnterobacteria phage L1-677128
2.2 A resolution, crystal structure of a complete RNA ligase, Rnl1, in complex with adenosine 5'-(alpha,beta-methylenetriphosphate)Enterobacteria phage T4-674568
crystal structure of the ligase domain with AMP bound at the active site, space group P2(1)2(1)2, a = 57.72 A, b = 89.89 A, c = 47.74 AEnterobacteria phage T4-653915
hanging-drop vapor diffusion. Crystal structures of: 1. Covalent Rnl2-AMP intermediate, 2. Rnl2 bound to an adenylylated nicked duplex, captured immediately following reaction step 2, 3. Rnl2 at an adenylylated nick in a state poised for step 3. These structures illuminate the stereochemistry of nucleotidyl transfer and reveal how remodeling of active-site contacts and conformational changes propel the ligation reaction forwardEnterobacteria phage T4-672949
crystal structure of the catalytic domain of TbREL1 at 1.2 A resolution, in complex with ATP and magnesium.The magnesium ion interacts with the beta and gamma-phosphate groups and is almost perfectly octahedrally coordinated by six phosphate and water oxygen atoms. Sitting-drop, vapor-diffusion with 100 mM HEPES, 100 mM Mg2+ and 35% (w/v) PEG3350 at pH 7.0. The crystal belongs to space group P2(1), with cell dimensions of a = 44.9 A, b = 58.6 A, c = 53.0 A and beta = 100.2°, and one molecule in the asymmetric unitTrypanosoma brucei-662636
virtual screen of REL1 crystal structure for inhibitorsTrypanosoma brucei-694881

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
30-Triticum aestivum-stable for at least 2 h1983
56-Triticum aestivum-2 min, complete inactivation1983
6090Rhodothermus phage RM378-relatively stable at 60°C with a half-life of 10 h, activity increases after incubation, not stable at temperatures. Enzyme starts to lose activity rapidly, no activity at all after 1 h at 80°C, loses all of its activity after 5 min at 90°C653392
65-Phage TS2126-realatively stable at662976
80-Phage TS2126-loses all activity above662976

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
activity is unaffected by at least 3 freeze-thaw cyclesTriticum aestivum-1983, 1999
extremely unstable, when stored at low ionic strengthTriticum aestivum-1999

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-20°CEnterobacteria phage T4-1910, 1989
in liquid nitrogen, at 0.5 mg protein per ml, stable for at least 6 monthsEnterobacteria phage T4-1994
-20°C, stable for at least 6 monthsHomo sapiens-1985
-70°C, stable for at least 1 yearTriticum aestivum-1983
4°C, 32% loss of activity after 2 weeksTriticum aestivum-1983, 1999

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Enterobacteria phage T4-1989, 1993, 1995, 651061, 652246, 672949, 674568
histidine-taggedEnterobacteria phage T4-650653
large-scaleEnterobacteria phage T4-1990
mutant enzymesEnterobacteria phage T4-652387
mutant enzymes, expressed in bacteriaEnterobacteria phage T4-652429
produced in Escherichia coliEnterobacteria phage T4-653915
recombinant enzymeEnterobacteria phage T4-653679
-Homo sapiens-1985
-Phage TS2126-662976
recombinant enzymeRhodothermus phage RM378-653392
-synthetic construct-650172
-Triticum aestivum-1984, 1987
copurifies with 5'-hydroxyl polynucleotide kinaseTriticum aestivum-1983
-Trypanosoma brucei-653869
a complex with 4 activities predicted to catalyze RNA editing: gRNA-directed endonuclease, terminal uridyl transferase, 3' U-specific endonuclease, RNA ligaseTrypanosoma brucei-1996
editing complexTrypanosoma brucei-653217, 653889
purified via a C-terminal tandem affinity purification tagTrypanosoma brucei-716670
recombinantTrypanosoma brucei-662636
recombinant proteinVibrio phage KVP40-654015

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Enterobacteria phage T4-1986, 653915, 674568
encoded by T4 gene 24.1, mutants expressed in Escherichia coliEnterobacteria phage T4-652387
overexpressed in Escherichia coli BL21 (DE3)Enterobacteria phage T4-650653
transformed into Escherichia coli BL21 (DE3)Enterobacteria phage T4-652429
transformed into Escherichia coli BL21(DE3)Enterobacteria phage T4-653679
enzymatically active Leishmania tarentolae REL1 and REL2 and Trypanosoma brucei REL1 proteins from a Baculovirus expression system. The recombinant proteins can each integrate into an L-complex that has been depleted of the cognate ligase by RNAi. In the case of REL1, the integration of the recombinant enzyme functionally complements the REL1-depleted L-complex in an in vitro editing systemLeishmania tarentolae-663245
expression in Escherichia coliMethanothermobacter thermautotrophicus-694452
RNA ligase gene is inserted into a pET23b expression vector with a C-terminal His6-tag. This vector is transformed into Escherichia coli strain BL21Phage TS2126-662976
RnlA gene overexpressed in Escherichia coli BL21Rhodothermus phage RM378-653392
expression in Escherichia coliSaccharomyces cerevisiae-676215
-synthetic construct-650172
-Trypanosoma brucei-653889
enzymatically active Leishmania tarentolae REL1 and REL2 and Trypanosoma brucei REL1 proteins from a Baculovirus expression system. The recombinant proteins can each integrate into an L-complex that has been depleted of the cognate ligase by RNAi. In the case of REL1, the integration of the recombinant enzyme functionally complements the REL1-depleted L-complex in an in vitro editing systemTrypanosoma brucei-663245
expressed in Escherichia coliTrypanosoma brucei-650982
expressed in Sf9 insect cellsTrypanosoma brucei-716670
expressed in Trypanosoma brucei lines as an epitope-tagged fusion protein, recombinant p48 also expressed in Escherichia coliTrypanosoma brucei-653869
expression in Escherichia coli BL21goldDE3Trypanosoma brucei-662636
expressed in Escherichia coli as a His10-tagged fusion proteinVibrio phage KVP40-654015

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
K184ABranchiostoma floridaeC3YGD8inactive716756
DELTA1-105Deinococcus radiodurans-reacts with ATP to form covalent protein-adenylate adducts,mutant protein retains RNA sealing activity662304
DELTA1-125Deinococcus radiodurans-reacts with ATP to form covalent protein-adenylate adducts, mutant protein retains RNA sealing activity662304
DELTA1-135Deinococcus radiodurans-does not reacts with ATP to form covalent protein-adenylate adducts, mutant enzyme is unable to seal RNA strands662304
E230ADeinococcus radiodurans-mutant is defective in phosphodiester formation at a preadenylylated nick; mutant is dysfunctional in ligase adenylylation676230
E230DDeinococcus radiodurans-mutation reduces nick sealing activity to 1% of the wild-type level676230
E230QDeinococcus radiodurans-mutation reduces nick sealing activity to less than 1% of the wild-type level676230
E278ADeinococcus radiodurans-mutant enzyme retains adenylyltransferase and RNA ligase activities662304
E305ADeinococcus radiodurans-mutant is defective in phosphodiester formation at a preadenylylated nick; mutant is dysfunctional in ligase adenylylation676230
E305DDeinococcus radiodurans-mutation reduces nick sealing activity to 1% of the wild-type level676230
E305QDeinococcus radiodurans-mutation reduces nick sealing activity to 7% of the wild-type level676230
F281ADeinococcus radiodurans-mutant is defective in phosphodiester formation at a preadenylylated nick; mutant is dysfunctional in ligase adenylylation676230
F281LDeinococcus radiodurans-mutation reduces nick sealing activity to 5% of the wild-type level676230
G168ADeinococcus radiodurans-mutant is defective in phosphodiester formation at a preadenylylated nick; mutant is dysfunctional in ligase adenylylation676230
H167ADeinococcus radiodurans-mutant is dysfunctional in ligase adenylylation676230
H167NDeinococcus radiodurans-mutation reduces nick sealing activity to 7% of the wild-type level676230
H167QDeinococcus radiodurans-mutation reduces nick sealing activity to less than 1% of the wild-type level676230
K165ADeinococcus radiodurans-mutant is inert in enzyme-adenylate formation and nick-joining662304
K186ADeinococcus radiodurans-mutant is dysfunctional in ligase adenylylation676230
K186QDeinococcus radiodurans-mutation reduces nick sealing activity to 1% of the wild-type level676230
K186RDeinococcus radiodurans-mutation reduces nick sealing activity to 3% of the wild-type level676230
K326QDeinococcus radiodurans-mutation reduces nick sealing activity to less than 1% of the wild-type level676230
K326RDeinococcus radiodurans-mutation reduces nick sealing activity to 3% of the wild-type level676230
S185NDeinococcus radiodurans-mutation reduces nick sealing activity to less than 1% of the wild-type level676230
S185TDeinococcus radiodurans-mutation reduces nick sealing activity to 12% of the wild-type level676230
T163ADeinococcus radiodurans-mutant is dysfunctional in ligase adenylylation676230
T163SDeinococcus radiodurans-mutation reduces nick sealing activity to 2% of the wild-type level676230
T163VDeinococcus radiodurans-mutation reduces nick sealing activity to 30% of the wild-type level676230
D120AEnterobacteria phage T4-alanine-scanning mutagenesis652387
D135AEnterobacteria phage T4-about 5% of the ligation activity of wild-type enzyme, mutant enzyme displays 4% of the adenylyltransferase activity observed with wild-type enzyme662241
D244AEnterobacteria phage T4-site-directed mutagenesis652429
D292AEnterobacteria phage T4-no ligation activity662241
D292EEnterobacteria phage T4-about 10% of the ligation activity of wild-type enzyme662241
D308AEnterobacteria phage T4-about 70% of the ligation activity of wild-type enzyme662241
E139AEnterobacteria phage T4-about as active as wild-type enzyme in RNA ligation, mutant displays near wild-type adenylyltransferase activity662241
E185AEnterobacteria phage T4-site-directed mutagenesis652429
E204AEnterobacteria phage T4-substitution mutation introduced into the ORFb y PCR with two-stage overlap extension method653679
E227AEnterobacteria phage T4-site-directed mutagenesis652429
E227DEnterobacteria phage T4-site-directed mutagenesis652429
E227QEnterobacteria phage T4-site-directed mutagenesis652429
E295AEnterobacteria phage T4-about as active as wild-type enzyme in RNA ligation662241
E296AEnterobacteria phage T4-about 10% of the ligation activity of wild-type enzyme662241
E299AEnterobacteria phage T4-about 80% of the ligation activity of wild-type enzyme662241
E29AEnterobacteria phage T4-about 90% of the RNA ligation activity of wild-type enzyme, mutant displays near wild-type adenylyltransferase activity662241
E300AEnterobacteria phage T4-about 50% of the ligation activity of wild-type enzyme662241
E34AEnterobacteria phage T4-alanine-scanning mutagenesis652387
E34DEnterobacteria phage T4-substitution mutant, introduced into the rnl2 gene by PCR652387
E34QEnterobacteria phage T4-substitution mutant, introduced into the rnl2 gene by PCR652387
E63AEnterobacteria phage T4-about 80% of the RNA ligation activity of wild-type enzyme, mutant displays near wild-type adenylyltransferase activity662241
E81AEnterobacteria phage T4-site-directed mutagenesis652429
E99AEnterobacteria phage T4-alanine-scanning mutagenesis652387
F119AEnterobacteria phage T4-alanine-scanning mutagenesis652387
F76AEnterobacteria phage T4-site-directed mutagenesis652429
F77AEnterobacteria phage T4-site-directed mutagenesis652429
F77LEnterobacteria phage T4-site-directed mutagenesis652429
G102AEnterobacteria phage T4-site-directed mutagenesis652429
G228AEnterobacteria phage T4-site-directed mutagenesis652429
G55AEnterobacteria phage T4-site-directed mutagenesis652429
H250AEnterobacteria phage T4-pRNA circularization by the mutant enzyme is 6% of the wild-type rate677101
H37AEnterobacteria phage T4-substitution mutation introduced into the ORFb y PCR with two-stage overlap extension method653679
H37DEnterobacteria phage T4-substitution mutation introduced into the ORFb y PCR with two-stage overlap extension method653679
K107AEnterobacteria phage T4-about as active as wild-type enzyme in RNA ligation, mutant displays near wild-type adenylyltransferase activity662241
K117AEnterobacteria phage T4-mutation is lethal in vivo677101
K119AEnterobacteria phage T4-site-directed mutagenesis652429
K119QEnterobacteria phage T4-site-directed mutagenesis652429
K119REnterobacteria phage T4-site-directed mutagenesis652429
K189AEnterobacteria phage T4-alanine-scanning mutagenesis652387
K209AEnterobacteria phage T4-alanine-scanning mutagenesis652387
K225AEnterobacteria phage T4-substitution mutation introduced into the ORFb y PCR with two-stage overlap extension method653679
K227AEnterobacteria phage T4-substitution mutation introduced into the ORFb y PCR with two-stage overlap extension method653679
K240AEnterobacteria phage T4-site-directed mutagenesis652429
K240QEnterobacteria phage T4-site-directed mutagenesis652429
K240REnterobacteria phage T4-site-directed mutagenesis652429
K242AEnterobacteria phage T4-site-directed mutagenesis652429
K273AEnterobacteria phage T4-about as active as wild-type enzyme in RNA ligation662241
K314AEnterobacteria phage T4-about as active as wild-type enzyme in RNA ligation662241
K315AEnterobacteria phage T4-about 90% of the ligation activity of wild-type enzyme662241
K319AEnterobacteria phage T4-about as active as wild-type enzyme in RNA ligation662241
K35AEnterobacteria phage T4-substitution mutation introduced into the ORFb y PCR with two-stage overlap extension method653679
K54AEnterobacteria phage T4-about 15% of the RNA ligation activity of wild-type enzyme, mutant displays near wild-type adenylyltransferase activity662241
K75AEnterobacteria phage T4-site-directed mutagenesis652429
K75QEnterobacteria phage T4-site-directed mutagenesis652429
K75REnterobacteria phage T4-site-directed mutagenesis652429
K99AEnterobacteria phage T4-site-directed mutagenesis652429
N184AEnterobacteria phage T4-site-directed mutagenesis652429
N309AEnterobacteria phage T4-about 70% of the ligation activity of wild-type enzyme662241
N40AEnterobacteria phage T4-alanine-scanning mutagenesis652387
N40DEnterobacteria phage T4-substitution mutant, introduced into the rnl2 gene by PCR652387
N40QEnterobacteria phage T4-substitution mutant, introduced into the rnl2 gene by PCR652387
N40REnterobacteria phage T4-substitution mutant, introduced into the rnl2 gene by PCR652387
N78AEnterobacteria phage T4-site-directed mutagenesis652429
Q106AEnterobacteria phage T4-about 20% of the RNA ligation activity of wild-type enzyme, mutant displays near wild-type adenylyltransferase activity662241
R155AEnterobacteria phage T4-about 35% of the ligation activity of wild-type enzyme, mutant enzyme displays 16% of the adenylyltransferase activity observed with wild-type enzyme662241
R166AEnterobacteria phage T4-site-directed mutagenesis652429
R182AEnterobacteria phage T4-site-directed mutagenesis652429
R221AEnterobacteria phage T4-about 60% of the ligation activity of wild-type enzyme, mutant displays near wild-type adenylyltransferase activity662241
R266AEnterobacteria phage T4-no ligation activity662241
R266KEnterobacteria phage T4-about 50% of the ligation activity of wild-type enzyme662241
R266QEnterobacteria phage T4-no ligation activity662241
R33AEnterobacteria phage T4-no ligation activity, mutant enzyme displays 3% of the adenylyltransferase activity observed with wild-type enzyme662241
R54AEnterobacteria phage T4-site-directed mutagenesis652429
R54KEnterobacteria phage T4-site-directed mutagenesis652429
R54QEnterobacteria phage T4-site-directed mutagenesis652429
R55AEnterobacteria phage T4-alanine-scanning mutagenesis652387
R71AEnterobacteria phage T4-site-directed mutagenesis652429
S103AEnterobacteria phage T4-pRNA circularization by the mutant enzyme is 5% of the wild-type rate; S103A strain is temperature sensitive, no growth at 37°C677101
S118AEnterobacteria phage T4-S118 strain is temperature sensitive, no growth at 37°C677101
S170AEnterobacteria phage T4-about 5% of the ligation activity of wild-type enzyme, mutant enzyme displays 8% of the adenylyltransferase activity observed with wild-type enzyme662241
S272AEnterobacteria phage T4-about 50% of the ligation activity of wild-type enzyme662241
S292NEnterobacteria phage T4-about 25% of the ligation activity of wild-type enzyme662241
W329AEnterobacteria phage T4-about as active as wild-type enzyme in RNA ligation662241
Y136AEnterobacteria phage T4-about 95% of the ligation activity of wild-type enzyme, mutant displays near wild-type adenylyltransferase activity662241
D425NSaccharomyces cerevisiae-lethal mutation676215
D726ASaccharomyces cerevisiae-lethal mutation676215
E218ASaccharomyces cerevisiae-lethal mutation676215
E326ASaccharomyces cerevisiae-lethal mutation676215
E741ASaccharomyces cerevisiae-lethal mutation676215
H1060ASaccharomyces cerevisiae-lethal mutation676215
H515ASaccharomyces cerevisiae-lethal mutation676215
H515NSaccharomyces cerevisiae-lethal mutation676215
H515QSaccharomyces cerevisiae-lethal mutation676215
H777NSaccharomyces cerevisiae-lethal mutation676215
H777QSaccharomyces cerevisiae-lethal mutation676215
K152ASaccharomyces cerevisiae-lethal mutation676215
K541ASaccharomyces cerevisiae-lethal mutation676215
K543ASaccharomyces cerevisiae-lethal mutation676215
R463ASaccharomyces cerevisiae-lethal mutation676215
R463KSaccharomyces cerevisiae-lethal mutation676215
R463QSaccharomyces cerevisiae-lethal mutation676215
R511KSaccharomyces cerevisiae-lethal mutation676215
R511QSaccharomyces cerevisiae-lethal mutation676215
S701ASaccharomyces cerevisiae-lethal mutation676215
T1001ASaccharomyces cerevisiae-lethal mutation676215
T675ASaccharomyces cerevisiae-lethal mutation676215
T675VSaccharomyces cerevisiae-lethal mutation676215
K109RTrypanosoma brucei-site-directed mutagenesis650982
K86RTrypanosoma brucei-site-directed mutagenesis650982
L104AEnterobacteria phage T4-L104A strain is temperature sensitive, no growth at 37°C; pRNA circularization by the mutant enzyme is 6% of the wild-type rate677101
additional informationEnterobacteria phage T4-S121A, S124A, and H250 strains grow at all temperatures677101
Y5AEnterobacteria phage T4-about 10% of the RNA ligation activity of wild-type enzyme, mutant enzyme displays 39% of the adenylyltransferase activity observed with wild-type enzyme662241
additional informationMethanothermobacter thermautotrophicus-expression of N-terminal amino acids 1-253 gives a protein defective in overall ligation but retaining the ability to form EpA intermediate, bind to pRNA and transfer AMP to pRNA, albeit less efficiently than wild-type ligase. Expression of amino acids 255-381 results in a protein that fails to form a detectable protein-RNA complex and does not support overall ligation or RNA circularization694452

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
synthesisEnterobacteria phage T4-synthesis of oligoribonucleotides with defined sequence1989
synthesisEnterobacteria phage T4-RNA ligase-mediated method for the efficient creation of large, synthetic RNAs677096
synthesisEnterobacteria phage T4-selective isotope labeling of RNA by introducing a labeled RNA segment via a two-step protocol, which uses T4 DNA ligase and T4 RNA ligase 1, and a one-pot protocol, which uses T4 RNA ligase 1 alone. Protection of termini is not required, provided segmentation sites can be chosen such that the segments fold into the target structure or target-like structures and thus are not trapped into stable alternate structures. Labeling protocols are generally applicable to large RNA molecules and can be extended to more than three segments694461
molecular biologyPhage TS2126-RNA ligase-mediated rapid amplification of cDNA ends (RLM-RACE); the properties of TS2126 RNA ligase 1 makes it very attractive for processes like adaptor ligation, and single-stranded solid phase gene synthesis662976
medicineTrypanosoma brucei-regulated repression of the enzyme blocks editing, this repression is lethal in bloodforms of the parasite, indicating that editing is essential in the mammalian stage of the life cycle, the editing complex, which is present in all kinetoplastid parasites, may thus be a chemotherapeutic target653889

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
Acquired Immunodeficiency SyndromeMutational analysis defines the 5'-kinase and 3'-phosphatase active sites of T4 polynucleotide kinase. PubMed
InfectionBacteriophage T4 RNA ligase is gene 63 product, the protein that promotes tail fiber attachment to the baseplate. PubMed
InfectionBacteriophage T4 RNA ligase: preparation of a physically homogeneous, nuclease-free enzyme from hyperproducing infected cells. PubMed
InfectionBacteriophage T4-induced anticodon-loop nuclease detected in a host strain restrictive to RNA ligase mutants. PubMed
InfectionHost transfer RNA cleavage and reunion in T4-infected Escherichia coli CTr5x. PubMed
InfectionIn vitro reconstitution of anticodon nuclease from components encoded by phage T4 and Escherichia coli CTr5X. PubMed
InfectionPhage and host genetic determinants of the specific anticodon loop cleavages in bacteriophage T4-infected Escherichia coli CTr5X. PubMed
InfectionRNA ligase reaction products in plasmolyzed Escherichia coli cells infected by T4 bacteriophage. PubMed
InfectionStructure of a tRNA repair enzyme and molecular biology workhorse: T4 polynucleotide kinase. PubMed
InfectionThe C-terminal domain of T4 RNA ligase 1 confers specificity for tRNA repair. PubMed
Influenza, HumanCrystalDock: a novel approach to fragment-based drug design. PubMed
Influenza, HumanRapid method for the characterization of 3' and 5' UTRs of influenza viruses. PubMed
Trypanosomiasis, AfricanCrystalDock: a novel approach to fragment-based drug design. PubMed
Trypanosomiasis, AfricanFunctional and Structural Insights Revealed by Molecular Dynamics Simulations of an Essential RNA Editing Ligase in Trypanosoma brucei. PubMed
Vesicular StomatitisNucleotide sequence homology at the 3' termini of RNA from vesicular stomatitis virus and its defective interfering particles. PubMed
Vesicular StomatitisThe complete sequence of a unique RNA species synthesized by a DI particle of VSV. PubMed

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
1910Maunders, M.J.DNA and RNA ligases (EC 6.5.1.1, EC 6.5.1.2, and EC 6.5.1.3)Methods Mol. Biol.16213-2301993Enterobacteria phage T4 PubMed
1983Pick, L.; Hurwitz, J.Purification of wheat germ RNA ligase. I. Characterization of a ligase-associated 5'-hydroxyl polynucleotide kinase activityJ. Biol. Chem.2616684-66931986Triticum aestivum PubMed
1984Pick, L.; Furneaux, H.; Hurwitz, J.Purification of wheat germ RNA ligase. II. Mechanism of action of wheat germ RNA ligaseJ. Biol. Chem.2616694-67041986Triticum aestivum PubMed
1985Perkins, K.K.; Furneaux, H.; Hurwitz, J.Isolation and characterization of an RNA ligase from HeLa cellsProc. Natl. Acad. Sci. USA82684-6881985Homo sapiens PubMed
1986Rand, K.N.; Gait, M.J.Sequence and cloning of bacteriophage T4 gene 63 encoding RNA ligase and tail fibre attachment activitiesEMBO J.3397-4021984Enterobacteria phage T4 PubMed
1987Furneaux, H.; Pick, L.; Hurwitz, J.Isolation and characterization of RNA ligase from wheat germProc. Natl. Acad. Sci. USA803933-39371983Triticum aestivum PubMed
1988Gegenheimer, P.; Gabius, H.J.; Peebles, C.L.; Abelson, J.An RNA ligase from wheat germ which participates in transfer RNA splicing in vitroJ. Biol. Chem.2588365-83731983Triticum aestivum PubMed
1989Mei-Hao, H.; Wang, A.; Hui-Fen, H.Purification of T4 RNA ligase by dextran blue-Sepharose 4B affinity chromatographyAnal. Biochem.1251-51982Enterobacteria phage T4 PubMed
1990Dolganov, G.M.; Chestukhin, A.V.; Shemyakin, M.A new procedure for the simultaneous large-scale purification of bacteriophage-T4-induced polynucleotide kinase, DNA ligase, RNA ligase and DNA polymeraseEur. J. Biochem.114247-2541981Enterobacteria phage T4 PubMed
1991Konarska, M.; Filipowicz, W.; Domdey, H.; Gross, H.J.Formation of a 2'-phosphomonoester, 3',5'-phosphodiester linkage by a novel RNA ligase in wheat germNature293112-1161981Triticum aestivum PubMed
1992Moseman McCoy, M.I.; Lubben, T.H.; Gumport, R.I.The Purification of nuclease-free T4-RNA ligaseBiochim. Biophys. Acta562149-1611979Enterobacteria phage T4 PubMed
1993Sugiura, M.; Suzuki, M.; Ohtsuka, E.; Nishikawa, S.; Uemura, H.; Ikehara, M.Purification of T4 RNA ligase by 2',5'-ADP Sepharose chromatographyFEBS Lett.9773-761979Enterobacteria phage T4 PubMed
1994Last, J.A.; Anderson, W.F.Purification and properties of bacteriophage T4-induced RNA ligaseArch. Biochem. Biophys.174167-1761976Enterobacteria phage T4 PubMed
1995Silber, R.; Malathi, V.G.; Hurwitz, J.Purification and properties of bacteriophage T4-induced RNA ligaseProc. Natl. Acad. Sci. USA693009-30131972Enterobacteria phage T4 PubMed
1996Rusche, L.N.; Cruz-Reyes, J.; Piller, K.J.; Sollner-Webb, B.Purification of a functional enzymatic editing complex from Trypanosoma brucei mitochondriaEMBO J.164069-40811997Trypanosoma brucei PubMed
1997Bakalara, N.; Simpson, A.M.; Simpson, L.The Leishmania kinetoplast-mitochondrion contains terminal uridylyltransferase and RNA ligase activitiesJ. Biol. Chem.26418679-186861989Leishmania tarentolae PubMed
1998Juodka, B.; Labeikyte, D.Inhibition of the first stage of RNA ligase reaction by ATP analoguesNucleosides Nucleotides10367-3701991Enterobacteria phage T4-
1999Pick, L.; Furneaux, H.M.; Hurwitz, J.Purification and characterization of wheat germ RNA ligase and associated activitiesMethods Enzymol.181480-4991990Triticum aestivum PubMed
2000Harada, K.; Orgel, L.E.In vitro selection of optimal substrates for T4 RNA ligaseProc. Natl. Acad. Sci. USA901576-15791993Enterobacteria phage T4 PubMed
2001Iuoda, B.A.; Labeikite, D.; Sasnauskene, S.I.Substrate specificity of T4 RNA-ligase: the role of a purine nucleotide base in forming a covalent AMP-RNA ligase complexBiokhimiia58857-8651993Enterobacteria phage T4 PubMed
649963Bergman, N.H.; Johnston, W.K.; Bartel, D.P.Kinetic framework for ligation by an efficient RNA ligase ribozymeBiochemistry393115-31232000synthetic construct PubMed
650172Glasner, M.E.; Bergman, N.H.; Bartel, D.P.Metal ion requirements for structure and catalysis of an RNA ligase ribozymeBiochemistry418103-81122002synthetic construct PubMed
650653Wang, Q.S.; Unrau, P.J.Purification of histidine-tagged T4 RNA ligase from E. coliBiotechniques331256-12602002Enterobacteria phage T4 PubMed
650982Huang, C.E.; Cruz-Reyes, J.; Zhelonkina, A.G.; O'Hearn, S.; Wirtz, E.; Sollner-Webb, B.Roles for ligases in the RNA editing complex of Trypanosoma brucei: band IV is needed for U-deletion and RNA repairEMBO J.204694-47032001Trypanosoma brucei PubMed
651051Atencia, E.A.; Madrid, O.; Gunther Sillero, M.A.; Sillero, A.T4 RNA ligase catalyzes the synthesis of dinucleoside polyphosphatesEur. J. Biochem.261802-8111999Enterobacteria phage T4 PubMed
651061Atencia, E.A.; Montes, M.; Gunther Sillero, M.A.; Sillero, A.Several dinucleoside polyphosphates are acceptor substrates in the T4 RNA ligase catalyzed reactionEur. J. Biochem.2671707-17142000Enterobacteria phage T4 PubMed
651858Piller, K.J.; Rusche, L.N.; Sollner-Webb, B.Trypanosoma brucei RNA editing. A full round of uridylate insertional editing in vitro mediated by endonuclease and RNA ligaseJ. Biol. Chem.2714613-46191996Trypanosoma brucei PubMed
652246Cherepanov, A.V.; de Vries, S.Kinetic mechanism of the Mg2+-dependent nucleotidyl transfer catalyzed by T4 DNA and RNA ligasesJ. Biol. Chem.2771695-17042002Enterobacteria phage T4 PubMed
652387Yin, S.; Ho, C.K.; Shuman, S.Structure-function analysis of T4 RNA ligase 2J. Biol. Chem.27817601-176082003Enterobacteria phage T4 PubMed
652429Wang, L.K.; Ho, C.K.; Pei, Y.; Shuman, S.Mutational analysis of bacteriophage T4 RNA ligase 1. Different functional groups are required for the nucleotidyl transfer and phosphodiester bond formation steps of the ligation reactionJ. Biol. Chem.27829454-294622003Enterobacteria phage T4 PubMed
653217Cruz-Reyes, J.; Zhelonkina, A.G.; Huang, C.E.; Sollner-Webb, B.Distinct functions of two RNA ligases in active Trypanosoma brucei RNA editing complexesMol. Cell. Biol.224652-46602002Trypanosoma brucei PubMed
653234Nishigaki, K.; Taguchi, K.; Kinoshita, Y.; Aita, T.; Husimi, Y.Y-ligation: an efficient method for ligating single-stranded DNAs and RNAs with T4 RNA ligaseMol. Divers.4187-1901998Enterobacteria phage T4 PubMed
653368Ekland, E.H.; Bartel, D.P.The secondary structure and sequence optimization of an RNA ligase ribozymeNucleic Acids Res.233231-32381995synthetic construct PubMed
653369Wang, L.; Ruffner, D.E.Oligoribonucleotide circularization by 'template-mediated' ligation with T4 RNA ligase: synthesis of circular hammerhead ribozymesNucleic Acids Res.262502-25041998Enterobacteria phage T4 PubMed
653392Blondal, T.; Hjorleifsdottir, S.H.; Fridjonsson, O.F.; Aevarsson, A.; Skirnisdottir, S.; Hermannsdottir, A.G.; Hreggvidsson, G.O.; Smith, A.V.; Kristjansson, J.K.Discovery and characterization of a thermostable bacteriophage RNA ligase homologous to T4 RNA ligase 1Nucleic Acids Res.317247-72542003Rhodothermus phage RM378 PubMed
653679Ho, C.K.; Shuman, S.Bacteriophage T4 RNA ligase 2 (gp24.1) exemplifies a family of RNA ligases found in all phylogenetic domainsProc. Natl. Acad. Sci. USA9912709-127142002Enterobacteria phage T4 PubMed
653869McManus, M.T.; Shimamura, M.; Grams, J.; Hajduk, S.L.Identification of candidate mitochondrial RNA editing ligases from Trypanosoma bruceiRNA7167-1752001Trypanosoma brucei PubMed
653882Ekland, E.H.; Szostak, J.W.; Bartel, D.P.Structurally complex and highly active RNA ligases derived from random RNA sequencesScience269364-3701995synthetic construct PubMed
653889Schnaufer, A.; Panigrahi, A.K.; Panicucci, B.; Igo, R.P., Jr.; Wirtz, E.; Salavati, R.; Stuart, K.An RNA ligase essential for RNA editing and survival of the bloodstream form of Trypanosoma bruceiScience2912159-21622001Trypanosoma brucei PubMed
653915Ho, C.K.; Wang, L.K.; Lima, C.D.; Shuman, S.Structure and mechanism of RNA ligaseStructure12327-3392004Enterobacteria phage T4 PubMed
654015Yin, S.; Kiong Ho, C.; Miller, E.S.; Shuman, S.Characterization of bacteriophage KVP40 and T4 RNA ligase 2Virology319141-1512004Enterobacteria phage T4, Vibrio phage KVP40 PubMed
662241Nandakumar, J.; Ho, C.K.; Lima, C.D.; Shuman, S.RNA substrate specificity and structure-guided mutational analysis of bacteriophage T4 RNA ligase 2J. Biol. Chem.27931337-313472004Enterobacteria phage T4 PubMed
662304Martins, A.; Shuman, S.An RNA ligase from Deinococcus radioduransJ. Biol. Chem.27950654-506612004Deinococcus radiodurans PubMed
662636Deng, J.; Schnaufer, A.; Salavati, R.; Stuart, K.D.; Hol, W.G.High resolution crystal structure of a key editosome enzyme from Trypanosoma brucei:RNA editing ligase 1J. Mol. Biol.343601-6132004Trypanosoma brucei PubMed
662976Blondal, T.; Thorisdottir, A.; Unnsteinsdottir, U.; Hjorleifsdottir, S.; Aevarsson, A.; Ernstsson, S.; Fridjonsson, O.H.; Skirnisdottir, S.; Wheat, J.O.; Hermannsdottir, A.G.; Sigurdsson, S.T.; Hreggvidsson, G.O.; Smith, A.V.; Kristjansson, J.K.Isolation and characterization of a thermostable RNA ligase 1 from a Thermus scotoductus bacteriophage TS2126 with good single-stranded DNA ligation propertiesNucleic Acids Res.33135-1422005Phage TS2126 PubMed
663245Gao, G.; Simpson, A.M.; Kang, X.; Rogers, K.; Nebohacova, M.; Li, F.; Simpson, L.Functional complementation of Trypanosoma brucei RNA in vitro editing with recombinant RNA ligaseProc. Natl. Acad. Sci. USA1024712-47172005Leishmania tarentolae, Trypanosoma brucei PubMed
672949Nandakumar, J.; Shuman, S.; Lima, C.D.RNA ligase structures reveal the basis for RNA specificity and conformational changes that drive ligation forwardCell12771-842006Enterobacteria phage T4 PubMed
673669Sillero, M.A.; de Diego, A.; Silles, E.; Perez-Zuniga, F.; Sillero, A.Synthesis of bisphosphonate derivatives of ATP by T4 RNA ligaseFEBS Lett.5805723-57272006Enterobacteria phage T4 PubMed
674568El Omari, K.; Ren, J.; Bird, L.E.; Bona, M.K.; Klarmann, G.; LeGrice, S.F.; Stammers, D.K.Molecular architecture and ligand recognition determinants for T4 RNA ligaseJ. Biol. Chem.2811573-15792006Enterobacteria phage T4 PubMed
676215Wang, L.K.; Schwer, B.; Englert, M.; Beier, H.; Shuman, S.Structure-function analysis of the kinase-CPD domain of yeast tRNA ligase (Trl1) and requirements for complementation of tRNA splicing by a plant Trl1 homologNucleic Acids Res.34517-5272006Saccharomyces cerevisiae PubMed
676230Raymond, A.; Shuman, S.Deinococcus radiodurans RNA ligase exemplifies a novel ligase clade with a distinctive N-terminal module that is important for 5-PO4 nick sealing and ligase adenylylation but dispensable for phosphodiester formation at an adenylylated nickNucleic Acids Res.35839-8492007Deinococcus radiodurans PubMed
677096Stark, M.R.; Pleiss, J.A.; Deras, M.; Scaringe, S.A.; Rader, S.D.An RNA ligase-mediated method for the efficient creation of large, synthetic RNAsRNA122014-20192006Enterobacteria phage T4 PubMed
677101Wang, L.K.; Nandakumar, J.; Schwer, B.; Shuman, S.The C-terminal domain of T4 RNA ligase 1 confers specificity for tRNA repairRNA131235-12442007Enterobacteria phage T4 PubMed
677128Robertson, M.P.; Scott, W.G.The structural basis of ribozyme-catalyzed RNA assemblyScience3151549-15532007Enterobacteria phage L1 PubMed
694311Vicens, Q.; Cech, T.R.A natural ribozyme with 3,5 RNA ligase activityNat. Chem. Biol.597-992009Anabaena sp. PubMed
694452Torchia, C.; Takagi, Y.; Ho, C.K.Archaeal RNA ligase is a homodimeric protein that catalyzes intramolecular ligation of single-stranded RNA and DNANucleic Acids Res.366218-62272008Methanothermobacter thermautotrophicus PubMed
694461Nelissen, F.H.; van Gammeren, A.J.; Tessari, M.; Girard, F.C.; Heus, H.A.; Wijmenga, S.S.Multiple segmental and selective isotope labeling of large RNA for NMR structural studiesNucleic Acids Res.36e892008Enterobacteria phage T4 PubMed
694881Amaro, R.E.; Schnaufer, A.; Interthal, H.; Hol, W.; Stuart, K.D.; McCammon, J.A.Discovery of drug-like inhibitors of an essential RNA-editing ligase in Trypanosoma bruceiProc. Natl. Acad. Sci. USA10517278-172832008Trypanosoma brucei PubMed
707449Sillero, M.A.; de Diego, A.; Tavares, J.E.; Silva, J.A.; Perez-Zuniga, F.J.; Sillero, A.Synthesis of ATP derivatives of compounds of the mevalonate pathway (isopentenyl di- and triphosphate; geranyl di- and triphosphate, farnesyl di- and triphosphate, and dimethylallyl diphosphate) catalyzed by T4 RNA ligase, T4 DNA ligase and other ligasesBiochem. Pharmacol.78335-3432009Enterobacteria phage T4 PubMed
708449Swift, R.V.; Amaro, R.E.Discovery and design of DNA and RNA ligase inhibitors in infectious microorganismsExpert Opin. Drug Discov.41281-12942009Trypanosoma brucei PubMed
713745Park, K.; Choi, B.R.; Kim, Y.S.; Shin, S.; Hah, S.S.; Jung, W.; Oh, S.; Kim, D.E.Detection of single-base mutation in RNA using T4 RNA ligase-based nick-joining or DNAzyme-based nick-generationAnal. Biochem.414303-3052011Enterobacteria phage T4 PubMed
714026Makino, S.; Sawasaki, T.; Endo, Y.; Takai, K.In vitro dissection revealed that the kinase domain of wheat RNA ligase is physically isolatable from the flanking domains as a non-overlapping domain enzymeBiochem. Biophys. Res. Commun.397762-7662010Triticum aestivum PubMed
714046Makino, S.; Sawasaki, T.; Endo, Y.; Takai, K.Use of domain enzymes from wheat RNA ligase for in vitro preparation of RNA moleculesBiochem. Biophys. Res. Commun.4041050-10542011Triticum aestivum PubMed
716670Durrant, J.D.; Hall, L.; Swift, R.V.; Landon, M.; Schnaufer, A.; Amaro, R.E.Novel naphthalene-based inhibitors of Trypanosoma brucei RNA editing ligase 1PLoS Negl. Trop. Dis.4e8032010Trypanosoma brucei PubMed
716756Englert, M.; Sheppard, K.; Gundllapalli, S.; Beier, H.; Soell, D.Branchiostoma floridae has separate healing and sealing enzymes for 5'-phosphate RNA ligationProc. Natl. Acad. Sci. USA10716834-168392010Branchiostoma floridae PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 6.5.1.3)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)