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Information on EC 5.6.2.2 - DNA topoisomerase (ATP-hydrolysing) and Organism(s) Pyrococcus furiosus and UniProt Accession P95479

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EC Tree
IUBMB Comments
The enzyme can introduce negative superhelical turns into double-stranded circular DNA. One unit has nicking-closing activity, and another catalyses super-twisting and hydrolysis of ATP (cf. EC 5.6.2.1 DNA topoisomerase).
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This record set is specific for:
Pyrococcus furiosus
UNIPROT: P95479
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Word Map
The taxonomic range for the selected organisms is: Pyrococcus furiosus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
ATP-dependent breakage, passage and rejoining of double-stranded DNA
Synonyms
atpase, topoisomerase ii, dna gyrase, topo ii, gyrase, top2a, dna topoisomerase ii, topoisomerase iialpha, topo iialpha, topoisomerase ii alpha, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DNA gyrase
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DNA topoisomerase II
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DNA topoisomerase type II
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Isomerase, deoxyribonucleate topo-, II
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NP170 proteins
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Nuclear proteins 170,000-mol.wt.
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Protein Gp39
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Protein Gp52
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Protein Gp60
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Proteins , NP170 (specific proteins and subclasses nuclear protein, 170,000-mol.-wt.)
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PsTopII
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TOPOII
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Topoisomerase II
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Topoisomerase type II
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Type II-DNA-topoisomerase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
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SYSTEMATIC NAME
IUBMB Comments
DNA topoisomerase (ATP-hydrolysing)
The enzyme can introduce negative superhelical turns into double-stranded circular DNA. One unit has nicking-closing activity, and another catalyses super-twisting and hydrolysis of ATP (cf. EC 5.6.2.1 DNA topoisomerase).
CAS REGISTRY NUMBER
COMMENTARY hide
142805-56-9
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80449-01-0
formerly not distinguished from EC 5.99.1.2
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
negatively supercoiled pBR322 DNA
?
show the reaction diagram
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ATP-dependent positive supercoiling activity
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?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
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assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120000
sucrose gradient centrifugation, N-terminal microsequencing
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
the monmomeric protein contains a helicase-like module and a type I topoisomerase module
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Borges, K.M.; Bergerat, A.; Bogert, A.M.; DiRuggiero, J.; Forterre, P.; Robb, F.T.
Characterization of the reverse gyrase from the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
179
1721-1726
1997
Pyrococcus furiosus (P95479)
Manually annotated by BRENDA team
Bouthier de la Tour, C.; Portemer, C.; Nadal, M.; Stetter, K.O.; Forterre, P.; Duguet, M.
Reverse gyrase, a hallmark of the hyperthermophilic archaebacteria
J. Bacteriol.
172
6803-6808
1990
Archaeoglobus fulgidus, Methanopyrus kandleri, Methanothermus fervidus, Pyrobaculum islandicum, Pyrococcus furiosus, Pyrodictium occultum, Sulfolobus acidocaldarius, Sulfolobus sp., Thermococcus sp., Pyrobaculum neutrophilum, Acidianus infernus, Thermococcus celer, Desulfurococcus saccharovorans, Sulfolobus sp. B12, Thermococcus sp. OB9
Manually annotated by BRENDA team