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Information on EC 3.6.4.B7 - RadA recombinase

for references in articles please use BRENDA:EC3.6.4.B7
preliminary BRENDA-supplied EC number
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UNIPROT: Q9UWR5
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Word Map
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Reaction Schemes
Synonyms
rad51, rada/sms, ssorada, rada recombinase, rada intein, dna repair protein rad51 homolog 1, radc1, dna repair and recombination protein, mvrada, hvo rada, more
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
show the reaction diagram
the enzyme binds ssDNA, hydrolyzes ATP in a DNA-dependent manner and to catalyzes DNA strand exchange.It shows the ability to bind ssDNA and catalyze DNA strand exchange between ssDNA and homologous linear dsDNA. The ssDNA-dependent ATPase activity displays a temperature-dependent capacity to exist in two different catalytic modes, with 75°C being the critical threshold temperature
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
the enzyme requires the presence of bivalent cations, such as Mg2+ and Mn2+
Mn2+
the enzyme requires the presence of bivalent cations, such as Mg2+ and Mn2+
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ssDNA
at 75°C, all DNAs tested stimulated ATPase activity of the RadA. The ssDNA-dependent ATPase activity of displays a temperature-dependent capacity to exist in two different catalytic modes, with 75°C being the critical threshold temperature
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
49 - 531
ATP
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013 - 0.068
ATP
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85
the rate of the ATP hydrolysis increases with temperature up to 85°C, the maximum temperature at which the protein maintains its secondary structure
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75
the enzyme exhibits a biphasic Arrhenius plot of ATP hydrolysis with two characteristic energies of activation with a break point at 75°C. The activation energy below 75°C is higher than that above the break point. The cooperativity of ATP hydrolysis and ssDNA-binding ability of the protein above 75°C are greater than those at lower temperatures
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RADA_PYRIL
Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3)
330
0
36799
Swiss-Prot
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 87
the enzyme maintains its secondary structure and activities in vitro at high temperatures, up to 87°C. It also shows high stability of 18.3 kcal/mol at 25°C and neutral pH
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanidine-HCl
the enzyme is stable up to 4.5 M guanidine hydrochloride
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Spies, M.; Kil, Y.; Masui, R.; Kato, R.; Kujo, C.; Ohshima, T.; Kuramitsu, S.; Lanzov, V.
The RadA protein from a hyperthermophilic archaeon Pyrobaculum islandicum is a DNA-dependent ATPase that exhibits two disparate catalytic modes, with a transition temperature at 75C
Eur. J. Biochem.
267
1125-1137
2000
Pyrobaculum islandicum (Q9UWR5), Pyrobaculum islandicum, Pyrobaculum islandicum DSM 4184 (Q9UWR5)
Manually annotated by BRENDA team