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Information on EC 3.6.1.61 - diadenosine hexaphosphate hydrolase (ATP-forming) and Organism(s) Escherichia coli and UniProt Accession P0A776

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IUBMB Comments
The enzyme requires the presence of the divalent cations (Mn2+, Mg2+, Zn2+, and Co2+). It hydrolyses P1,P4-bis(5-guanosyl) tetraphosphate very slowly [cf. EC 3.6.1.17, bis(5-nucleosyl)-tetraphosphatase (asymmetrical)].
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This record set is specific for:
Escherichia coli
UNIPROT: P0A776
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
Ndx1, ygdP, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
P1,P6-bis(5'-adenosyl)hexaphosphate nucleotidohydrolase (ATP-forming)
The enzyme requires the presence of the divalent cations (Mn2+, Mg2+, Zn2+, and Co2+). It hydrolyses P1,P4-bis(5-guanosyl) tetraphosphate very slowly [cf. EC 3.6.1.17, bis(5-nucleosyl)-tetraphosphatase (asymmetrical)].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
P1,P4-bis(5'-adenosyl)tetraphosphate + H2O
ATP + AMP
show the reaction diagram
-
-
-
?
P1,P5-bis(5'-adenosyl)pentaphosphate + H2O
ATP + ADP
show the reaction diagram
preferred substrate
-
-
?
P1,P6-bis(5'-adenosyl)hexaphosphate + H2O
2 ATP
show the reaction diagram
hydrolyzed at about 70% compared to P1,P5-bis(5'-adenosyl)pentaphosphate
-
-
?
additional information
?
-
YgdP does not act on other nucleoside diphosphate derivatives such as ADP-ribose, NADH, UDP-glucose and P1,P3-bis(5'-adenosyl)triphosphate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
divalent cation required, Mg2+, Zn2+ or Mn2+. Maximal activity with 10 mM Mg2+ and to a lesser extent with Zn2+ and Mn2+
Mn2+
divalent cation required, Mg2+, Zn2+ or Mn2+. Maximal activity with 10 mM Mg2+ and to a lesser extent with Zn2+ and Mn2+
Zn2+
divalent cation required, Mg2+, Zn2+ or Mn2+. Maximal activity with 10 mM Mg2+ and to a lesser extent with Zn2+ and Mn2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 9.0, 37°C
0.36
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 9.0, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 9.0, 37°C
1
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 9.0, 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.43
P1,P4-bis(5'-adenosyl)tetraphosphate
pH 9.0, 37°C
2.78
P1,P5-bis(5'-adenosyl)pentaphosphate
pH 9.0, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
gel filtration
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bessman, M.J.; Walsh, J.D.; Dunn, C.A.; Swaminathan, J.; Weldon, J.E.; Shen, J.
The gene ygdP, associated with the invasiveness of Escherichia coli K1, designates a Nudix hydrolase, Orf176, active on adenosine (5')-pentaphospho-(5')-adenosine (Ap5A)
J. Biol. Chem.
276
37834-37838
2001
Escherichia coli (P0A776)
Manually annotated by BRENDA team