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Information on EC 2.5.1.B21 - S-adenosyl-L-methionine hydroxide adenosyltransferase and Organism(s) Pyrococcus horikoshii and UniProt Accession O58212

for references in articles please use BRENDA:EC2.5.1.B21
preliminary BRENDA-supplied EC number
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Pyrococcus horikoshii
UNIPROT: O58212 not found.
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The taxonomic range for the selected organisms is: Pyrococcus horikoshii
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
duf-62, duf62, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
duf62
gene name. duf: domain of unknown function. Found in extremophiles
SAM hydroxide adenosyltransferase
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:hydroxide adenosyltransferase
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5'-deoxy-5'-chloroadenosine + H2O
adenosine + ?
show the reaction diagram
adenosine is generated from 5'-deoxy-5'-chloroadenosine with much lower efficiency than from S-adenosyl-L-methionine
-
-
?
S-adenosyl-L-methionine + H2O
adenosine + L-methionine + H+
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + H2O
adenosine + L-methionine + H+
show the reaction diagram
the enzyme is most active at pH 8.5, so perhaps it has a regulatory role in influencing the cellular pH in the host organism. Many, but not all of the duf-62 containing organisms are extremophiles
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-homocysteine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0392
S-adenosyl-L-methionine
pH 8.5, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.14
S-adenosyl-L-methionine
pH 8.5, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0036
S-adenosyl-L-homocysteine
pH 8.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
the enzyme is inactive below pH 5 and above pH 10
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, sitting-drop vapour diffusion technique
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
the enzyme retains full activity after being heated at 80°C for 30 min and then cooled to 37°C
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
Deng, H.; Botting, C.H.; Hamilton, J.T.; Russell, R.J.; O'Hagan, D.
S-adenosyl-L-methionine:hydroxide adenosyltransferase: a SAM enzyme
Angew. Chem. Int. Ed. Engl.
47
5357-5361
2008
Pyrococcus horikoshii (O58212), Pyrococcus horikoshii OT-3 (O58212)
Manually annotated by BRENDA team
Deng, H.; McMahon, S.A.; Eustaquio, A.S.; Moore, B.S.; Naismith, J.H.; O'Hagan, D.
Mechanistic insights into water activation in SAM hydroxide adenosyltransferase (duf-62)
Chembiochem
10
2455-2459
2009
Salinispora arenicola, Pyrococcus horikoshii (O58212)
Manually annotated by BRENDA team
Deng, H.; O'Hagan, D.
The fluorinase, the chlorinase and the duf-62 enzymes
Curr. Opin. Chem. Biol.
12
582-592
2008
Pyrococcus horikoshii (O58212)
Manually annotated by BRENDA team