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Information on EC 3.13.1.9 - S-inosyl-L-homocysteine hydrolase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58783

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IUBMB Comments
The enzyme, characterized from the methanogenic archaeon Methanocaldococcus jannaschii, binds an NAD+ cofactor. It participates in an alternative pathway for the regeneration of S-adenosyl-L-methionine from S-adenosyl-L-homocysteine that involves the deamination of the latter to S-inosyl-L-homocysteine.
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Methanocaldococcus jannaschii
UNIPROT: Q58783
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The enzyme appears in selected viruses and cellular organisms
Synonyms
s-inosyl-l-homocysteine hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SIHH
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-inosyl-L-homocysteine hydrolase (inosine-forming)
The enzyme, characterized from the methanogenic archaeon Methanocaldococcus jannaschii, binds an NAD+ cofactor. It participates in an alternative pathway for the regeneration of S-adenosyl-L-methionine from S-adenosyl-L-homocysteine that involves the deamination of the latter to S-inosyl-L-homocysteine.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
inosine + L-homocysteine
S-inosyl-L-homocysteine + H2O
show the reaction diagram
the enzyme shows a slight preference for L-homocysteine in the synthesis direction
-
-
r
S-inosyl-L-homocysteine + H2O
inosine + L-homocysteine
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-inosyl-L-homocysteine + H2O
inosine + L-homocysteine
show the reaction diagram
the enzyme participates in an alternative pathway for the regeneration of S-adenosyl-L-methionine from S-adenosyl-L-homocysteine that involves the deamination of the latter to S-inosyl-L-homocysteine
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
the enzyme binds an NAD+ cofactor. Apo-enzyme has no activity without the addition of NAD+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.64
Inosine
pH 7.0, 70°C
0.0054
L-homocysteine
pH 7.0, 70°C
0.22
S-Inosyl-L-homocysteine
pH 7.0, 70°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.83
Inosine
pH 7.0, 70°C
0.83
L-homocysteine
pH 7.0, 70°C
0.42
S-Inosyl-L-homocysteine
pH 7.0, 70°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3
Inosine
pH 7.0, 70°C
152
L-homocysteine
pH 7.0, 70°C
1.9
S-Inosyl-L-homocysteine
pH 7.0, 70°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
Inosine
pH 7.0, 70°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
the enzyme shows maximal activity at pH 7.0 to 7.5 and pH 9.6
9.6
the enzyme shows maximal activity at pH 7.0 to 7.5 and pH 9.6
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 11
no measurable activity at either pH 6.5 or pH 11 and shows maximal activity at pH 7.0 to 7.5 and pH 9.6. pH 11: about 70% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme participates in an alternative pathway for the regeneration of S-adenosyl-L-methionine from S-adenosyl-L-homocysteine that involves the deamination of the latter to S-inosyl-L-homocysteine
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 49000, SDS-PAGE, the ratio of the tetramer form to the dimer form is 4:1
tetramer
4 * 49000, SDS-PAGE, the ratio of the tetramer form to the dimer form is 4:1
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
the enzyme remains soluble up to 80°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
Miller, D.; Xu, H.; White, R.H.
S-inosyl-L-homocysteine hydrolase, a novel enzyme involved in S-adenosyl-L-methionine recycling
J. Bacteriol.
197
2284-2291
2015
Methanocaldococcus jannaschii (Q58783), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii ATCC 43067 (Q58783)
Manually annotated by BRENDA team