Information on EC 3.2.2.9 - adenosylhomocysteine nucleosidase

Word Map on EC 3.2.2.9
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.2.2.9
-
RECOMMENDED NAME
GeneOntology No.
adenosylhomocysteine nucleosidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-homocysteine + H2O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of N-glycosyl bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
autoinducer AI-2 biosynthesis I
-
-
autoinducer AI-2 biosynthesis II (Vibrio)
-
-
Cysteine and methionine metabolism
-
-
L-cysteine biosynthesis VI (from L-methionine)
-
-
Metabolic pathways
-
-
S-adenosyl-L-methionine cycle I
-
-
methionine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-homocysteine homocysteinylribohydrolase
Also acts on S-methyl-5'-thioadenosine to give adenine and S-methyl-5-thioribose (cf. EC 3.2.2.16, methylthioadenosine nucleosidase).
CAS REGISTRY NUMBER
COMMENTARY hide
9055-10-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
var. cereus
-
-
Manually annotated by BRENDA team
strain B31
-
-
Manually annotated by BRENDA team
strain W-ATCC 963
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
rat
-
-
Manually annotated by BRENDA team
tomato, cv. Lukullus
-
-
Manually annotated by BRENDA team
bifunctional 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
-
-
Manually annotated by BRENDA team
strain N16961
-
-
Manually annotated by BRENDA team
strain N16961
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
single MTN1 or MTN2 knock down mutants do not display an obvious morphological phenotype when grown on sulfur sufficient media or on soil, mtn1-1/mtn2-1 double mutant plants display delayed flowering, produce underdeveloped siliques, and are sterile
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-deoxy-2'-fluoro-5'-deoxy-5'-(methylthio)adenosine + H2O
adenine + ?
show the reaction diagram
-
F-MeSAdo, slow substrate
-
-
?
2'-deoxymethylthioadenosine + H2O
adenine + 2-deoxymethylthioribose
show the reaction diagram
-
fairly good substrate
-
-
?
5'-butylthioadenosine + H2O
adenine + 5-butylthio-D-ribose
show the reaction diagram
24% activity compared to 5'-methylthioadenosine
-
-
?
5'-chloroadenosine + H2O
adenine + 5-chloro-D-ribose
show the reaction diagram
13% activity compared to 5'-methylthioadenosine
-
-
?
5'-deoxyadenosine + H2O
5-deoxy-D-ribose + adenine
show the reaction diagram
5'-ethylthioadenosine + H2O
adenine + 5-ethylthio-D-ribose
show the reaction diagram
5'-iodoadenosine + H2O
adenine + 5-iodo-D-ribose
show the reaction diagram
17% activity compared to 5'-methylthioadenosine
-
-
?
5'-isobutylthioadenosine + H2O
adenine + 5-isobutylthio-D-ribose
show the reaction diagram
32% activity compared to 5'-methylthioadenosine
-
-
?
5'-isobutylthioadenosine + H2O
adenine + 5-isobutylthioribose
show the reaction diagram
-
rate of 5'-methylthioadenosine hydrolysis taken as 100%, relative activity 52%
-
-
?
5'-methylthioadenosine + H2O
5-methylthio-D-ribose + adenine
show the reaction diagram
5'-methylthioadenosine + H2O
?
show the reaction diagram
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
show the reaction diagram
5'-n-propylthioadenosine + H2O
adenine + 5-n-propylthioribose
show the reaction diagram
-
rate of 5'-methylthioadenosine hydrolysis taken as 100%, relative activity 106%
-
-
?
5'-phenylthioadenosine + H2O
adenine + 5-phenylthio-D-ribose
show the reaction diagram
39% activity compared to 5'-methylthioadenosine
-
-
?
6-amino-6-deoxyfutalosine + H2O
dehypoxanthine futalosine + adenine
show the reaction diagram
adenosine + H2O
adenine + D-ribose
show the reaction diagram
6% activity compared to 5'-methylthioadenosine
-
-
?
S-2-aza-adenosylhomocysteine + H2O
2-azaadenine + 5-(S-L-homocysteinyl)ribose
show the reaction diagram
-
rate of 5'-methylthioadenosine hydrolysis taken as 100%, relative activity 27%
-
-
?
S-adenosyl-D-homocysteine + H2O
adenine + 5-(S-D-homocysteinyl)ribose
show the reaction diagram
-
rate of 5'-methylthioadenosine hydrolysis taken as 100%, relative activity 26%
-
-
?
S-adenosyl-L-homocysteine + H2O
?
show the reaction diagram
S-adenosyl-L-homocysteine + H2O
adenine + 5-ribosyl-L-homocysteine
show the reaction diagram
S-adenosyl-L-homocysteine + H2O
adenine + S-ribosyl-L-homocysteine
show the reaction diagram
S-adenosyl-L-homocysteine + H2O
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
show the reaction diagram
S-adenosylhomocysteine + ?
?
show the reaction diagram
S-adenosylmethionine + H2O
adenine + hypoxanthine + methylthioribose + homoserine lactone
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
5'-deoxyadenosine + H2O
5-deoxy-D-ribose + adenine
show the reaction diagram
5'-methylthioadenosine + H2O
5-methylthio-D-ribose + adenine
show the reaction diagram
5'-methylthioadenosine + H2O
?
show the reaction diagram
S-adenosyl-L-homocysteine + H2O
?
show the reaction diagram
S-adenosyl-L-homocysteine + H2O
adenine + 5-ribosyl-L-homocysteine
show the reaction diagram
S-adenosyl-L-homocysteine + H2O
S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine
show the reaction diagram
additional information
?
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(+/-)-cis-1-[(9-deazaadenin-9-yl)methyl]-4-ethyl-3-hydroxypyrrolidine
-
-
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(1H-1,2,3-triazol-4-yl)pyrrolidine
-
-
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(penta-3-yl)pyrrolidine
-
-
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-isobutylpyrrolidine
-
-
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-phenylpyrrolidine
-
-
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-vinylpyrrolidine
-
-
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-4-ethynyl-3-hydroxypyrrolidine
-
-
(+/-)-trans-4-(1-benzyl-1H-1,2,3-triazol-4-yl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
(+/-)-trans-4-(cyclohexylmethyl)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
(+/-)-trans-4-allyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
(+/-)-trans-4-butyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
(+/-)-trans-4-cyclopentyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
(+/-)-trans-4-cyclopropyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
(+/-)-trans-4-[3-(benzylthio)propyl]-1-[(9-deazaadenin-9-yl)-methyl]-3-hydroxypyrrolidine
-
-
(+/-)trans-1-[(9-deazaadenin-9-yl)methyl]-4-ethyl-3-hydroxypyrrolidine
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-(3-methylphenylthio)-D-ribitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-(4-methylphenylthio)-D-ribitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-methylthio-D-ribitol
(1S)-5-(4-chlorophenylthio)-1-(9-deaza-adenin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol
-
-
(2R)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-(methylsulfanyl)propan-1-ol
(2R)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-[(hydroxymethyl)sulfanyl]propan-1-ol
-
-
(2R,3R)-2-([[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl](methyl)amino]methyl)-4-(methylsulfanyl)butane-1,3-diol
(2R,3R)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
(2R,3S)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
(2R,3S)-4-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl](methyl)amino]-3-[(methylsulfanyl)methyl]butane-1,2-diol
(2S)-1-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-(methylsulfanyl)propan-2-ol
(2S)-2-[[(1S)-1-(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)-2-hydroxyethyl]amino]-3-(methylsulfanyl)propan-1-ol
(2S)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-[(hydroxymethyl)sulfanyl]propan-1-ol
-
-
(2S,3R)-1-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl](methyl)amino]-4-(methylsulfanyl)butane-2,3-diol
(2S,3R)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
(2S,3R)-N-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-3,4-dihydroxy-2-[(methylsulfanyl)methyl]butan-1-aminium trifluoroacetate
(2S,3S)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(methylthiomethyl)pyrrolidine
-
-
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-4-ethyl-3-hydroxypyrrolidine
-
-
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]3-hydroxy-4-methylthiomethylpyrrolidine
(3R,4S)-4-(1-butylthiomethyl)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
(3R,4S)-4-(4-chlorophenyl-thiomethyl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
potential antibiotic to interfere with the metabolic pathways involved in methylation, polyamine biosynthesis, methionine recycling, and quorum sensing pathways
(3R,4S)-4-(benzylthiomethyl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
(3R,4S)-4-butyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
(3R,4S)-butylthio-5'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin
-
-
(3R,4S)-ethylthio-5'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin
-
-
(3R,4S)-methylthio-5'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin
-
-
(5'R)-cycloMethylthioadenosine
-
competitive inhibition
-
(p-bromophenyl)thioadenosine
-
-
(p-fluorophenyl)thioadenosine
-
-
2',3'-didehydromethylthioadenosine
-
competitive inhibition
2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-2-[(methylsulfanyl)methyl]propane-1,3-diol
2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-(methylsulfanyl)propan-1-ol
3'-deoxy-methylthioadenosine
-
competitive inhibition
4-chlorophenylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
5'-(4-aminophenyl)thioadenosine
-
-
5'-(4-bromophenyl)thioadenosine
-
moderate inhibitor
5'-(4-chlorophenyl)thioadenosine
-
-
5'-(4-fluorophenyl)thioadenosine
-
moderate inhibitor
5'-(4-iodophenyl)thioadenosine
-
-
5'-(4-nitrophenyl)thioadenosine
-
most potent inhibitor
5'-(p-nitrophenyl)thioadenosine
-
most potent inhibitor
5'-butylthio-DADMe-ImmucillinA
-
potent MTAN inhibitor, disrupting autoinducer production in a dose-dependent manner without affecting growth. Despite having a 3fold lower affinity with purified MTAN, 5'-butylthio-DADMe-ImmucillinA inhibits cellular MTAN activity 5fold better than its methylthio- and ethylthio-counterparts, significant diffusion barrier
5'-butylthioadenosine
-
-
5'-Chloroadenosine
-
-
5'-Chloroformycin
5'-dimethylthioadenosine
-
-
5'-ethylthio-DADMe-ImmucillinA
-
potent MTAN inhibitor, disrupting autoinducer production in a dose-dependent manner without affecting growth
5'-ethylthioadenosine
5'-isobutylthio-3-deaza-adenosine
-
poor inhibitor
5'-isobutylthioadenosine
-
-
5'-Isobutylthioinosine
-
-
5'-Isopropylthioadenosine
-
-
5'-Methylselenoadenosine
-
-
5'-methylthio-3-deaza-adenosine
-
poor inhibitor
5'-methylthio-DADMe-ImmucillinA
-
potent MTAN inhibitor, disrupting autoinducer production in a dose-dependent manner without affecting growth
5'-methylthioadenosine
-
-
5'-Methylthioformycin
5'-methylthioinosine
-
-
5'-methylthiotubercidin
5'-n-butylthioinosine
-
-
5'-n-Propylthioadenosine
-
competitive inhibition
5'-p-aminophenylthioadenosine
-
Pfs protein shows 45% relative activity in the presence of 0.1 mM 5'-p-aminophenylthioadenosine, Bgp protein shows 20% relative activity in the presence of 0.1 mM 5'-p-aminophenylthioadenosine
5'-p-nitrophenylthioadenosine
-
-
5'-p-nitrophenythioadenosine
-
Pfs protein shows 0.6% relative activity in the presence of 0.1 mM 5'-p-aminophenylthioadenosine, Bgp protein shows 5% relative activity in the presence of 0.1 mM 5'-p-aminophenylthioadenosine
5'-phenylthioadenosine
-
; moderate inhibitor
5'-propylthioadenosine
-
-
5'-purinothioadenosine
-
-
adenine
adenosine
-
-
benzylthio-immucillin A
-
-
butylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
-
picomolar inhibitor of MTAN
carbocyclic 5'-methylthioadenosine
-
-
ethylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
-
picomolar inhibitor of MTAN
ethylthio-immucillin A
-
-
ethylthio-immucillin-A
Formycin A
methylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
methylthio-DADMe-immucillin-A
-
i.e. (3R,4S)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(methylsulfanyl)methyl]pyrrolidin-3-ol
methylthio-immucillin A
-
-
methylthio-immucillin-A
p-chlorophenylthio-immucillin A
-
-
p-tolylthio-immucillin-A
phenylthio-immucillin-A
S-8-aza-adenosyl-L-homocysteine
-
powerful inhibitor
S-8-aza-adenosylhomocysteine
-
-
S-adenosyl-L-homocysteine
-
; moderate inhibitor
S-adenosyl-L-homocysteine sulfoxide
-
poor inhibitor
S-adenosylhomocysteine
-
competitive inhibition
S-Formycinylhomocysteine
-
S-N6-dimethyl-3-deaza-adenosyl-L-homocysteine
-
poor inhibitor
S-Tubercidinylhomocysteine
-
; powerful inhibitor
sinefungin
-
poor inhibitor
Tris
weak inhibitor; weak inhibitor, about 20% residual activity at 250 mM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5'-methylthioadenosine
-
enzyme activity is induced by 5'-methylthioadenosine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00031 - 5.4
5'-methylthioadenosine
0.00103
6-amino-6-deoxyfutalosine
in 50 mM potassium phosphate buffer, pH 7.0, at 25°C
0.001 - 1.3
S-adenosyl-L-homocysteine
0.0043 - 9
S-adenosylhomocysteine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13 - 10.2
5'-methylthioadenosine
0.53
6-amino-6-deoxyfutalosine
Campylobacter jejuni
Q0PC20
in 50 mM potassium phosphate buffer, pH 7.0, at 25°C
0.00021 - 9.1
S-adenosyl-L-homocysteine
0.5
S-adenosylhomocysteine
Vibrio cholerae
-
at 25°C, in 100 mM HEPES buffer, pH 7.5, 50 mM KCl
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
660
5'-methylthioadenosine
Vibrio cholerae
-
at 25°C, in 100 mM HEPES buffer, pH 7.5, 50 mM KCl
400
1.6 - 1800
S-adenosyl-L-homocysteine
36
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0018
(+/-)-cis-1-[(9-deazaadenin-9-yl)methyl]-4-ethyl-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.002
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(1H-1,2,3-triazol-4-yl)pyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.0007
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(penta-3-yl)pyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000047
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-isobutylpyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.00003
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-phenylpyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.00065
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-vinylpyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.00039
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-4-ethynyl-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000064
(+/-)-trans-4-(1-benzyl-1H-1,2,3-triazol-4-yl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000059
(+/-)-trans-4-(cyclohexylmethyl)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.00035
(+/-)-trans-4-allyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000009
(+/-)-trans-4-butyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000013
(+/-)-trans-4-cyclopentyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000063
(+/-)-trans-4-cyclopropyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000054
(+/-)-trans-4-[3-(benzylthio)propyl]-1-[(9-deazaadenin-9-yl)-methyl]-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.00084
(+/-)trans-1-[(9-deazaadenin-9-yl)methyl]-4-ethyl-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000000009 - 0.000000015
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-(3-methylphenylthio)-D-ribitol
0.000000008 - 0.000000018
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-(4-methylphenylthio)-D-ribitol
0.00000008 - 0.00000036
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-methylthio-D-ribitol
0.000000002 - 0.000000006
(1S)-5-(4-chlorophenylthio)-1-(9-deaza-adenin-9-yl)-1,4-dideoxy-1,4-imino-D-ribitol
0.0000008 - 0.0000017
(2R)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-(methylsulfanyl)propan-1-ol
0.00000023
(2R)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-[(hydroxymethyl)sulfanyl]propan-1-ol
-
pH and temperature not specified in the publication
0.000132 - 0.000401
(2R,3R)-2-([[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl](methyl)amino]methyl)-4-(methylsulfanyl)butane-1,3-diol
0.00001
(2R,3R)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
0.0000008 - 0.0000009
(2R,3S)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
0.000061 - 0.0023
(2R,3S)-4-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl](methyl)amino]-3-[(methylsulfanyl)methyl]butane-1,2-diol
0.000036 - 0.00004
(2S)-1-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-(methylsulfanyl)propan-2-ol
0.000047 - 0.00172
(2S)-2-[[(1S)-1-(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)-2-hydroxyethyl]amino]-3-(methylsulfanyl)propan-1-ol
0.0000011
(2S)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-[(hydroxymethyl)sulfanyl]propan-1-ol
-
pH and temperature not specified in the publication
0.000085 - 0.000202
(2S,3R)-1-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl](methyl)amino]-4-(methylsulfanyl)butane-2,3-diol
0.0000039 - 0.000006
(2S,3R)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
0.000005 - 0.000009
(2S,3R)-N-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-3,4-dihydroxy-2-[(methylsulfanyl)methyl]butan-1-aminium trifluoroacetate
0.0000018 - 0.0000021
(2S,3S)-2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
0.000000002 - 0.000000048
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(methylthiomethyl)pyrrolidine
0.00031
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-4-ethyl-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000000002 - 0.00000014
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]3-hydroxy-4-methylthiomethylpyrrolidine
0.0000000003
(3R,4S)-4-(1-butylthiomethyl)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyrrolidine
-
pH and temperature not specified in the publication
0.000000000047 - 0.000000026
(3R,4S)-4-(4-chlorophenyl-thiomethyl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
0.00000000046 - 0.0000034
(3R,4S)-4-(benzylthiomethyl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
0.0000034
(3R,4S)-4-butyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
in 100 mM HEPES, pH 7.4, 50 mM KCl, at 25°C
0.000004 - 0.0000058
2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-2-[(methylsulfanyl)methyl]propane-1,3-diol
0.00000036 - 0.0000012
2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-(methylsulfanyl)propan-1-ol
0.00000036
4-chlorophenylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
0.00017
5'-(4-iodophenyl)thioadenosine
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.00002
5'-(4-nitrophenyl)thioadenosine
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.000000208
5'-butylthio-DADMe-ImmucillinA
-
in 50 mM phosphate buffer, pH 7.9, 10 mM KCl, at 25°C
0.000322
5'-Chloroformycin
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.00000007
5'-ethylthio-DADMe-ImmucillinA
-
in 50 mM phosphate buffer, pH 7.9, 10 mM KCl, at 25°C
0.000000073
5'-methylthio-DADMe-ImmucillinA
-
in 50 mM phosphate buffer, pH 7.9, 10 mM KCl, at 25°C
0.000027
5'-Methylthioformycin
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.00075 - 0.0041
5'-methylthiotubercidin
0.000077 - 0.000116
5'-p-aminophenylthioadenosine
0.000587 - 0.000698
5'-p-nitrophenylthioadenosine
0.3
adenine
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.000000208
butylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
-
at 25°C, in 50 mM phosphate buffer, pH 7.9, and 10 mM KCl
0.00000007
ethylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
-
at 25°C, in 50 mM phosphate buffer, pH 7.9, and 10 mM KCl
0.00004
ethylthio-immucillin-A
0.00105 - 0.01
Formycin A
0.000000073 - 0.000024
methylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
0.001
methylthio-immucillin-A
0.00006
p-tolylthio-immucillin-A
0.000335
phenylthio-immucillin-A
0.000928
S-8-aza-adenosyl-L-homocysteine
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.0024
S-adenosyl-L-homocysteine
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.0000097
S-Formycinylhomocysteine
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
-
0.0019
S-Tubercidinylhomocysteine
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
25.24
Tris
at 37°C, pH 7.5
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00037
5'-(4-aminophenyl)thioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.00085
5'-(4-bromophenyl)thioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.0002
5'-(4-chlorophenyl)thioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.0009
5'-(4-fluorophenyl)thioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.00022
5'-(4-iodophenyl)thioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.00013
5'-(4-nitrophenyl)thioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.000006
5'-butylthio-DADMe-ImmucillinA
Vibrio cholerae
-
in 50 mM phosphate buffer, pH 7.9, 10 mM KCl, at 25°C
0.00068
5'-butylthioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.0098
5'-Chloroadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.0004
5'-Chloroformycin
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.0068
5'-dimethylthioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.000031
5'-ethylthio-DADMe-ImmucillinA
Vibrio cholerae
-
in 50 mM phosphate buffer, pH 7.9, 10 mM KCl, at 25°C
0.0009
5'-ethylthioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.013
5'-isobutylthio-3-deaza-adenosine
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.00074
5'-isobutylthioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.132
5'-Isobutylthioinosine
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.0011
5'-Isopropylthioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.0045
5'-Methylselenoadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.079
5'-methylthio-3-deaza-adenosine
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.000027
5'-methylthio-DADMe-ImmucillinA
Vibrio cholerae
-
in 50 mM phosphate buffer, pH 7.9, 10 mM KCl, at 25°C
0.001
5'-methylthioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.00006
5'-Methylthioformycin
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.03
5'-methylthioinosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.0033 - 0.0077
5'-methylthiotubercidin
0.094
5'-n-butylthioinosine
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.00088
5'-phenylthioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.00058
5'-propylthioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.0047
5'-purinothioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.216 - 0.305
adenine
0.000006
butylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
Vibrio cholerae
-
at 25°C, in 50 mM phosphate buffer, pH 7.9, and 10 mM KCl
0.027
carbocyclic 5'-methylthioadenosine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.000031
ethylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
Vibrio cholerae
-
at 25°C, in 50 mM phosphate buffer, pH 7.9, and 10 mM KCl
0.057
Formycin A
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.000027
methylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
Vibrio cholerae
-
at 25°C, in 50 mM phosphate buffer, pH 7.9, and 10 mM KCl
0.0018
S-8-aza-adenosyl-L-homocysteine
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.002 - 4
S-adenosyl-L-homocysteine
Escherichia coli
-
in 50 mM potassium phosphate (pH 7.0), at 37°C
0.069
S-adenosyl-L-homocysteine sulfoxide
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.00002
S-Formycinylhomocysteine
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
-
0.02
S-N6-dimethyl-3-deaza-adenosyl-L-homocysteine
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.0032
S-Tubercidinylhomocysteine
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.024
sinefungin
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0152
-
crude extract, with S-adenosyl-L-homocysteine as substrate, in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.9
using S-adenosyl-L-homocysteine as substrate, at pH 6.0 and 22°C
3.1
-
Bgp protein, using S-adenosyl-L-homocysteine as substrate, pH 5.0
3.7
-
Pfs protein, using S-adenosyl-L-homocysteine as substrate, pH 5.0
3.75
-
substrate S-adenosyl-L-homocysteine
156
-
after 9810fold purification, with S-adenosyl-L-homocysteine as substrate, in 50 mM potassium phosphate buffer, pH 7.0, at 37°C; substrate S-adenosyl-L-homocysteine
373
-
substrate 5'-methylthioadenosine
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7
6.5
-
optimal pH for both natural substrates, 5'-methylthioadenosine and S-adenosyl-L-homocysteine, with little variation from pH 5.7-7.1
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 45
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
rapidly inactivated after exposure for 15 min
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Colwellia psychrerythraea (strain 34H / ATCC BAA-681)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli O139:H28 (strain E24377A / ETEC)
Francisella philomiragia subsp. philomiragia (strain ATCC 25017)
Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Vibrio fischeri (strain ATCC 700601 / ES114)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
-
estimation from pfs gene product
24350
-
estimation from pfs gene product
25000 - 31000
-
native MTA/SAH'ase
25000
-
x * 25000, His-tagged enzyme, calculated from amino acid sequence
26030
-
2 * 26030, calculated from amino acid sequence and acquired by nanoESI-QTOF mass spectrometry
26500
-
SDS-PAGE
27462
x * 27462, isoform MATN2, calculated from amino acid sequence
28000
-
x * 28000, SDS-PAGE
31000
-
gel filtration
34000
-
x * 34000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
-
1 * 26500, SDS-PAGE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 100 mM Bis-Tris (pH 6.5) and 26-32% (w/v) PEG MME 2000; isozyme AtMTAN2, X-ray diffraction structure determination and analysis at 2.9 A resolution, molecular replacement, modelling
isoform MTAN1 in complex with S-adenosyl-L-homocysteine, hanging drop vapor diffusion method, using 0.2 M NH4Cl, 18% (w/v) PEG3350, 15% (v/v) ethylene glycol; isozyme AtMTAN1 in complex with S-adenosyl-L-homocysteine, mixing of 0.004 ml of 10 mg/ml protein with 0.002 ml of precipitant solution containing 0.2 M NH4Cl, 18% w/v PEG 3350, 15% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 2.2 A resolution
in complex with adenine, hanging drop vapor diffusion method, using 20% (w/v) PEG 1000, 0.1 M phosphate–citrate (pH 4.2) and 0.2 M Li2SO4
-
enzyme in complex with transition state analogue methylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A. Enzyme forms a dimer with the methylthio group in a flexible hydrophobic pocket
-
hanging-drop vapor diffusion method. Three structures along the reaction coordinate of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase are solved: Asp197Asn 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/5'-methylthioadenosine complex, Glu12Gln 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/5-methylthioribose/adenine complex, and wild-type 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase/glycerol complex. These structures provide insight into the conformational flexibility of the enzyme and nucleoside during catalysis
-
in complex with the transition-state analogue formycin A, hanging drop vapour diffusion method, using 50 mM potassium phosphate with 20% (w/v) PEG 8000
in complex with transition state analog formycin A and with substrate analog 5’-methylthiotubercidin
-
enzyme alone, in complex with formycin A and in complex with adenine, hanging drop vapor diffusion method, using 0.1 M Tris pH 8.5 and 16% (w/v) polyethyleneglycol 8000, at 18°C; enzyme only or in complex with formycin A or adenine, hanging drop vapor diffusion method, using 0.1 M Tris pH 8.5 and 16% (w/v) polyethyleneglycol 8000, at 18°C
hanging drop vapor diffusion method. Inactive D198N mutant bound to S-adenosyl-L-homocysteine and active enzyme bound to S-(5-deoxy-D-ribos-5-yl)-L-homocysteine and adenine using 0.05 M magnesium chloride hexahydrate, 0.1 M HEPES (pH 7.5), and 30% (v/v) PEG-MME 550
-
in complex with the transition-state analogue formycin A, hanging drop vapour diffusion method, using 50 mM potassium phosphate with 20% (w/v) PEG 8000
enzyme in complex with transition state analogue methylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A. Enzyme forms a dimer with the methylthio group in a flexible hydrophobic pocket
-
5'-butylthio-DADMe-immucillinA-MTAN complex, by sitting drop vapor diffusion, at 18°C, to 2.3 A resolution. Structure of the MTAN monomer is a single mixed alpha/beta domain with central twisted nine-stranded mixed beta-sheet surrounded by six alpha-helices. Catalytic site is situated in a pocket formed by residues from beta10, a loop between beta8 and alpha4 and a loop contributed by the adjacent subunit. The catalytic site consists of the base binding site, the ribose binding site and the 5'-alkylthio-binding site; in complex with But-dadme-imma A, sitting drop vapour diffusion method, with 0.2 M potassium iodide and 20% (w/v) PEG3350
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 55
-
significant substrate conversion is seen even at 4°C. Activity is also seen at higher temperatures than 45°C, however the enzyme is rapidly inactivated (about 90%) after incubation at 55°C for 10 min
55
-
enzyme rapidly inactivated after 10 min at 55°C
60
-
rapidly inactivated after exposure for 15 min; the enzyme is rapidly inactivated after exposure for 15 min at 60°C
66
-
Tm-value for mutant enzyme S196A and F105A
67
-
Tm-value for mutant enzymeV102A and Y107F
68
-
Tm-value for wild-type enzyme and mutant enzyme F151A
70
-
Tm-value for mutant enzymeS76A
71
-
Tm-value for mutant enzyme M173A and M9A
72
-
Tm-value for mutant enzyme R193A and F207A
74
the melting temperature is 74°C
75
-
Tm-value for mutant enzyme I50A
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
unstable in solution of low ionic strength
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°, repeatedly frozen and thawed without loss of activity over a 9 months period, upon storage at 4°C only 50% of activity retained after 3 weeks
-
-20°C, 50 mM potassium phosphate buffer (pH 7.0), at least 2 months, no significant loss of activity
-
0°C, 0.1 M phosphate buffer containing 0.009 M 2-mercaptoethanol and 0.0005 M EDTA stable for 2 weeks, retains 80% of its total activity after 2 weeks at -40°C
-
0°C, loses 50% activity in 48 h, -20°C very unstable, lost nearly all activity when stored for 1 week
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
30-fold
-
9800-fold; ammonium sulfate precipitation, DEAE-Sephadex gel filtration, hydroxyapatite column chromatography, S-formycinylhomocysteine-Sepharose column chromatography, and Sephacryl S-200 gel filtration
-
glutathione column chromatography, HiTrap Q Sepharose column chromatography, and Superose 12 gel filtration; recombinant isozyme AtMTAN2 from Escherichia coli to homogeneity
HisTrap column chromatography and Superdex 200 gel filtration
-
HisTrap column chromatography and Superdex 200 gel filtration; HisTrap column chromatography and Superdex 200 gel filtration
Ni-NTA affinity column chromatography and gel filtration; recombinant His-tagged wild-type and mutant isozymes AtMTAN1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
Ni-NTA agarose column chromatography
Ni-NTA column chromatography
-
Ni-NTA column chromatography and Superdex 200 gel filtration
-
Ni-NTA Superflow resin column chromatography and Superdex-200 gel filtration
Ni-Sepharose column chromatography
nickel affinity column chromatography and Superdex 200 gel filtration
-
recombinant wild-type and mutant His-tagged MTAN from strain BL21(DE3) by nickel affinity chromatography
-
rMTAN, recombinant MTA/SAH nucleosidase
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged recombinant protein; expressed in Escherichia coli as His-tagged protein
-
expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21 Codon + cells; isozyme AtMTAN1, overexpression of wild-type and mutant His-tagged enzymes in Escherichia coli strain BL21(DE3)
expressed in Escherichia coli BL21 Codon+ cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) RIL cells; isozyme AtMTAN2, DNA and amino acid sequence determination and analysis, overexpression of isozyme AtMTAN2 in Escherichia coli
expressed in Escherichia coli BL21(DE3) Rosetta cells
-
expressed in Escherichia coli DH5alpha cells
-
expressed in Escherichia coli Top10F' cells; gene encoding the enzyme cloned and recombinant MTA/SAH nucleosidase rMTAN expressed
-
expression in Escherichia coli
expression with His-tag
-
overexpression of wild-type and mutant His-tagged enzyme in strain BL21(DE3)
-
pfs gene cloned and expressed in pCRII using PCR, subcloned into pAL781
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E202Q
inactive; site-directed mutagenesis, structure comparison with the wild-type enzyme
D168A
-
completely inactive
D168N
-
completely inactive
E145Q
-
completely inactive
E18A
-
completely inactive
E18Q
-
completely inactive
M144A
-
the mutant shows 0.1% catalytic efficiency compared to the wild type enzyme
R164A
-
the mutant shows 19.4% catalytic efficiency compared to the wild type enzyme
R85A
-
the mutant shows 7.6% catalytic efficiency compared to the wild type enzyme
R85H
-
the mutant shows 8.1% catalytic efficiency compared to the wild type enzyme
S167A
-
the mutant shows 5.6% catalytic efficiency compared to the wild type enzyme
Y134A
-
the mutant shows 0.6% catalytic efficiency compared to the wild type enzyme
Y134F
-
the mutant shows 0.4% catalytic efficiency compared to the wild type enzyme
D197A
-
enzyme is inactive with 5'-methylthioadenosine and S-adenosyl-L-homocysteine
D197N
-
enzyme is inactive with 5'-methylthioadenosine and S-adenosyl-L-homocysteine
E12A
-
enzyme is inactive with 5'-methylthioadenosine and S-adenosyl-L-homocysteine
E12Q
-
enzyme is inactive with 5'-methylthioadenosine and S-adenosyl-L-homocysteine
E174A
-
enzyme is inactive with 5'-methylthioadenosine and S-adenosyl-L-homocysteine
F105A
-
kcat/Km for 5'-methylthioadenosine is 87.4% of wild-type value, kcat/Km for S-adenosyl-L-homocysteine is 128% of wild-type value
F151A
-
kcat/Km for 5'-methylthioadenosine is 0.5% of wild-type value kcat/Km for S-adenosyl-L-homocysteine is 0.2% of wild-type value
F207A
-
kcat/Km for 5'-methylthioadenosine is 2.2% of wild-type value, kcat/Km for S-adenosyl-L-homocysteine is 2.7% of wild-type value
I50A
-
kcat/Km for 5'-methylthioadenosine is 11.8% of wild-type value, kcat/Km for S-adenosyl-L-homocysteine is 23.3% of wild-type value
M173A
-
kcat/Km for 5'-methylthioadenosine is 0.6% of wild-type value, kcat/Km for S-adenosyl-L-homocysteine is 0.1% of wild-type value
M9A
-
kcat/Km for 5'-methylthioadenosine is 12.6% of wild-type value, kcat/Km for S-adenosyl-L-homocysteine is 18.6% of wild-type value
R193A
-
kcat/Km for 5'-methylthioadenosine is 12.9% of wild-type value, kcat/Km for S-adenosyl-L-homocysteine is 28.1% of wild-type value
S196A
-
kcat/Km for 5'-methylthioadenosine is 2.3% of wild-type value kcat/Km for S-adenosyl-L-homocysteine is 4% of wild-type value
S76A
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kcat/Km for 5'-methylthioadenosine is 13.4% of wild-type value, kcat/Km for S-adenosyl-L-homocysteine is 22.9% of wild-type value
V102A
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kcat/Km for 5'-methylthioadenosine is 95% of wild-type value, kcat/Km for S-adenosyl-L-homocysteine is 233% of wild-type value
Y107F
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kcat/Km for 5'-methylthioadenosine is 32.2% of wild-type value, kcat/Km for S-adenosyl-L-homocysteine is 58.1% of wild-type value
E173Q
-
inactive
F104C/C186S
-
the mutations give an enzyme with steady-state kinetic properties similar to the native enzyme
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