Information on EC 3.2.2.16 - methylthioadenosine nucleosidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.2.2.16
-
RECOMMENDED NAME
GeneOntology No.
methylthioadenosine nucleosidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of N-glycosyl bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Cysteine and methionine metabolism
-
-
Metabolic pathways
-
-
S-methyl-5'-thioadenosine degradation I
-
-
S-methyl-5'-thioadenosine degradation IV
-
-
methionine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
S-methyl-5'-thioadenosine adeninehyrolase
Does not act on S-adenosylhomocysteine. cf. EC 3.2.2.9 adenosylhomocysteine nucleosidase.
CAS REGISTRY NUMBER
COMMENTARY hide
50812-28-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
unicellular uninuclear green alga
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
isolate B314 and strain N40
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
cucumber, Mill. cv Poinsett 76
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
human
-
-
Manually annotated by BRENDA team
Ochromonas malhamensis
protozoan, Pringsheim strain
-
-
Manually annotated by BRENDA team
expression is not regulated by ethylene, 5'-methylthioadenosine, or methionine
SwissProt
Manually annotated by BRENDA team
pea
-
-
Manually annotated by BRENDA team
strain N16961
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5'-(4-fluorosulfonylbenzoyl)adenosine + H2O
5-fluorosulfonylbenzoyl-D-ribose + adenine
show the reaction diagram
-
-
-
?
5'-adenosylcysteine + H2O
adenine + S-ribosylcysteine
show the reaction diagram
-
-
-
?
5'-butylthioadenosine + H2O
5-butylthio-D-ribose + adenine
show the reaction diagram
5'-butylthioadenosine + H2O
adenine + 5-butylthio-D-ribose
show the reaction diagram
-
25% activity compared to 5'-methylthioadenosine
-
-
?
5'-chloroadenosine + H2O
5-chloro-D-ribose + adenine
show the reaction diagram
-
-
-
-
?
5'-chloroadenosine + H2O
adenine + 5-chloro-D-ribose
show the reaction diagram
-
4% activity compared to 5'-methylthioadenosine
-
-
?
5'-deoxy-5'-(difluoromethylthio)adenosine + H2O
5-deoxy-5-(difluoromethylthio)-D-ribose + adenine
show the reaction diagram
-
DFMTA, fluorinated substrate analogue
-
-
?
5'-deoxy-5'-(monofluoromethylthio)adenosine + H2O
5-deoxy-5-(monofluoromethylthio)-D-ribose + adenine
show the reaction diagram
-
MFMTA , fluorinated analogue of MTA
-
-
?
5'-deoxy-5'-(trifluoromethylthio)adenosine + H2O
5-deoxy-5-(trifluoromethylthio)-D-ribose + adenine
show the reaction diagram
-
TFMTA, fluorinated substrate analogue
-
-
?
5'-deoxy-5'-isobutylthio-adenosine + H2O
5-isobutylthio-D-ribose + adenine
show the reaction diagram
-
1-butanol buffer/propan-2-ol buffer
-
-
?
5'-deoxy-5'-methylthioadenosine + H2O
5-methylthio-D-ribose + adenine
show the reaction diagram
5'-deoxy-5'-methylthioadenosine + H2O
?
show the reaction diagram
-
-
-
-
?
5'-deoxy-5'-propylthioadenosine + H2O
5-propylthio-D-ribose + adenine
show the reaction diagram
5'-deoxy-5'-S-adenosyl-L-cysteine + H2O
S-(5-deoxy-5-D-ribosyl)-L-cysteine + adenine
show the reaction diagram
-
relative activity 95.2%
-
-
?
5'-deoxy-5'-S-adenosyl-L-homocysteine + H2O
S-(5-deoxy-5-D-ribosyl)-L-homoscysteine + adenine
show the reaction diagram
-
substrate analogue, relative activity 95.8%
-
-
?
5'-deoxy-5'-thioethanoladenosine + H2O
?
show the reaction diagram
-
relative activity 98%
-
-
?
5'-deoxyadenosine + H2O
5-deoxy-D-ribose + adenine
show the reaction diagram
5'-ethylthio-2-aminoadenosine + H2O
5-ethylthio-D-ribose + 2-aminoadenosine
show the reaction diagram
-
1-butanol buffer/propan-2-ol buffer
-
-
?
5'-ethylthioadenosine + H2O
5-ethylthio-D-ribose + adenine
show the reaction diagram
5'-ethylthioadenosine + H2O
adenine + 5-ethylthio-D-ribose
show the reaction diagram
-
40% activity compared to 5'-methylthioadenosine
-
-
?
5'-ethylthioinosine + H2O
5-ethylthio-D-ribose + hypoxanthine
show the reaction diagram
-
1-butanol buffer
-
-
?
5'-iodoadenosine + H2O
adenine + 5-iodo-D-ribose
show the reaction diagram
-
28% activity compared to 5'-methylthioadenosine
-
-
?
5'-iodothioadenosine + H2O
5-iodothio-D-ribose + adenine
show the reaction diagram
5'-isobutylthio-3-deaza-adenosine + H2O
5-isobutylthio-D-ribose + 3-deazadenosine
show the reaction diagram
-
1-butanol buffer/propan-2-ol buffer
-
-
?
5'-isobutylthioadenosine + H2O
5-isobutylthioribose + adenine
show the reaction diagram
-
-
-
-
?
5'-isobutylthioadenosine + H2O
?
show the reaction diagram
-
52% activity compared to 5'-methylthioadenosine
-
-
?
5'-isobutylthioadenosine + H2O
adenine + 5-isobutylthio-D-ribose
show the reaction diagram
-
17% activity compared to 5'-methylthioadenosine
-
-
?
5'-isobutylthioinosine + H2O
5-isobutylthio-D-ribose + hypoxanthine
show the reaction diagram
-
1-butanol buffer
-
-
?
5'-isopropylthioadenosine + H2O
5-isopropylthio-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
5'-methylthioadenosine + H2O
adenine + S-methyl-5-thio-D-ribose
show the reaction diagram
5'-methylthioarabinosyladenine + H2O
5-methylthioarabinose + adenine
show the reaction diagram
-
1-butanol buffer/propan-2-ol buffer
-
-
?
5'-methylthioinosine + H2O
5-methylthio-D-ribose + hypoxanthine
show the reaction diagram
5'-n-butylthioadenosine + H2O
5-n-butylthio-D-ribose + adenine
show the reaction diagram
-
1-butanol buffer
-
-
?
5'-n-butylthioadenosine + H2O
?
show the reaction diagram
-
40% activity compared to 5'-methylthioadenosine
-
-
?
5'-n-butylthioinosine + H2O
5-n-butylthio-D-ribose + hypoxanthine
show the reaction diagram
-
1-butanol buffer
-
-
?
5'-phenylthioadenosine + H2O
5-phenylthio-D-ribose + adenine
show the reaction diagram
5'-phenylthioadenosine + H2O
adenine + 5-phenylthio-D-ribose
show the reaction diagram
-
12% activity compared to 5'-methylthioadenosine
-
-
?
5'-propylthioadenosine + H2O
5-propylthio-D-ribose + adenine
show the reaction diagram
-
-
-
?
6-amino-6-deoxyfutalosine + H2O
3-{3-[(2R,3S,4R,5R)-3,4,5-trihydroxytetrahydrofuran-2-yl]propanoyl}benzoic acid + 9H-purine-6-amine
show the reaction diagram
6-amino-6-deoxyfutalosine + H2O
adenine + dehypoxanthinyl futalosine
show the reaction diagram
adenosine + H2O
adenine + D-ribose
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-homocysteine + H2O
adenine + S-ribosyl-L-homocysteine
show the reaction diagram
S-adenosyl-L-homocysteine + H2O
S-D-ribosyl-L-homocysteine + adenine
show the reaction diagram
S-adenosyl-L-homocysteine + H2O
S-ribosyl-L-homocysteine + adenine
show the reaction diagram
S-adenosylhomocysteine + H2O
adenine + S-ribosylhomocysteine
show the reaction diagram
S-adenosylmercaptoethanol + H2O
?
show the reaction diagram
-
1-butanol buffer/propan-2-ol buffer
-
-
?
S-inosylmercaptoethanol + H2O
?
show the reaction diagram
-
propan-2-ol buffer
-
-
?
S-isobutyl-5'-thioadenosine + H2O
5-S-(2-methylpropyl)-5-thio-beta-D-ribofuranose + adenine
show the reaction diagram
-
-
-
?
S-methyl-5'-thioadenosine + H2O
adenine + S-methyl-5-thio-D-ribose
show the reaction diagram
S-methyl-5'-thioadenosine + H2O
S-methyl-5-thio-D-ribose + adenine
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'-deoxy-5'-methylthioadenosine + H2O
?
show the reaction diagram
-
-
-
-
?
5'-deoxyadenosine + H2O
5-deoxy-D-ribose + adenine
show the reaction diagram
5'-methylthioadenosine + H2O
5-methylthio-D-ribose + adenine
show the reaction diagram
-
-
-
-
ir
5'-methylthioadenosine + H2O
?
show the reaction diagram
5'-methylthioadenosine + H2O
adenine + S-methyl-5-thio-D-ribose
show the reaction diagram
6-amino-6-deoxyfutalosine + H2O
3-{3-[(2R,3S,4R,5R)-3,4,5-trihydroxytetrahydrofuran-2-yl]propanoyl}benzoic acid + 9H-purine-6-amine
show the reaction diagram
S-adenosyl-L-homocysteine + H2O
S-D-ribosyl-L-homocysteine + adenine
show the reaction diagram
S-adenosyl-L-homocysteine + H2O
S-ribosyl-L-homocysteine + adenine
show the reaction diagram
S-adenosylhomocysteine + H2O
adenine + S-ribosylhomocysteine
show the reaction diagram
-
-
-
-
?
S-methyl-5'-thioadenosine + H2O
adenine + S-methyl-5-thio-D-ribose
show the reaction diagram
S-methyl-5'-thioadenosine + H2O
S-methyl-5-thio-D-ribose + adenine
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
required for catalytic function; requires Co2+ for activity. Cobalt is bound to the nucleosidase with a stoichiometry of 1 equivalent of cobalt/subunit
Mg2+
-
enzyme activity depended upon, optimum concentration 50-120 mM
Mn2+
-
enzyme activity depended upon, optimum concentration 50-120 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R,2S)-2-(((4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl)amino)-1-(methylthio)propane-1,3-diol
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-methylthio-D-ribitol
(1S,2R)-2-(((4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl)amino)-1-(methylthio)propane-1,3-diol
(2R)-2-[[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-(methylsulfanyl)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-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
(2R,3S)-2-[[(4-amino-5,7a-dihydro-4aH-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,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-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
-
-
(2S,3R)-2-[[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol - methane (1:1)
-
-
(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-5,7a-dihydro-4aH-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-methylthiomethylpyrrolidine
(3R,4S)-1-[9-deazaadenin-(9-yl)methyl]-3-hydroxy-4-(methylthiomethyl)pyrrolidine
-
-
(3R,4S)-4-(benzylthiomethyl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
complete inhibition at 0.1 mM
-
(4S,5S)-2-(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)-5-[(methylsulfanyl)methyl]-1,2-thiazolidin-4-ol
(S)-9-(2,3-dihydroxy-propyl)adenine
-
-
1'-aza-4'-deaza-2'-deoxy-1'-(9-methylene)-immucillin-A
-
-
1-[(9-deazaadenin-9-yl)methyl]-3-methylthiomethylazetidine
1-[(9-deazaadenin-9-yl)methyl]-3-methylthiomethylazetidine-3-methanol
2-[[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-2-[(methylsulfanyl)methyl]propane-1,3-diol
3-Deazaadenine
-
-
3-[[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-2-[(methylsulfanyl)methyl]propan-1-ol
4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
4-chlorophenylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
5'-4-chloro-phenylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
5'-4-chloro-phenylthio-immucillin-A
5'-Chloroadenosine
-
exhibits a 35-47% inhibition of enzyme activity
5'-Chloroformycin
5'-ethylthioadenosine
5'-isobutylthio-3-deaza-adenosine
-
poor inhibitor
5'-isobutylthioadenosine
-
inhibits the reaction with methylthioadenosine by about 40%
5'-Isobutylthioinosine
-
-
5'-Isopropylthioadenosine
-
inhibits the reaction with methylthioadenosine by about 40%
5'-methylthio-3-deaza-adenosine
-
poor inhibitor
5'-Methylthioformycin
-
powerful inhibitor
5'-methylthiotubercidin
5'-n-butylthioinosine
-
-
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
5,5'-dithio-bis(2-nitrobenzoic acid)
-
-
9-erythro-(2-hydroxyl 3-nonyl)adenine
-
-
adenine
adenosine
Adenosine 5'-carboxamide
aminoethoxyvinylglycine
-
34% inhibition
benzylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
benzylthio-immucillin A
-
-
BuT-DADMe-ImmA
-
-
butylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
-
picomolar inhibitor of MTAN
calcineurin B-like 3 protein
-
calcineurin B-like 3 protein and MTAN physically associate only in the presence of Ca2+
-
Decoyinine
-
-
ethylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
ethylthio-immucillin A
-
-
ethylthio-immucillin-A
Formycin A
immucillin-A
methylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene) -immucillin-A
-
-
methylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
methylthio-immucillin A
-
-
methylthio-immucillin-A
p-chloromercuribenzoic acid
-
mM PCMB causes quantitative inhibition
p-chlorophenylthio-immucillin A
-
-
p-tolylthio-immucillin-A
phenylthio-immucillin-A
S-8-aza-adenosyl-L-homocysteine
-
powerful inhibitor
S-adenosyl-L-homocysteine sulfoxide
-
poor inhibitor
S-adenosylhomocysteine
-
competitive inhibition
S-adenosylmethionine
-
competitive inhibition
S-Formycinylhomocysteine
-
powerful inhibitor
-
S-N6-dimethyl-3-deaza-adenosyl-L-homocysteine
-
poor inhibitor
S-Tubercidinylhomocysteine
-
powerful inhibitor
sinefungin
Tris
-
Tris buffer severely inhibits
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
dithiothreitol
-
requires reducing agents, only 67% of maximal activity is observable in absence, optimal concentration 2 mM
phosphate
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00031 - 0.0435
5'-deoxy-5'-methylthioadenosine
0.00019 - 2.1
5'-methylthioadenosine
0.00055 - 0.055
5'-methylthioinosine
0.004 - 1.3
S-adenosyl-L-homocysteine
0.00000019 - 0.039
S-methyl-5'-thioadenosine
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00973 - 20
5'-methylthioadenosine
0.15 - 7.1
S-adenosyl-L-homocysteine
0.0079 - 20
S-methyl-5'-thioadenosine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 1200
5'-methylthioadenosine
400
1.6 - 1800
S-adenosyl-L-homocysteine
36
0.00012 - 50000
S-methyl-5'-thioadenosine
1578
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000011
(1R,2S)-2-(((4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl)amino)-1-(methylthio)propane-1,3-diol
-
pH and temperature not specified in the publication
0.00000008 - 0.00000036
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-methylthio-D-ribitol
0.00000023
(1S,2R)-2-(((4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl)amino)-1-(methylthio)propane-1,3-diol
-
pH and temperature not specified in the publication
0.0000008 - 0.0000017
(2R)-2-[[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-3-(methylsulfanyl)propan-1-ol
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-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
0.0000008 - 0.0000009
(2R,3S)-2-[[(4-amino-5,7a-dihydro-4aH-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
0.000085 - 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
(2S,3R)-2-[[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
-
pH and temperature not specified in the publication
0.000006
(2S,3R)-2-[[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol - methane (1:1)
-
pH and temperature not specified in the publication
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-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-4-(methylsulfanyl)butane-1,3-diol
-
0.000000002 - 0.00000014
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-methylthiomethylpyrrolidine
0.0000023 - 0.0000034
(3R,4S)-4-(benzylthiomethyl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
0.00000045 - 0.000084
1-[(9-deazaadenin-9-yl)methyl]-3-methylthiomethylazetidine
0.00000084 - 0.00015
1-[(9-deazaadenin-9-yl)methyl]-3-methylthiomethylazetidine-3-methanol
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
3-[[(4-amino-5,7a-dihydro-4aH-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]amino]-2-[(methylsulfanyl)methyl]propan-1-ol
0.00000036
4-chlorophenylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
0.00000000004 - 0.0000000093
5'-4-chloro-phenylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
0.0000000055 - 0.000000059
5'-4-chloro-phenylthio-immucillin-A
0.000322
5'-Chloroformycin
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.000027
5'-Methylthioformycin
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.0041 - 0.01
5'-methylthiotubercidin
0.000077 - 0.000116
5'-p-aminophenylthioadenosine
0.000587 - 0.000698
5'-p-nitrophenylthioadenosine
0.0000000003
BuT-DADMe-ImmA
-
pH and temperature not specified in the publication
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 - 0.00269
Formycin A
0.000000005
methylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene) -immucillin-A
-
in 100 mM HEPES, 50 mM KCl (pH 7.5), at 25°C
0.00000000011 - 0.000024
methylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin-A
0.000000089 - 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
0.0000097
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
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0004
5'-Chloroformycin
Escherichia coli
-
in 50 mM potassium phosphate buffer, 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
0.132
5'-Isobutylthioinosine
Escherichia coli
-
in 50 mM potassium phosphate buffer, 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
0.00006
5'-Methylthioformycin
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.0077
5'-methylthiotubercidin
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.094
5'-n-butylthioinosine
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.216
adenine
Escherichia coli
-
in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
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
0.000031
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
0.000027
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
0.069
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
0.025
-
crude extract, at pH 7.0 and 37°C
0.038
-
crude extract, with 5'-methylthioadenosine as substrate, in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
0.28
substrate 5'-adenosylcysteine, pH 7.0, 22°C
0.38
-
substrate adenosine, 22°C
0.46
-
substrate 5'-chloroadenosine, 22°C
0.61
substrate 5'-adenosylhomocysteine, pH 7.0, 22°C
0.83
-
substrate 5'-chloroadenosine, 22°C
0.84
substrate 5'-fluorosulfonylbenzoyladenosine, pH 7.0, 22°C
0.9
-
substrate S-adenosylhomocysteine, 22°C
1.06
-
substrate 5'-iodoadenosine, 22°C
1.36
-
substrate 5'-phenylthioadenosine, 22°C
1.5
-
substrate 5'-butylthioadenosine, 22°C
1.85
-
substrate 5'-isobutylthioadenosine, 22°C
1.98
-
substrate 5'-isobutylthioadenosine, 22°C
2.07
substrate 5'-phenylthioadenosine, pH 7.0, 22°C
2.24
substrate 5'-iodothioadenosine, pH 7.0, 22°C
2.35
substrate 5'-butylthioadenosine, pH 7.0, 22°C
2.44
-
substrate 5'-phenylthioadenosine, 22°C
2.6
-
substrate 5'-ethylthioadenosine, 22°C
2.72
-
substrate 5'-butylthioadenosine, 22°C
2.85
substrate 5'-propylthioadenosine, pH 7.0, 22°C
2.95
substrate 5'-ethylthioadenosine, pH 7.0, 22°C
3.04
substrate 5'-isopropylthioadenosine, pH 7.0, 22°C
3.14
-
substrate 5'-iodoadenosine, 22°C
3.84
substrate 5'-methylthioadenosine, pH 7.0, 22°C
4.1
-
Bgp protein, using 5'-methylthioadenosine as substrate, pH 5.0
4.4
-
Pfs protein, using 5'-methylthioadenosine as substrate, pH 5.0
4.42
-
substrate 5'-ethylthioadenosine, 22°C
6.25
-
substrate 5'-methylthioadenosine, 22°C
11.05
-
substrate 5'-methylthioadenosine, 22°C
16.88
-
after 675.2fold purification, at pH 7.0 and 37°C; purified native enzyme, pH 7.0, 37°C
373
-
after 9810fold purification, with 5'-methylthioadenosine as substrate, in 50 mM potassium phosphate buffer, pH 7.0, at 37°C
additional information
-
amide proton exchange rates of isozyme AtMTAN1
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
-
50 mM potassium phosphate buffer
7
-
assay at
8 - 8.5
-
-
10 - 12
; recombinant His-tagged enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.5
-
-
7.5 - 9
-
Tris-HCl buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
-
quite stable in this range
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
flowers express the highest level of the MTAN transcript
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240)
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240)
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240)
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240)
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Neisseria meningitidis serogroup B (strain MC58)
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
2 * 25000, His-tagged enzyme, calculated from amino acid sequence
25460
-
electrospray mass spectrometry
26030
-
2 * 26030, calculated from amino acid sequence
28000
-
SDS-PAGE
34000
-
x * 34000, SDS-PAGE
46000
-
gel filtration
59500
-
3 * 59500, SDS-PAGE
95000
-
gel filtration
180000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 34000, SDS-PAGE
homodimer
homotrimer
-
3 * 59500, SDS-PAGE
trimer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apo-enzyme as well as in complex with substrate-and transition-state-analogues 5'-methylthiotubercidin and formycin A, at 2.0-1.8 A resolution. Comparison with isoform MTAN2; homology model of structure based on isoform MTAN1; in complex with 5'-methylthiotubercidin or formycin A, hanging drop vapour diffusion method, in 70 mM sodium acetate trihydrate, pH 4.6, 5.6% (w/v) PEG 4000, 30% (v/v) glycerol
-
at 1.5 A resolution, comparison with Escherichia coli enzyme structure
-
crystal structure comparison of MTAN from Escherichia coli with the isozyme AtMTAN1 from Arabidopsis thaliana, overview
-
isozymes AtMTAN1 and AtMTAN2, X-ray diffraction structure determination and analysis at 2.9 A resolution, molecular replacement, modelling
-
in complex with its product 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
crystal structure analysis, PDB entry 1Y6Q and PDB entry 1Z5P
-
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
-
hanging drop vapor diffusion method, complexed with formycin A and 5'-methylthiotubercidin
-
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
sitting drop vapor diffusion method, using
hanging drop vapor diffusion method, using 0.2 M magnesium chloride, 0.1 M HEPES pH 7.5 and 25% (w/v) PEG 3350 or 0.05 M magnesium chloride hexahydrate, 0.1 M HEPES pH 7.5 and 30% (v/v) PEG-MME 550
purified recombinant wild-type and mutant enzymes, sitting drop vapour diffusion method, mixing of 50 mg/ml protein in 10 mM Tris-HCl, pH 8.0, with 4.0 M NaH2PO4/K2HPO4, pH 7.0, using a 1:1 ratio of protein to mother liquor, X-ray diffraction structure determination and analysis at 1.65-2.11 A resolution, molecular replacement. for the mutant enzymess th following crystallization slutions are used: for E14Q 0.1 M HEPES, pH 7.5, 25% PEG 3350, 0.2 M NaCl, for D199N 0.1 M bis-Tris, pH 5.5, 25% PEG 3350, 0.2 M MgCl2 x 6H2O, and for D199A 0.1 M bis-Tris, pH 6.5, 25% PEG 3350, 0.2 M Li2SO4 xH2O; sitting drop vapor diffusion method, over 4.0 M NaH2PO4/K2HPO4 pH 7.0
K4NDB8, O24915
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
in complex with But-dadme-imma A, sitting drop vapour diffusion method, with 0.2 M potassium iodide and 20% (w/v) PEG3350
-
sitting drop vapor diffusion method
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 12
recombinant His-tagged enzyme, stable at, denaturation and loss of activity at and below pH 7.0
731666
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 50
-
quite stable in this range
50
-
at temperatures above, the activity decreases, heating at 100°C for 3 min results in complete inhibition
60
-
the enzyme is rapidly inactivated after exposure for 15 min at 60°C
67
-
enzyme activity rapidly dropping at temperatures above
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme activity stabilized by glutathione
-
enzyme activity stabilized by L-cysteine
-
moderately stable
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM Bicine buffer, 5% glycerol buffer, stable for at least 3 months, tolerates repeated freezing and thawing
-
-20°C, 50 mM potassium phosphate buffer (pH 7.0), at least 2 months, no significant loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, acetone precipitation, Sephacryl S-200 gel filtration, DEAE-Sephacel gel filtration, and 5'-AMP-Sepharose column chromatography; native enzyme 675.2fold from cotyledons by ammonium sulfate fractionation, acetone precipitation, gel filtration, anion exchange chromatography, and affinity chromatography
-
ammonium sulfate precipitation, DEAE-Sephadex gel filtration, hydroxyapatite column chromatography, S-formycinylhomocysteine-Sepharose column chromatography, and Sephacryl S-200 gel filtration
-
ammonium sulfate precipitation, nickel affinity column chromatography, and Superdex 200 gel filtration
glutathione-Sepharose column chromatography
-
His-bind resin column chromatography
-
HisTrap column chromatography and Superdex 200 gel filtration
HisTrap column chromatography and Superdex 75 gel filtration; recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration
K4NDB8, O24915
homogeneity
-
Ni-NTA agarose column chromatography; Ni-NTA agarose column chromatography and Superdex-200 gel filtration
-
Ni-NTA column chromatography
Ni-NTA column chromatography and Superdex 200 gel filtration
-
Ni-NTA column chromatography, and gel filtration; recombinant His-tagged enzyme from Escherichia coli strain BL21trxB by nickel affinity chromatography to over 95% purity
Ni-NTA column chromatography; recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21 Star(DE3) by nickel affinity chromatography
Ni-NTA Superflow resin column chromatography and Superdex-200 gel filtration
recombinant His-tagged isozyme AtMTAN1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant isozyme AtMTAN2 from Escherichia coli to homogeneity
-
recombinant wild-type and mutant His-tagged MTAN from strain BL21(DE3) by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as His-tagged protein
-
expressed in Escherichia coli BL21 (DE3) cells
-
expressed in Escherichia coli BL21 (DE3) Rosetta cells
expressed in Escherichia coli BL21 cells and in Nicotiana benthamiana
-
expressed in Escherichia coli BL21 Codon+ cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells; gene mnqB, expression of recombinant His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
K4NDB8, O24915
expressed in Escherichia coli BL21(DE3) cells; recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strain BL21 Star(DE3)
expressed in Escherichia coli BL21trxB cells; gene RV0091, recombinant expression of active His-tagged enzyme in Escherichia coli strain BL21trxB, optimization of expression method
expression in Escherichia coli
gene inactivation/replacement with Escherichia coli pfs gene, cloning of the yrrU gene, PCR amplified
-
isozyme AtMTAN1, overexpression of the His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
isozymes AtMTAN1 and AtMTAN2, DNA and amino acid sequence determination and analysis, overexpression of isozyme AtMTAN2 in Escherichia coli
-
overexpression of wild-type and mutant His-tagged enzyme in strain BL21(DE3)
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE