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2',3'-dideoxyadenosine + phosphate
adenine + 2,3-deoxy-D-ribose 1-phosphate
-
substrate for trypanosomal but not for mammalian enzyme
-
-
?
2'-chloro-2'-deoxyadenosine + phosphate
adenine + 2-chloro-2-deoxy-alpha-D-ribose 1-phosphate
2'-deoxy-2'-amino-5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 2-deoxy-2-amino-5-thio-D-ribose 1-phosphate
-
-
-
-
?
2'-deoxy-2'-azido-5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 2-deoxy-2-azido-5-thio-D-ribose 1-phosphate
-
-
-
-
?
2'-deoxy-2-fluoro-5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 2-deoxy-2-fluoro-5-thio-D-ribose 1-phosphate
-
-
-
-
?
2'-deoxy-5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 2-deoxy-5-thio-D-ribose 1-phosphate
-
-
-
-
?
2'-deoxyadenosine + phosphate
adenine + 2'-deoxy-D-ribose 1-phosphate
the enzyme can use adenosine with the same efficiency as 5'-deoxy-5'-methylthioadenosine
-
-
?
2'-deoxyadenosine + phosphate
adenine + 2-deoxy-D-ribose 1-phosphate
2'-fluoro-2'-deoxyadenosine + phosphate
adenine + 2'-fluoro-2'-deoxy-D-ribose 1-phosphate
2-amino-5'-deoxy-5'-(hydroxyethylthio)adenosine + phosphate
2-aminoadenosine + 5-hydroxyethylthio-D-ribose 1-phosphate
-
28% activity compared to 5'-methyladenosine or 5'-deoxy-5'-(hydroxyethylthio)adenosine
-
-
?
2-chloro-2'-deoxyadenosine + phosphate
2-chloroadenine + 2-deoxy-D-ribose 1-phosphate
-
-
-
-
r
2-chloro-5'-O-methyl-2'-deoxyadenosine + phosphate
2-chloroadenine + 5-O-methyl-2-deoxy-D-ribose 1-phosphate
-
-
-
-
r
2-chloroadenosine + phosphate
2-chloroadenine + D-ribose 1-phosphate
-
-
-
-
r
2-fluoro-5'-deoxy-5'-(hydroxyethylthio)adenosine + phosphate
2-fluoroadenosine + 5-hydroxyethylthio-D-ribose 1-phosphate
-
149% activity compared to 5'-methyladenosine or 5'-deoxy-5'-(hydroxyethylthio)adenosine
-
-
?
3'-deoxy-5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 3-deoxy-5-thio-D-ribose 1-phosphate
-
-
-
-
?
3'-deoxyadenosine + phosphate
adenine + 3-deoxy-D-ribose 1-phosphate
-
substrate for trypanosomal but not for mammalian enzyme
-
-
?
5'-butylthioadenosine + phosphate
adenine + 5-butylthio-D-ribose 1-phosphate
5'-chloroadenosine + phosphate
adenine + 5-deoxy-5-chloro-D-ribose 1-phosphate
5'-deoxy-5'-(1,3-thiazol)-2-yl-sulfanyladenosine + phosphate
adenine + 5-(1,3-thiazol-2-yl)thio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-(2-(pyridin-2-yl)ethyl)-thioadenosine + phosphate
adenine + 5-ethylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-(2-methylbutyl)-thioadenosine + phosphate
adenine + 5-(2-methylbutyl)thio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-(2-methylphenyl)-thioadenosine + phosphate
adenine + 5-(2-methylphenyl)thio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-(3-methylphenyl)-thioadenosine + phosphate
adenine + 5-(3-methylphenyl)thio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-(4-methoxyphenyl)-thioadenosine + phosphate
adenine + 5-(4-methoxyphenyl)thio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-(4-methylphenyl)-thioadenosine + phosphate
adenine + 5-(4-methylphenyl)thio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-(hydroxyethylthio)adenosine + phosphate
adenine + 5-hydroxyethylthio-D-ribose 1-phosphate
5'-deoxy-5'-(phenylethyl)-thioadenosine + phosphate
adenine + 5-phenylethylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-(phenylmethyl)-thioadenosine + phosphate
adenine + 5-phenylmethylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-(quinolin-2-yl)-sulfanyladenosine + phosphate
adenine + 5-(quinolin-2-yl)thio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-butylthioadenosine + phosphate
adenine + 5-butylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-cyclohexyl-thioadenosine + phosphate
adenine + 5-cyclohexylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-cyclopentyl-thioadenosine + phosphate
adenine + 5-cyclopentylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-ethylthioadenosine + phosphate
adenine + 5-ethylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-hydroxyethylthioadenosine + phosphate
adenine + 5-(2-hydroxyethyl)thio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-imidazol-2-yl-sulfanyladenosine + phosphate
adenine + 5-(imidazol-2-yl)thio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-isobutylthioadenosine + phosphate
adenine + 5-isobutylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-isopentylthioadenosine + phosphate
adenine + 5-isopentylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-methyl-thioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5'-deoxy-5'-methyl-thio-D-ribose-1-phosphate
-
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
5'-deoxy-5'-phenyl-thioadenosine + phosphate
adenine + 5-phenylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-phenylmethylene-adenosine + phosphate
adenine + 5-deoxy-5-phenylmethylene-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-pyridin-2-yl-sulfanyladenosine + phosphate
adenine + 5-(pyridin-2-yl)thio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-pyridin-4-yl-sulfanyladenosine + phosphate
adenine + 5-(pyridin-4-yl)thio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-tert-butylthioadenosine + phosphate
adenine + 5-tert-butylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-[4-(trifluoromethyl)phenyl]-thioadenosine + phosphate
adenine + 5-[4-(trifluoromethyl)phenyl]thio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'phenylaminoadenosine + phosphate
adenine + 5-deoxy-5-phenylamino-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-adenosine + phosphate
adenine + 5-thio-D-ribose 1 phosphate
-
-
-
-
?
5'-deoxyadenosine + phosphate
adenine + 5-deoxy-D-ribose 1-phosphate
5'-ethylthioadenosine + phosphate
adenine + 5-ethylthio-D-ribose 1-phosphate
5'-iodo-5'-deoxyadenosine + phosphate
adenine + 5-iodo-5-deoxy-D-ribose 1-phosphate
-
-
-
-
r
5'-iodoadenosine + phosphate
adenine + 5-deoxy-5-iodo-D-ribose 1-phosphate
5'-isobutylthioadenosine + phosphate
adenine + 5-isobutylthio-D-ribose 1-phosphate
5'-isobutylthioinosine + phosphate
hypoxanthine + 5-isobutylthio-D-ribose 1-phosphate
Caldariella acidophila
-
8.1% of the reaction with 5'-methylthioadenosine
-
-
?
5'-methylselenoadenosine + phosphate
adenine + 5-methylseleno-D-ribose 1-phosphate
-
95% of the activity with 5'-methylthioadenosine
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
5'-methylthioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
?
5'-methylthioinosine + phosphate
hypoxanthine + 5-methylthio-alpha-D-ribose 1-phosphate
5'-n-butylthioadenosine + phosphate
adenine + 5-n-butylthio-D-ribose 1-phosphate
Caldariella acidophila
-
93.3% of the reaction with 5'-methylthioadenosine
-
-
?
5'-n-propylthioadenosine + phosphate
adenine + 5-n-propylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-phenyladenosine + phosphate
adenine + 5-phenyl-D-ribose 1-phosphate
-
-
-
-
?
5'-phenylthioadenosine + phosphate
adenine + 5-phenylthio-D-ribose 1-phosphate
6-methylpurine 2'-deoxyribonucleoside + phosphate
6-methylpurine + 2-deoxy-D-ribose 1-phosphate
-
substrate for trypanosomal but not for mammalian enzyme
-
-
?
9-[2-deoxy-beta-D-ribofuranosyl]-6-methylpurine + phosphate
?
-
a toxic prodrug, 5% of the activity with S-methyl-5'-thioadenosine
-
-
?
9-[6-deoxy-beta-L-talofuranosyl]-2-F-adenine + phosphate
?
-
a toxic prodrug, 23% of the activity with S-methyl-5'-thioadenosine
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
deoxyadenosine + phosphate
adenine + deoxy-D-ribose 1-phosphate
-
-
-
-
?
guanosine + phosphate
guanine + D-ribose 1-phosphate
inosine + phosphate
hypoxanthine + D-ribose 1-phosphate
S-adenosyl-L-homocysteine + phosphate
?
0.81% activity compared to activity with 5'-methylthioadenosine
-
-
?
S-adenosylhomocysteine + ?
?
-
-
-
?
S-adenosylhomocysteine + phosphate
?
14% relative activity
-
-
?
S-methyl-5'-thioadenosine + arsenate
adenine + S-methyl-5-thio-alpha-D-ribose 1-arsenate
-
arsenolysis
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
additional information
?
-
2'-chloro-2'-deoxyadenosine + phosphate
adenine + 2-chloro-2-deoxy-alpha-D-ribose 1-phosphate
-
-
-
-
?
2'-chloro-2'-deoxyadenosine + phosphate
adenine + 2-chloro-2-deoxy-alpha-D-ribose 1-phosphate
-
-
-
-
?
2'-deoxyadenosine + phosphate
adenine + 2-deoxy-D-ribose 1-phosphate
-
low activity
-
-
r
2'-deoxyadenosine + phosphate
adenine + 2-deoxy-D-ribose 1-phosphate
-
-
-
-
?
2'-deoxyadenosine + phosphate
adenine + 2-deoxy-D-ribose 1-phosphate
-
substrate for trypanosomal but not for mammalian enzyme
-
-
?
2'-fluoro-2'-deoxyadenosine + phosphate
adenine + 2'-fluoro-2'-deoxy-D-ribose 1-phosphate
-
-
-
-
?
2'-fluoro-2'-deoxyadenosine + phosphate
adenine + 2'-fluoro-2'-deoxy-D-ribose 1-phosphate
-
-
-
-
?
5'-butylthioadenosine + phosphate
adenine + 5-butylthio-D-ribose 1-phosphate
24% relative activity
-
-
?
5'-butylthioadenosine + phosphate
adenine + 5-butylthio-D-ribose 1-phosphate
25% relative activity
-
-
?
5'-chloroadenosine + phosphate
adenine + 5-deoxy-5-chloro-D-ribose 1-phosphate
13% relative activity
-
-
?
5'-chloroadenosine + phosphate
adenine + 5-deoxy-5-chloro-D-ribose 1-phosphate
4% relative activity
-
-
?
5'-deoxy-5'-(hydroxyethylthio)adenosine + phosphate
adenine + 5-hydroxyethylthio-D-ribose 1-phosphate
-
trypanocidal substrate analogue
-
-
?
5'-deoxy-5'-(hydroxyethylthio)adenosine + phosphate
adenine + 5-hydroxyethylthio-D-ribose 1-phosphate
-
preincubation of cells with the substrate lead to 22-37% inhibition of spermidine synthesis from ornithine and 2-7fold increased cytosolic levels of S-adenosyl-L-methionine and S-adenosyl-L-homocysteine, and up to 8fold increased cytosolic level of 5'-methyladenosine
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
sugar specificity
-
r
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
salvage reaction
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
involved in cardiac purine breakdown during ischemia
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
substrate is a by-product of polyamine biosynthesis, which is essential for cell growth and proliferation
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
r
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
substrate-induced conformational change involving Glu163, which is located at the interface between subunits and swings in toward the active site upon nucleoside binding
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
the transition state is stabilized in different ways for 6-amino versus 6-oxo substrates
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxyadenosine + phosphate
adenine + 5-deoxy-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxyadenosine + phosphate
adenine + 5-deoxy-D-ribose 1-phosphate
-
-
-
-
r
5'-deoxyadenosine + phosphate
adenine + 5-deoxy-D-ribose 1-phosphate
-
-
-
-
?
5'-deoxyadenosine + phosphate
adenine + 5-deoxy-D-ribose 1-phosphate
-
phosphate-dependent
-
r
5'-ethylthioadenosine + phosphate
adenine + 5-ethylthio-D-ribose 1-phosphate
40% relative activity
-
-
?
5'-ethylthioadenosine + phosphate
adenine + 5-ethylthio-D-ribose 1-phosphate
42% relative activity
-
-
?
5'-ethylthioadenosine + phosphate
adenine + 5-ethylthio-D-ribose 1-phosphate
-
60% of the activity with 5'-methylthioadenosine
-
-
?
5'-ethylthioadenosine + phosphate
adenine + 5-ethylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-iodoadenosine + phosphate
adenine + 5-deoxy-5-iodo-D-ribose 1-phosphate
17% relative activity
-
-
?
5'-iodoadenosine + phosphate
adenine + 5-deoxy-5-iodo-D-ribose 1-phosphate
28% relative activity
-
-
?
5'-isobutylthioadenosine + phosphate
adenine + 5-isobutylthio-D-ribose 1-phosphate
32% relative activity
-
-
?
5'-isobutylthioadenosine + phosphate
adenine + 5-isobutylthio-D-ribose 1-phosphate
17% relative activity
-
-
?
5'-isobutylthioadenosine + phosphate
adenine + 5-isobutylthio-D-ribose 1-phosphate
Caldariella acidophila
-
97% of the reaction with 5'-methylthioadenosine
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
100% relative activity
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
adenine-bound MTAN1 is exclusively in its closed form, substantial conformational changes occur in this region during the enzymatic reaction. Residues Met35, Val90, Leu181, Met201, Phe237 and Ile143', Ile145' and Phe148' in a neighboring MTAN1 monomer bind adenine via hydrophobic and van der Waals interactions. The hydrophobic side chains Phe237 and Leu181 show structural perturbations that provide the flexible accommodation of the adenine ring. The carboxylic side chain of Asp225 hydrogen bonds with nitrogen atoms in the adenine ring, therefore being key determinant for the adenine base. The side chain Thr116 and backbone Gly118 also interact with the adenine molecule
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
hydrolysis of 5'-methylthioadenosine predominates despite MTAN2 possessing both 5'-methylthioadenosine and S-adenosylhomocysteine hydrolysis activity. MTAN2 binds 5'-methylthioadenosine approximately 6fold higher than S-adenosylhomocysteine. Residues between 216 and 225 in MTAN2 contain conformational differences representing an open conformation when compared with MTAN1. The side chains Met22, Val78, Met168, Met188, Phe224 along with Ile130', Val132' and Leu135' in a neighboring MTAN2 monomer bind adenine via hydrophobic and van der Waals interactions. The hydrophobic side chains Phe224 and Met168 show structural perturbations that provide the flexible accommodation of the adenine ring. The carboxylic side chain of Asp211 hydrogen bonds with nitrogen atoms in the adenine ring, therefore being key determinant for the adenine base. The side chain Thr103 and backbone Gly105 also interact with the adenine molecule
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
Caldariella acidophila
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
Caldariella acidophila
-
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
Caldariella acidophila
-
an antiproliferative effect on stimulated human lymphocytes and virally transformed mouse fibroblasts
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
Caldariella acidophila
-
involved in salvage of adenine and methionine from 5'-methylthioadenosine
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
Caldariella acidophila
-
physiological significance of 5'-methylthioadenosine cleavage is probably related to removal of the thioether which in turn exerts a significant inhibition on methyl transfer reactions
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
r
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
r
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
r
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
completely dependent on phosphate
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
important for the salvage of adenine and methionine
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
involved in salvage of adenine and methionine from 5'-methylthioadenosine
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
structural comparison of MTA phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
5'-methylthioadenosine is the best substrate
-
-
r
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
preferred direction of reaction is temperature-dependent
-
-
r
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
r
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
r
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
involved in salvage of adenine and methionine from 5'-methylthioadenosine
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
completely dependent on phosphate
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
binding of phosphate and 5-methylthioribose 1-phosphate to the enzyme induces a conformational transition that stabilizes the folded structure of the enzyme
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
5'-methylthioadenosine and adenine form ternary complexes with the enzyme only in presence of phosphate and methylthioribose 1-phosphate, respectively
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
the enzyme regulates ornithine decarboxylase by production of downstream metabolites. Tumor suppressor activity of MTAP may be due to its effect on ornithine decarboxylase activity
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
the [3'-2H] kinetic isotope effect is consistent with a unique H3'-endo-exo configuration and 3'-hydroxyl polarization without full ionization at the MTAN transition state. The MTAN transition state is a fully dissociative (SN1), ribooxacarbenium-like structure with its C1'-N9 distance larger than 3.2 A. The ribosyl moiety adopts a H3'-endo-exo transition conformation, and the 3'-OH residue is partially polarized by the adjacent carboxylate with a hydrogen bond distance of 2.83 A. The MTAN transition state has a geometry between the unrestrained H3'-endo 5'-methylthioadenosine substrate and a fully developed 3'-exo ribooxacarbenium ion
-
-
ir
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
r
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
completely dependent on phosphate
-
-
?
5'-methylthioinosine + phosphate
hypoxanthine + 5-methylthio-alpha-D-ribose 1-phosphate
Caldariella acidophila
-
-
-
-
?
5'-methylthioinosine + phosphate
hypoxanthine + 5-methylthio-alpha-D-ribose 1-phosphate
Caldariella acidophila
-
8.8% of the reaction with 5'-methylthioadenosine
-
-
?
5'-methylthioinosine + phosphate
hypoxanthine + 5-methylthio-alpha-D-ribose 1-phosphate
-
8.9% of the reaction with 5'-methylthioadenosine
-
-
?
5'-phenylthioadenosine + phosphate
adenine + 5-phenylthio-D-ribose 1-phosphate
39% relative activity
-
-
?
5'-phenylthioadenosine + phosphate
adenine + 5-phenylthio-D-ribose 1-phosphate
12% relative activity
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
6% relative activity
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
-
-
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
-
-
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
-
-
-
-
r
adenosine + phosphate
adenine + D-ribose 1-phosphate
-
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
-
-
-
-
?, r
adenosine + phosphate
adenine + D-ribose 1-phosphate
2.1% activity compared to activity with 5'-methylthioadenosine
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
-
-
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
-
-
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
-
-
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
-
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
-
-
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
the enzyme can use adenosine with the same efficiency as 5'-deoxy-5'-methylthioadenosine
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
-
-
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
-
-
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
-
-
-
-
?
guanosine + phosphate
guanine + D-ribose 1-phosphate
-
-
-
-
?
guanosine + phosphate
guanine + D-ribose 1-phosphate
-
-
-
?
guanosine + phosphate
guanine + D-ribose 1-phosphate
-
-
-
-
?
inosine + phosphate
hypoxanthine + D-ribose 1-phosphate
-
-
-
-
?
inosine + phosphate
hypoxanthine + D-ribose 1-phosphate
-
-
-
?
inosine + phosphate
hypoxanthine + D-ribose 1-phosphate
-
-
-
-
?
inosine + phosphate
hypoxanthine + D-ribose 1-phosphate
most effective substrate
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
ir
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
phosphorolysis
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
recycling of 5'-methylthioadenosine, the byproduct from spermine and spermidine synthesis, to S-adenosylmethionine, the precursor for polyamine synthesis, pathway overview
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
?
additional information
?
-
can not hydrolyze S-adenosylhomocysteine
-
-
?
additional information
?
-
can not hydrolyze S-adenosylhomocysteine
-
-
?
additional information
?
-
the plant active site is likely less flexible, which may contribute to its reduced efficiency in binding larger substrates. The 5'-alkylthio binding subsite is more constricted in MTAN1
-
-
?
additional information
?
-
the plant active site is likely less flexible, which may contribute to its reduced efficiency in binding larger substrates. The 5'-alkylthio binding subsite is more constricted in MTAN1
-
-
?
additional information
?
-
-
the plant active site is likely less flexible, which may contribute to its reduced efficiency in binding larger substrates. The 5'-alkylthio binding subsite is more constricted in MTAN1
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
specificity in both directions of nucleoside cleavage and nucleoside synthesis
-
-
?
additional information
?
-
-
replacement of the 6-amino group by an OH-group and of N-7 by a methinic radical results in almost complete loss of activity
-
-
?
additional information
?
-
enzyme plays a role in purine and polyamine metabolism and in the regulation of transmethylation reactions
-
-
?
additional information
?
-
-
enzyme plays a role in purine and polyamine metabolism and in the regulation of transmethylation reactions
-
-
?
additional information
?
-
-
inverse correlation between enzyme expression and progression of melanocytic tumors, important role of enzyme inactivation in the development of melanomas
-
-
?
additional information
?
-
-
enzyme is involved in the methionine dependent tumor cell growth
-
-
?
additional information
?
-
-
many malignant cells lack MTAP activity because of chromosomal loss or epigeneticregulation
-
-
?
additional information
?
-
-
principal enzyme involved in purine synthesis via the salvage pathway, such that MTAP-negative cancers are solely dependent on de novo purine synthesis mechanisms, intracellular Mtap protein levels determine response to purine biosynthesis inhibitor L-alanosine, overview
-
-
?
additional information
?
-
-
9-[6-deoxy-beta-L-talofuranosyl]-6-methylpurine is a poor substrate for the enzyme
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
6-amino purine nucleosides are the preferred substrates, substrate specificity
-
-
?
additional information
?
-
PfMTAP is characterized by a broad substrate specificity towards purine nucleosides, with a 20fold higher catalytic efficacy for adenosine and 5'-methylthioadenosine than for inosine and guanosine
-
-
?
additional information
?
-
-
PfMTAP is characterized by a broad substrate specificity towards purine nucleosides, with a 20fold higher catalytic efficacy for adenosine and 5'-methylthioadenosine than for inosine and guanosine
-
-
?
additional information
?
-
-
no activity with S-adenosylhomocysteine
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
substrate specificity
-
-
?
additional information
?
-
-
no activity with S-adenosyl-L-methionine
-
-
?
additional information
?
-
no activity with S-adenosyl-L-methionine
-
-
?
additional information
?
-
-
no activity with S-adenosylhomocysteine
-
-
?
additional information
?
-
no activity with S-adenosylhomocysteine
-
-
?
additional information
?
-
-
involved in the catabolism of 5'-methylthioadenosine, adenosine, guanosine and inosine
-
-
?
additional information
?
-
involved in the catabolism of 5'-methylthioadenosine, adenosine, guanosine and inosine
-
-
?
additional information
?
-
-
very low activity with cordycepin, Ara-A, tubercidin, guanosine, deoxyguanosine, inosine, deoxyinosine, uridine, deoxyuridine, cytidine, deoxycytidine, and thymidine
-
-
?
additional information
?
-
-
fluorine substitution at the C-2 position of the purine ring increases activity by 50%, whereas substitution with an amino group reduces activity to about one-third of the control
-
-
?
additional information
?
-
-
metabolic pathway, overview
-
-
?
additional information
?
-
-
very low activity with cordycepin, Ara-A, tubercidin, guanosine, deoxyguanosine, inosine, deoxyinosine, uridine, deoxyuridine, cytidine, deoxycytidine, and thymidine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
5'-deoxy-5'-(hydroxyethylthio)adenosine + phosphate
adenine + 5-hydroxyethylthio-D-ribose 1-phosphate
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5'-deoxy-5'-methyl-thio-D-ribose-1-phosphate
-
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
adenosine + phosphate
adenine + D-ribose 1-phosphate
guanosine + phosphate
guanine + D-ribose 1-phosphate
-
-
-
?
inosine + phosphate
hypoxanthine + D-ribose 1-phosphate
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
additional information
?
-
5'-deoxy-5'-(hydroxyethylthio)adenosine + phosphate
adenine + 5-hydroxyethylthio-D-ribose 1-phosphate
-
trypanocidal substrate analogue
-
-
?
5'-deoxy-5'-(hydroxyethylthio)adenosine + phosphate
adenine + 5-hydroxyethylthio-D-ribose 1-phosphate
-
preincubation of cells with the substrate lead to 22-37% inhibition of spermidine synthesis from ornithine and 2-7fold increased cytosolic levels of S-adenosyl-L-methionine and S-adenosyl-L-homocysteine, and up to 8fold increased cytosolic level of 5'-methyladenosine
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
salvage reaction
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
involved in cardiac purine breakdown during ischemia
-
-
?
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
substrate is a by-product of polyamine biosynthesis, which is essential for cell growth and proliferation
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
Caldariella acidophila
-
an antiproliferative effect on stimulated human lymphocytes and virally transformed mouse fibroblasts
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
Caldariella acidophila
-
involved in salvage of adenine and methionine from 5'-methylthioadenosine
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
Caldariella acidophila
-
physiological significance of 5'-methylthioadenosine cleavage is probably related to removal of the thioether which in turn exerts a significant inhibition on methyl transfer reactions
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
important for the salvage of adenine and methionine
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
involved in salvage of adenine and methionine from 5'-methylthioadenosine
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
involved in salvage of adenine and methionine from 5'-methylthioadenosine
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
?
5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
the enzyme regulates ornithine decarboxylase by production of downstream metabolites. Tumor suppressor activity of MTAP may be due to its effect on ornithine decarboxylase activity
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
-
-
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
-
-
-
?
adenosine + phosphate
adenine + D-ribose 1-phosphate
the enzyme can use adenosine with the same efficiency as 5'-deoxy-5'-methylthioadenosine
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
ir
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
phosphorolysis
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
recycling of 5'-methylthioadenosine, the byproduct from spermine and spermidine synthesis, to S-adenosylmethionine, the precursor for polyamine synthesis, pathway overview
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
?
additional information
?
-
enzyme plays a role in purine and polyamine metabolism and in the regulation of transmethylation reactions
-
-
?
additional information
?
-
-
enzyme plays a role in purine and polyamine metabolism and in the regulation of transmethylation reactions
-
-
?
additional information
?
-
-
inverse correlation between enzyme expression and progression of melanocytic tumors, important role of enzyme inactivation in the development of melanomas
-
-
?
additional information
?
-
-
enzyme is involved in the methionine dependent tumor cell growth
-
-
?
additional information
?
-
-
many malignant cells lack MTAP activity because of chromosomal loss or epigeneticregulation
-
-
?
additional information
?
-
-
principal enzyme involved in purine synthesis via the salvage pathway, such that MTAP-negative cancers are solely dependent on de novo purine synthesis mechanisms, intracellular Mtap protein levels determine response to purine biosynthesis inhibitor L-alanosine, overview
-
-
?
additional information
?
-
-
involved in the catabolism of 5'-methylthioadenosine, adenosine, guanosine and inosine
-
-
?
additional information
?
-
involved in the catabolism of 5'-methylthioadenosine, adenosine, guanosine and inosine
-
-
?
additional information
?
-
-
metabolic pathway, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(+/-)-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]-4-ethyl-3-hydroxypyrrolidine
-
-
(+/-)-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-cyclopropyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
(+/-)-trans-4-[3-(benzylthio)propyl]-1-[(9-deazaadenin-9-yl)-methyl]-3-hydroxypyrrolidine
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-di-deoxy-1,4-imino-5-methylthio-D-ribitol
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-(1-naphthyl)thio-D-ribitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-(3-methylphenyl)thio-D-ribitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-(4-methylphenyl)thio-D-ribitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-methylthio-D-ribitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-O-methyl-D-ribitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-phenylthio-D-ribitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-5-(2-fluoroethyl)thio-1,4-imino-D-ribitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-5-(2-hydroxyethyl)thio-1,4-imino-D-ribitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-5-(4-fluorophenyl)thio-1,4-imino-D-ribitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-5-ethylthio-1,4-imino-D-ribitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-5-n-propylthio-1,4-imino-D-ribitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-imino-1,4,5,6,7-penta-deoxy-D-ribo-heptitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-1,4-imino-1,4,5-trideoxy-D-ribitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-5-(3-chlorophenyl)thio-1,4-dideoxy-1,4-imino-D-ribitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-5-(4-chlorophenyl)thio-1,4-dideoxy-1,4-imino-D-ribitol
-
-
(1S)-1-(9-deazaadenin-9-yl)-5-benzylthio-1,4-dideoxy-1,4-imino-D-ribitol
-
-
(3R,4R)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxy-4-methoxymethylpyrrolidine
-
-
(3R,4R)-4-(benzyloxymethyl)-1-[(9-deaza-adenin-9-yl)-methyl]-3-hydroxypyrrolidine
-
-
(3R,4S)-1-[(8-aza-9-deazaadenin-9-yl)methyl]-4-benzylthiomethyl-3-hydroxypyrrolidine hydrochloride
-
-
(3R,4S)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxy-4-(1-propylthiomethyl)pyrrolidine
-
-
(3R,4S)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxy-4-(2-propylthiomethyl)pyrrolidine
-
-
(3R,4S)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxy-4-(4-pyridylthiomethyl)pyrrolidine
-
-
(3R,4S)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxy-4-phenylthiomethylpyrrolidine
-
-
(3R,4S)-1-[(9-deaza-adenin-9-yl)methyl]-4-(4-fluorophenylthiomethyl)-3-hydroxypyrrolidine
-
-
(3R,4S)-1-[(9-deaza-adenin-9-yl)methyl]-4-ethylthiomethyl-3-hydroxypyrrolidine
-
-
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(1-propyl)pyrrolidine
-
-
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(4-chlorophe-nylthiomethyl)pyrrolidine
-
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(methylthiomethyl)pyrrolidine
-
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-methylthiomethylpyrrolidine
-
-
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-4-ethyl-3-hydroxypyrrolidine
-
-
(3R,4S)-1-[(9-deazaadenin-9yl)methyl]-3-hydroxy-4-(methylthio-methyl) pyrrolidine
-
treatment of cultured FaDu and Cal27 cells with 0.001 mM (3R,4S)-1-[(9-deazaadenin-9yl)methyl]-3-hydroxy-4-(methylthio-methyl) pyrrolidine and 0.02 mM 5'-methylthioadenosine inhibits MTAP by 96%, increases cellular 5'-methylthioadenosine concentrations, decreases polyamines, and induces apoptosis
(3R,4S)-4-(1-butylthiomethyl)-1-[(9-deaza-adenin-9-yl)-methyl]-3-hydroxypyrrolidine
-
-
(3R,4S)-4-(3-chlorophenylthiomethyl)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
(3R,4S)-4-(4-chlorophenylthiomethyl)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
(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)-4-cyclohexylthiomethyl-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
2'-deoxyinosine
-
weak, competitive
2-bromo-9-(1,3-dihydroxy-2-propoxymethyl)adenine
-
strong
2-bromo-9-(2-hydroxyethoxymethyl)adenine
-
-
2-chloro-9-(1,3-dihydroxy-2-propoxymethyl)adenine
-
strong
2-chloro-9-(2-hydroxyethoxymethyl)adenine
-
-
2-Deoxyribose 1-phosphate
-
-
2-iodo-9-(1,3-dihydroxy-2-propoxymethyl)adenine
-
strong
2-iodo-9-(2-hydroxyethoxymethyl)adenine
-
-
4-Cl-PhT-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin A
-
5'-(4-chlorophenyl)thio-DADMe-immucillin A
-
-
5'-butylthio-DADMe-immucillin A
-
-
5'-butylthio-DADMe-ImmucillinA
5'-Deoxy-5'-chloroformycin
-
competitive
5'-deoxy-5'-methylthiotubercidin
-
-
5'-deoxy-adenosine
-
and analogues; strong, competitive
5'-ethylthio-DADMe-ImmucillinA
-
inhibits quorum sensing induction completely at 0.001 mM
5'-ethylthioadenosine
-
-
5'-methylthio-DADMe-immucillin A
5'-methylthio-DaDMe-Immucillin-A
-
5'-methylthio-DADMe-ImmucillinA
5'-methylthio-immucillin A
-
-
5'-methylthio-immucillin-adenine
-
i.e. MT-immucillin-A
5'-n-Propylthioadenosine
-
-
5'-propylthio-DADMe-immucillin A
-
-
5-methylthio-4'-deaza-1'-aza-2'-deoxy-1'-(9-methylene)-immucillin A
-
5-methylthio-immucillin A
-
9-(phosphonoalkyl)adenine
-
-
9-(phosphonoheptyl)adenine
-
-
9-[(1-Hydroxy-3-iodo-2-propoxy)methyl]adenine
adenine arabinoside
-
weak, competitive
adenosine
-
strong, competitive
calcineurin B-like 3
inhibits only in the presence of Ca2+, MTAN interacts specifically with calcineurin B-like 3, but not with calcineurin B-like 1 and calcineurin B-like 4. The 91-amino acid region of calcineurin B-like 3 is sufficient for the interaction with MTAN. Calcineurin B-like 3 and MTAN associate with each other in plant cells, they interact in vitro and in vivo, form a complex outside of the nucleus, colocalize mainly at the plasma membrane
-
dithiothreitol
-
0.8 M, reduction of thermostability
guanidine hydrochloride
only recombinant enzyme
guanosine
-
weak, competitive
Inosine
-
weak, competitive
MT-ImmA
-
i.e. (3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-methylthiomethylpyrrolidine
N-ethylmaleimide
-
5'-methylthioadenosine partly protects
p-chloromercuribenzoic acid
proteinase K
-
recombinant enzyme, 10% remaining activity after 4 h at 37°C, phosphate protects
-
S-adenosyl-L-homocysteine
SH-group blocking compounds
-
Subtilisin
-
recombinant enzyme, 24% remaining activity after 4 h at 37°C, phosphate protects
-
tert-butyl trans-3-hydroxy-4-vinylpyrrolidine-1-carboxylate
-
-
trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-vinylpyrrolidine
-
-
trans-4-cyclopentyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
5'-butylthio-DADMe-ImmucillinA
-
inhibits autoinducer-2 production in enterohemorrhagic strain O157:H7 and MTAN knockout strain. Inhibition of autoinducer-2 production in both strains persists for several generations, and causes reduction in biofilm formation. Strong binding to MTAN, causes no growth defects of O157:H7 and MTAN knockout strain in the presence of up to 0.0005 mM, produces the same phenotype as the MTAN- strain
5'-butylthio-DADMe-ImmucillinA
-
inhibits quorum sensing induction completely at 0.001 mM
5'-dimethylthioadenosine
-
sulfonium salt, noncompetitive
5'-dimethylthioadenosine
-
weak
5'-methylthio-DADMe-immucillin A
-
-
5'-methylthio-DADMe-immucillin A
-
5'-methylthio-DADMe-ImmucillinA
-
inhibits autoinducer-2 production in enterohemorrhagic strain O157:H7 and MTAN knockout strain. Causes no growth defects of O157:H7 and MTAN knockout strain in the presence of up to 0.0005 mM
5'-methylthio-DADMe-ImmucillinA
-
inhibits quorum sensing induction completely at 0.001 mM
5'-methylthiotubercidin
combination of a more occluded active site in its open state and reduced ligand-induced conformational changes in the plant in contrast to Escherichia coli MTAN
5'-methylthiotubercidin
-
active site of apo-MTAN is more open, and greater conformational changes upon ligand binding in contrast to Arabidopsis MTAN1
5'-methylthiotubercidin
-
-
5'-methylthiotubercidin
-
competitive
5'-methylthiotubercidin
-
-
5'-methylthiotubercidin
-
-
9-[(1-Hydroxy-3-iodo-2-propoxy)methyl]adenine
-
-
9-[(1-Hydroxy-3-iodo-2-propoxy)methyl]adenine
-
competitive
adenine
-
-
adenine
-
competitive; strong
Formycin A
-
guanine
-
weak
hydrogen peroxide
-
reversible inactivation, 60% decrease of enzymatic activity at 0.5 mM hydrogen peroxide
hydrogen peroxide
reversible inactivation, 60% decrease of enzymatic activity at 0.5 mM hydrogen peroxide
iodoacetamide
-
reversal by dithiothreitol
iodoacetamide
-
no inhibition
iodoacetamide
only recombinant enzyme
iodoacetate
-
-
iodoacetate
-
no inhibition
iodoacetate
incorporation of 12 mol iodoactate per mol of enzyme
iodoacetate
only recombinant enzyme
p-chloromercuribenzoic acid
-
strong, partially reversed by dithiothreitol
p-chloromercuribenzoic acid
-
-
S-adenosyl-L-homocysteine
-
weak
S-adenosyl-L-homocysteine
no inhibition
SH-group blocking compounds
-
-
-
SH-group blocking compounds
-
inactivation
-
tert-butyl hydroperoxide
-
0.01 mM
tert-butyl hydroperoxide
0.01 mM
additional information
Tris buffer severely inhibits the nucleosidase reactions; Tris buffer severely inhibits the nucleosidase reactions
-
additional information
Tris buffer severely inhibits the nucleosidase reactions; Tris buffer severely inhibits the nucleosidase reactions
-
additional information
-
Tris buffer severely inhibits the nucleosidase reactions; Tris buffer severely inhibits the nucleosidase reactions
-
additional information
Caldariella acidophila
-
no effect by alkylating, mercaptide-forming or oxidizing thiol reagents
-
additional information
-
promotor hypermethylation strongly reduces enzyme expression
-
additional information
structural comparison of MTA phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design
-
additional information
-
structural comparison of MTA phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design
-
additional information
MTAP is inactivated in the liver of lipopolysaccharide-challenged mice
-
additional information
-
no inhibition by EDTA, putrescine, cadaverine
-
additional information
-
activity is not affected by alkylating, mercaptide-forming and oxidizing thiol reagents; no inhibition by S-adenosyl-L-methionine
-
additional information
activity is not affected by alkylating, mercaptide-forming and oxidizing thiol reagents; no inhibition by S-adenosyl-L-methionine
-
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0.0000018
(+/-)-cis-1-[(9-deazaadenin-9-yl)methyl]-4-ethyl-3-hydroxypyrrolidine
-
pH 7.4, 25°C
0.000002
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(1H-1,2,3-triazol-4-yl)pyrrolidine
-
pH 7.4, 25°C
0.0000007
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(penta-3-yl)pyrrolidine
-
pH 7.4, 25°C
0.000000047
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-isobutylpyrrolidine
-
pH 7.4, 25°C
0.00000084
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-4-ethyl-3-hydroxypyrrolidine
-
pH 7.4, 25°C
0.00000039
(+/-)-trans-1-[(9-deazaadenin-9-yl)methyl]-4-ethynyl-3-hydroxypyrrolidine
-
pH 7.4, 25°C
0.000000064
(+/-)-trans-4-(1-benzyl-1H-1,2,3-triazol-4-yl)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
pH 7.4, 25°C
0.000000059
(+/-)-trans-4-(cyclohexylmethyl)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyrrolidine
-
pH 7.4, 25°C
0.00000035
(+/-)-trans-4-allyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
pH 7.4, 25°C
0.000000009
(+/-)-trans-4-butyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
pH 7.4, 25°C
0.000000063
(+/-)-trans-4-cyclopropyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
pH 7.4, 25°C
0.000000054
(+/-)-trans-4-[3-(benzylthio)propyl]-1-[(9-deazaadenin-9-yl)-methyl]-3-hydroxypyrrolidine
-
pH 7.4, 25°C
0.000026
(1S)-1-(9-deazaadenin-9-yl)-1,4-di-deoxy-1,4-imino-5-methylthio-D-ribitol
pH 7.0, 25°C
0.00009
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-(1-naphthyl)thio-D-ribitol
-
pH 7.4, 25°C
0.00000139
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-(3-methylphenyl)thio-D-ribitol
-
pH 7.4, 25°C
0.0000044
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-(4-methylphenyl)thio-D-ribitol
-
pH 7.4, 25°C
0.000026
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-methylthio-D-ribitol
-
pH 7.4, 25°C
0.000134
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-O-methyl-D-ribitol
-
pH 7.4, 25°C
0.0000036
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-1,4-imino-5-phenylthio-D-ribitol
-
pH 7.4, 25°C
0.00002
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-5-(2-fluoroethyl)thio-1,4-imino-D-ribitol
-
pH 7.4, 25°C
0.000056
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-5-(2-hydroxyethyl)thio-1,4-imino-D-ribitol
-
pH 7.4, 25°C
0.0000064
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-5-(4-fluorophenyl)thio-1,4-imino-D-ribitol
-
pH 7.4, 25°C
0.0000092
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-5-ethylthio-1,4-imino-D-ribitol
-
pH 7.4, 25°C
0.000004
(1S)-1-(9-deazaadenin-9-yl)-1,4-dideoxy-5-n-propylthio-1,4-imino-D-ribitol
-
pH 7.4, 25°C
0.000044
(1S)-1-(9-deazaadenin-9-yl)-1,4-imino-1,4,5,6,7-penta-deoxy-D-ribo-heptitol
-
pH 7.4, 25°C
0.00072
(1S)-1-(9-deazaadenin-9-yl)-1,4-imino-1,4,5-trideoxy-D-ribitol
-
pH 7.4, 25°C
0.0000064
(1S)-1-(9-deazaadenin-9-yl)-5-(3-chlorophenyl)thio-1,4-dideoxy-1,4-imino-D-ribitol
-
pH 7.4, 25°C
0.000000576
(1S)-1-(9-deazaadenin-9-yl)-5-(4-chlorophenyl)thio-1,4-dideoxy-1,4-imino-D-ribitol
-
pH 7.4, 25°C
0.000026
(1S)-1-(9-deazaadenin-9-yl)-5-benzylthio-1,4-dideoxy-1,4-imino-D-ribitol
-
pH 7.4, 25°C
0.000085
(3R,4R)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxy-4-methoxymethylpyrrolidine
-
pH 7.5, 25°C
0.000022
(3R,4R)-4-(benzyloxymethyl)-1-[(9-deaza-adenin-9-yl)-methyl]-3-hydroxypyrrolidine
-
pH 7.5, 25°C
0.000055
(3R,4S)-1-[(8-aza-9-deazaadenin-9-yl)methyl]-4-benzylthiomethyl-3-hydroxypyrrolidine hydrochloride
-
pH 7.5, 25°C
0.0000013
(3R,4S)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxy-4-(1-propylthiomethyl)pyrrolidine
-
pH 7.5, 25°C
0.0000009
(3R,4S)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxy-4-(2-propylthiomethyl)pyrrolidine
-
pH 7.5, 25°C
0.000014
(3R,4S)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxy-4-(4-pyridylthiomethyl)pyrrolidine
-
pH 7.5, 25°C
0.0000015
(3R,4S)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxy-4-phenylthiomethylpyrrolidine
-
pH 7.5, 25°C
0.000002
(3R,4S)-1-[(9-deaza-adenin-9-yl)methyl]-4-(4-fluorophenylthiomethyl)-3-hydroxypyrrolidine
-
pH 7.5, 25°C
0.00000065
(3R,4S)-1-[(9-deaza-adenin-9-yl)methyl]-4-ethylthiomethyl-3-hydroxypyrrolidine
-
pH 7.5, 25°C
0.002
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(1-propyl)pyrrolidine
-
above, pH 7.5, 25°C
0.00000036 - 0.00000175
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(methylthiomethyl)pyrrolidine
0.0000017
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-methylthiomethylpyrrolidine
-
pH 7.5, 25°C
0.00000031
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-4-ethyl-3-hydroxypyrrolidine
-
pH 7.4, 25°C
0.00000028
(3R,4S)-4-(1-butylthiomethyl)-1-[(9-deaza-adenin-9-yl)-methyl]-3-hydroxypyrrolidine
-
pH 7.5, 25°C
0.00000081
(3R,4S)-4-(3-chlorophenylthiomethyl)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyrrolidine
-
pH 7.5, 25°C
0.000002
(3R,4S)-4-(4-chlorophenylthiomethyl)-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyrrolidine
-
pH 7.5, 25°C
0.0000014
(3R,4S)-4-benzylthiomethyl-1-[(9-deazaadenin-9-yl)-methyl]-3-hydroxypyrrolidine
-
pH 7.5, 25°C
0.0000000034
(3R,4S)-4-butyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
pH 7.4, 25°C
0.00000076
(3R,4S)-4-cyclohexylthiomethyl-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyrrolidine
-
pH 7.5, 25°C
0.0002 - 0.0007
2-bromo-9-(1,3-dihydroxy-2-propoxymethyl)adenine
-
-
0.001 - 0.01
2-bromo-9-(2-hydroxyethoxymethyl)adenine
-
-
0.0002 - 0.0007
2-chloro-9-(1,3-dihydroxy-2-propoxymethyl)adenine
-
-
0.001 - 0.01
2-chloro-9-(2-hydroxyethoxymethyl)adenine
-
-
0.0002 - 0.0007
2-iodo-9-(1,3-dihydroxy-2-propoxymethyl)adenine
-
-
0.001 - 0.01
2-iodo-9-(2-hydroxyethoxymethyl)adenine
-
-
0.00000001
5'-(4-chlorophenyl)thio-DADMe-immucillin A
-
pH and temperature not specified in the publication
0.000000086
5'-methylthio-DADMe-immucillin A
-
pH and temperature not specified in the publication
0.00000001
5'-methylthio-immucillin A
-
pH and temperature not specified in the publication
0.0083 - 0.031
5'-methylthiotubercidin
0.015
9-(phosphonoheptyl)adenine
-
low phosphate concentration of 3.5 mM
0.048
Formycin A
at 0.05 mM
0.000026
MT-ImmA
-
pH 7.5, 25°C
0.00000003
tert-butyl trans-3-hydroxy-4-vinylpyrrolidine-1-carboxylate
-
pH 7.4, 25°C
0.00000065
trans-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-vinylpyrrolidine
-
pH 7.4, 25°C
0.000000013
trans-4-cyclopentyl-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxypyrrolidine
-
pH 7.4, 25°C
0.00000036
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(methylthiomethyl)pyrrolidine
pH 7.0, 25°C
0.0000013
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(methylthiomethyl)pyrrolidine
pH 7.0, 25°C
0.00000175
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(methylthiomethyl)pyrrolidine
pH 7.0, 25°C
0.0083
5'-methylthiotubercidin
at 0.005 mM
0.031
5'-methylthiotubercidin
-
-
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Pegg, A.E.; Williams-Ashman, H.G.
Phosphate-stimulated breakdown of 5'-methylthioadenosine by rat ventral prostate
Biochem. J.
115
241-247
1969
Rattus norvegicus
brenda
Carteni'-Farina, M.; Oliva, A.; Romeo, G.; Napolitano, G.; De Rosa, M.; Gambacorta, A.; Zappia, V.
5'-Methylthioadenosine phosphorylase from Caldariella acidophila. Purification and properties
Eur. J. Biochem.
101
317-324
1979
Caldariella acidophila
brenda
Garbers, D.L.
Demonstration of 5'-methylthioadenosine phosphorylase activity in various rat tissues. Some properties of the enzyme from rat lung
Biochim. Biophys. Acta
523
82-93
1978
Rattus norvegicus
brenda
Lee, S.H.; Cho, Y.D.
Purification and properties of 5'-deoxy-5'methylthioadenosine phosphorylase from rat spleen
Korean Biochem. J.
26
433-439
1993
Rattus norvegicus
-
brenda
Cacciapuoti, G.; Porcelli, M.; Bertoldo, C.; Zappia, V.
Thermophilicity and thermostability of 5'-methylthioadenosine phosphorylase from Sulfolobus solfataricus
Life Chem. Rep.
10
75-81
1992
Saccharolobus solfataricus
-
brenda
Toorchen, D.; Miller, R.L.
Purification and characterization of 5'-deoxy-5'-methylthioadenosine (MTA) phosphorylase from human liver
Biochem. Pharmacol.
41
2023-2030
1991
Homo sapiens
brenda
Savarese, T.M.; Harrington, S.; Nakamura, C.; Chen, Z.H.; Kumar, P.; Mikkilineni, A.; Abushanab, E.; Chu, S.H.; Parks, R.E.
5'-Deoxy-5'-methylthioadenosine phosphorylase. V. Acycloadenosine derivatives as inhibitors of the enzyme
Biochem. Pharmacol.
40
2465-2471
1990
Homo sapiens, Mus musculus
brenda
Ghoda, L.Y.; Savarese, T.M.; Northup, C.H.; Parks, R.E.; Garofalo, J.; Katz, L.; Ellenbogen, B.B.; Bacchi, C.J.
Substrate specificities of 5'-deoxy-5'-methylthioadenosine phosphorylase from Trypanosoma brucei brucei and mammalian cells
Mol. Biochem. Parasitol.
27
109-118
1988
Trypanosoma brucei brucei
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