Any feedback?
Information on EC 2.4.2.28 - S-methyl-5'-thioadenosine phosphorylase and Organism(s) Homo sapiens and UniProt Accession Q13126
for references in articles please use BRENDA:EC2.4.2.28Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.4.2.28 S-methyl-5'-thioadenosine phosphorylaseIUBMB Comments
Also acts on 5'-deoxyadenosine and other analogues having 5'-deoxy groups.
Specify your search results
Word Map
- 2.4.2.28
- purine
- polyamine
-
salvage
-
mtap-deficient
-
cdkn2a
- mesothelioma
-
phosphorolysis
-
mesothelial
- nucleosidase
-
codeleted
-
l-alanosine
-
co-deletion
-
mtap-deleted
-
phosphorylase-deficient
- p15ink4b
- 5'-deoxyadenosine
- 5-methylthioribose
-
mtans
-
p14arf
-
enzyme-deficient
- diagnostics
- drug development
- medicine
- analysis
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
methylthioadenosine phosphorylase, 5'-methylthioadenosine phosphorylase, mta phosphorylase, mtap protein, 5'-deoxy-5'-methylthioadenosine phosphorylase, ssmtapii, ssmtap, mtapase, mesado phosphorylase, pfmtap, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-deoxy-5'-methylthioadenosine phosphorylase
5'-methylthioadenosine nucleosidase
-
-
-
-
5'-methylthioadenosine phosphorylase
MeSAdo phosphorylase
-
-
-
-
MeSAdo/Ado phosphorylase
-
-
-
-
methylthioadenosine nucleoside phosphorylase
-
-
-
-
methylthioadenosine phosphorylase
MTA phosphorylase
-
-
-
-
MTAP
-
-
MTAPase
-
-
-
-
phosphorylase, methylthioadenosine
-
-
-
-
5'-deoxy-5'-methylthioadenosine phosphorylase
-
-
-
-
5'-methylthioadenosine phosphorylase
-
-
-
-
methylthioadenosine phosphorylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
catalytic mechanism
-
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
active and substrate-binding sites, three-dimensional structures
-
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
phosphorolytic mechanism
-
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
3 binding sites between substrate and enzyme
-
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
transition state structure, computational modeling of the transition state, overview
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-methyl-5'-thioadenosine:phosphate S-methyl-5-thio-alpha-D-ribosyl-transferase
Also acts on 5'-deoxyadenosine and other analogues having 5'-deoxy groups.
CAS REGISTRY NUMBER
COMMENTARY
61970-06-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 5-methylthio-D-ribose 1-phosphate
-
-
-
?
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-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
-
low activity
-
-
r
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
3'-deoxy-5'-deoxy-5'-methylthioadenosine + phosphate
adenine + 3-deoxy-5-thio-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'-(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'-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'-ethylthioadenosine + phosphate
adenine + 5-ethylthio-D-ribose 1-phosphate
-
60% of the activity with 5'-methylthioadenosine
-
-
?
5'-iodo-5'-deoxyadenosine + phosphate
adenine + 5-iodo-5-deoxy-D-ribose 1-phosphate
-
-
-
-
r
5'-methylselenoadenosine + phosphate
adenine + 5-methylseleno-D-ribose 1-phosphate
-
95% of the activity with 5'-methylthioadenosine
-
-
?
5'-methylthioinosine + phosphate
hypoxanthine + 5-methylthio-alpha-D-ribose 1-phosphate
-
8.9% of the reaction with 5'-methylthioadenosine
-
-
?
5'-phenyladenosine + phosphate
adenine + 5-phenyl-D-ribose 1-phosphate
-
-
-
-
?
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
-
-
?
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
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
structural comparison of MTA phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design
-
-
?
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
-
-
-
?
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'-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
-
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
-
-
?
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
-
-
?
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
?
-
-
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
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
?
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
-
-
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1S)-1-(9-deazaadenin-9-yl)-1,4-di-deoxy-1,4-imino-5-methylthio-D-ribitol
-
(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
-
(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-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)-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
-
-
(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-methylthiomethylpyrrolidine
-
-
(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-cyclohexylthiomethyl-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyrrolidine
-
-
hydrogen peroxide
-
reversible inactivation, 60% decrease of enzymatic activity at 0.5 mM hydrogen peroxide
MT-ImmA
-
i.e. (3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-methylthiomethylpyrrolidine
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
-
promotor hypermethylation strongly reduces enzyme expression
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic isotope effects measured on the arsenolysis of 5'-methylthioadenosine catalyzed by the enzyme, the enzyme has a dissociative SN1 transition state with its cationic center at the anomeric carbon and insignificant bond order to the leaving group, the transition state has cationic character at the anomeric carbon and is anionic at the 3'-OH oxygen with an anionic leaving group, late SN1 transition state with significant participation of the phosphate nucleophile, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000026
(1S)-1-(9-deazaadenin-9-yl)-1,4-di-deoxy-1,4-imino-5-methylthio-D-ribitol
pH 7.0, 25°C
0.00000036 - 0.00000175
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-(methylthiomethyl)pyrrolidine
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
0.0000017
(3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-methylthiomethylpyrrolidine
-
pH 7.5, 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
0.00000076
(3R,4S)-4-cyclohexylthiomethyl-1-[(9-deaza-adenin-9-yl)methyl]-3-hydroxypyrrolidine
-
pH 7.5, 25°C
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
0.00000036
(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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.092
-
partially purified enzyme, forward reaction, substrate 5'-methylthioadenosine
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
diffuse histiocytic lymphoma cell line, possesses no enzyme activity, but intact gene
-
SK-Ml-28 cell line derived from metastases of malignant melanomas
-
CD34+ erythroid burst-forming unit, granulocyte/monocyte colony-forming unit, granulocyte/erythrocyte/macrophage/megakaryocyte colony-forming unit progenitors and primitive high proliferative potential colony-forming cells in the purified CD34+ cells are cultured
additional information
additional information
enzyme deficiency in malignant cells, partial or total deletions in the gene of leukemia cell lines of patients with T-cell acute lymphoblastic leukemia
additional information
-
enzyme deficiency in malignant cells, partial or total deletions in the gene of leukemia cell lines of patients with T-cell acute lymphoblastic leukemia
additional information
-
strongly reduced expression in all melanoma cell lines due to promotor hypermethylation, no enzyme content and expression in melanoma cell line HTZ19d
additional information
-
enzyme defect is associated with but not responsible for methionine-dependent tumor cell growth
additional information
-
enzyme is deficient in patients with T-cell acute lymphoblastic leukemia, no activity in enzyme-deficient CEM cells
additional information
-
immunohistochemical enzyme expression analysis in tumor tissues, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
enzyme knockdown both genetically and pharmacologically, blocks androgen sensitive prostate cancer growth in vivo
physiological function
the enzyme is associated with coronary artery disease risk in a Chinese Han population
physiological function
-
MTAP substrates protect MTAP-positive cells from toxicity of adenine analogs 2,6-diaminopurine, 6-methylpurine, and 2-fluoroadenine and clinical cancer drugs 5-fluorouracil or 6-thioguanine. Adenine analog plus 5'-methylthioadenosine, kills MTAP-negative A549 lung tumor cells, while MTAP-positive human fibroblasts are protected, whereas in co-cultures of the breast tumor cell line, MCF-7, and HF cells, MCF-7 is inhibited or killed, while HF cells proliferate robustly
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MTAP_HUMAN
283
0
31236
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
trimer
additional information
additional information
-
overall and active site structure, trimer of 3 identical subunits
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of apo MTAP and MTAP in complex with p-Cl-PhT-DADMe-ImmA are determined at 1.9 and 2.0 A resolution, respectively. Inhibitor binding causes condensation of the enzyme active site, reorganization at the trimer interfaces, the release of water from the active sites and subunit interfaces, and compaction of the trimeric structure. These structural changes cause the entropy-favored binding of transition state analogues
X-ray structure with (1S)-1-(9-deazaadenin-9-yl)-1,4-di-deoxy-1,4-imino-5-methylthio-D-ribitol
from recombinant enzyme, hanging drop-vapour diffusion method, protein 25 mg/ml, 10 mM Tris-HCl, pH 7.4, 5 mM DTT, 0.4 M NaCl against reservoir solution of 80 mM MES, pH 5.9, 5 mM DTT, 12% w/v polyethylene glycol 6000, 25% v/v ethylene glycol, in presence of substrates adenine, phosphate and sulfate, structure analysis by X-ray diffraction at light scattering
-
in complex with 5'-methylthio-DADMe-immucillin A, 5'-butylthio-DADMe-immucillin A, 5'-propylthio-immucillin A or 5'-methylthio-tubercidin, sitting drop vapor diffusion method, using 0.2 M magnesium chloride, 0.1 M sodium citrate:citric acid (pH 5.5), and 40% (w/v) PEG 400 for 5'-methylthio-DADMe-immucillin A or 5'-propylthio-immucillin A, 3 M sodium chloride and 0.1 M sodium acetate (pH 4.5) for BT-DADMe-immucillin A, and 0.2 M magnesium chloride and 20% (w/v) PEG 3350 for 5'-methylthio-tubercidin
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
V56I
-
natural polymorphism present in 7 of 9 melanoma cell lines, not in SK-Mel-28 and in HTZ19d
additional information
additional information
-
cell line DHL-9 contains a promotor sequence with a deletion of 14 bases, the deletion mutant allele is widespread throughout the japanese population and not responsible for the enzyme deficiency in this cell line
additional information
-
melanoma cell line HTZ19d is a deletion mutant without enzyme expression and activity
additional information
-
knockdown of Mtap protein by RNA interference in L-alanosine-resistant HuCCT1 cells conferred sensitivity to this agent, L-alanosine shows robust growth inhibition in MTAP-negative biliary cancer cell lines CAK-1 and GBD-1 accompanied by striking depletion of intracellular ATP and failure to rescue this depletion via addition of exogenous methylthioadenosine, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
resistance to thermal inactivation is increased remarkably by addition of 5'-methylthioadenosine or phosphate
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
rapid inactivation in absence of reducing agents: 50% inactivation within 24 h at both 4°C and -20°C
-
resistance to thermal inactivation is increased remarkably by addition of 5'-methylthioadenosine or phosphate
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 5 mM DTT, 50 mM potassium phosphate, pH 7.4, less than 10% loss of activity after 1 month
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
from cells of patients with T-cell acute lymphoblastic leukemia, DNA sequence analysis, 9p21 chromosome, topologic map
gene MTAP, located f100 kb telomeric to the p16INK4A/CDKN2A gene on chromosome 9p21, expression in HuCCT1 and SNU308 cell lines, the enzyme expression does not affect the cells
-
quantitative PCR, RNA mutational analysis, analysis of methylation status of the enzymes promotor
-
the gene maps on the 9p21 chromosome, strictly linked to the tumor suppressor gene p16INK4A, functional expression in Escherichia coli strain JM105
-
wild-type and promotor deletion mutant, expression in HeLa cells, luciferase reporter assay
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
methylthioadenosine phosphorylase protein expression may be a predictive marker of interferon therapy resistance in patients with melanoma and disease progression
diagnostics
-
methylthioadenosine phosphorylase protein expression may be a predictive marker of interferon therapy resistance in patients with melanoma and disease progression
drug development
medicine
drug development
-
combination of 5'-methylthioadenosine with clinical cancer drugs 5-fluorouracil or 6-thioguanine, in the treatment of MTAP-negative tumors, may produce a significantly improved therapeutic index
drug development
-
loss of MTAP activity in a subset of chordomas suggests that this group of patients may benefit from chemoselective inhibition of the de novo purine synthesis pathway. Purine synthesis inhibitors may be considered for chordoma patients with MTAP-deficient tumours
medicine
-
gene is linked to the important tumor suppressor gene p16INK4A, enzyme is of key importance in defining the chromosomal area homozygously deleted in a large number of human tumors, absence of enzyme activity only in malignant cells is of great value in developing selective antitumor therapeutic strategies
medicine
-
possibility of targeting the enzyme in the design of an enzyme-selective therapy for patients with T-cell acute lymphoblastic leukemia and other enzyme-deficient malignancies
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
White, M.W.; Vandenbark, A.A.; Barney, C.L.; Ferro, A.J.
Structural analogs of 5'-methylthioadenosine as substrates and inhibitors of 5'-methylthioadenosine phosphorylase and as inhibitors of human lymphocyte transformation
Biochem. Pharmacol.
31
503-507
1982
Homo sapiens
Zappia, V.; Oliva, A.; Cacciapuoti, G.; Galletti, P.; Mignucci, G.; Carteni-Farina, M.
Substrate specificity of 5'-methylthioadenosine phosphorylase from human prostate
Biochem. J.
175
1043-1050
1978
Homo sapiens
Della Ragione, F.; Carteni-Farina, M.; Gragnaniello, V.; Schettino, M.I.; Zappia, V.
Purification and characterization of 5'-deoxy-5'-methylthioadenosine phosphorylase from human placenta
J. Biol. Chem.
261
12324-12329
1986
Homo sapiens
Fabianowska-Majewska, K.; Duley, J.; Fairbanks, L.; Simmonds, A.; Wasiak, T.
Substrate specificity of methylthioadenosine phosphorylase from human liver
Acta Biochim. Pol.
41
391-395
1994
Homo sapiens
Della Ragione, F.; Takabayashi, K.; Mastropietro, S.; Mercurio, C.; Oliva, A.; Russo, G.L.; Della Pietra, V.; Borriello, A.; Nobori, T.; et al.
Purification and characterization of recombinant human 5'-methylthioadenosine phosphorylase: definite identification coding cDNA
Biochem. Biophys. Res. Commun.
223
514-519
1996
Homo sapiens
Nobori, T.; Takabayashi, K.; Tran, P.; Orvis, L.; Batova, A.; Yu, A.L.; Carson, D.A.
Genomic cloning of methylthioadenosine phosphorylase: a purine metabolic enzyme deficient in multiple different cancers
Proc. Natl. Acad. Sci. USA
93
6203-6208
1996
Homo sapiens (Q13126), Homo sapiens
Yu, J.; Batova, A.; Shao, L.e.; Carrera, C.J.; Yu, A.L.
Presence of methylthioadenosine phosphorylase (MTAP) in hematopoietic stem/progenitor cells: its therapeutic implication for MTAP (-) malignancies
Clin. Cancer Res.
3
433-438
1997
Homo sapiens
Appleby, T.C.; Erion, M.D.; Ealick, S.E.
The structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase at 1.7 A resolution provides insights into substrate binding and catalysis
Structure
7
629-641
1999
Homo sapiens
Slominska, E.M.; Kalsi, K.K.; Yacoub, M.H.; Smolenski, R.T.
The role of 5'-deoxy-5'-methyl thioadenosine phosphorylase in cardiac adenosine breakdown and adenine production
Adv. Exp. Med. Biol.
486
159-162
2000
Homo sapiens, Rattus norvegicus, Rattus norvegicus Wistar, Sus scrofa
Tang, B.; Li, Y.N.; Kruger, W.D.
Defects in methylthioadenosine phosphorylase are associated with but not responsible for methionine-dependent tumor cell growth
Cancer Res.
60
5543-5547
2000
Homo sapiens
Behrmann, I.; Wallner, S.; Komyod, W.; Heinrich, P.C.; Schuierer, M.; Buettner, R.; Bosserhoff, A.K.
Characterization of methylthioadenosin phosphorylase (MTAP) expression in malignant melanoma
Am. J. Pathol.
163
683-690
2003
Homo sapiens
Kadariya, Y.; Nishioka, J.; Nakatani, K.; Nakashima, K.; Nobori, T.
Deletion of dinucleotide repeat (DELTA14 allele) in the methylthioadenosine phosphorylase (MTAP) promoter and the allelotype of MTAP promoter in the Japanese population
Jpn. J. Cancer Res.
93
369-373
2002
Homo sapiens
Lee, J.E.; Settembre, E.C.; Cornell, K.A.; Riscoe, M.K.; Sufrin, J.R.; Ealick, S.E.; Howell, P.L.
Structural comparison of MTA phosphorylase and MTA/AdoHcy nucleosidase explains substrate preferences and identifies regions exploitable for inhibitor design
Biochemistry
43
5159-5169
2004
Homo sapiens (Q13126), Homo sapiens
Singh, V.; Shi, W.; Evans, G.B.; Tyler, P.C.; Furneaux, R.H.; Almo, S.C.; Schramm, V.L.
Picomolar transition state analogue inhibitors of human 5'-methylthioadenosine phosphorylase and X-ray structure with MT-immucillin-A
Biochemistry
43
9-18
2004
Homo sapiens (Q13126), Homo sapiens
Kung, P.P.; Zehnder, L.R.; Meng, J.J.; Kupchinsky, S.W.; Skalitzky, D.J.; Johnson, M.C.; Maegley, K.A.; Ekker, A.; Kuhn, L.A.; Rose, P.W.; Bloom, L.A.
Design, synthesis, and biological evaluation of novel human 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP) substrates
Bioorg. Med. Chem. Lett.
15
2829-2833
2005
Homo sapiens
Evans, G.B.; Furneaux, R.H.; Schramm, V.L.; Singh, V.; Tyler, P.C.
Targeting the polyamine pathway with transition-state analogue inhibitors of 5'-methylthioadenosine phosphorylase
J. Med. Chem.
47
3275-3281
2004
Homo sapiens
Wild, P.J.; Meyer, S.; Bataille, F.; Woenckhaus, M.; Ameres, M.; Vgt, T.; Landthaler, M.; Pauer, A.; Klinkhammer-Schalke, M.; Hofstaedter, F.; Bosserhoff, A.K.
Tissue microarray analysis of methylthioadenosine phosphorylase protein expression in melanocytic skin tumors
Arch. Dermatol.
142
471-476
2006
Homo sapiens
Singh, V.; Schramm, V.L.
Transition-state structure of human 5-methylthioadenosine phosphorylase
J. Am. Chem. Soc.
128
14691-14696
2006
Homo sapiens
Evans, G.B.; Furneaux, R.H.; Lenz, D.H.; Painter, G.F.; Schramm, V.L.; Singh, V.; Tyler, P.C.
Second generation transition state analogue inhibitors of human 5-methylthioadenosine phosphorylase
J. Med. Chem.
48
4679-4689
2005
Homo sapiens
Karikari, C.A.; Mullendore, M.; Eshleman, J.R.; Argani, P.; Leoni, L.M.; Chattopadhyay, S.; Hidalgo, M.; Maitra, A.
Homozygous deletions of methylthioadenosine phosphorylase in human biliary tract cancers
Mol. Cancer Ther.
4
1860-1866
2005
Homo sapiens
Parker, W.B.; Allan, P.W.; Ealick, S.E.; Sorscher, E.J.; Hassan, A.E.; Silamkoti, A.V.; Fowler, A.T.; Waud, W.R.; Secrist, J.A.
Design and evaluation of 5-modified nucleoside analogs as prodrugs for an E. coli purine nucleoside phosphorylase mutant
Nucleosides Nucleotides Nucleic Acids
24
387-392
2005
Homo sapiens
Williamson, R.E.; Darrow, K.N.; Michaud, S.; Jacobs, J.S.; Jones, M.C.; Eberl, D.F.; Maas, R.L.; Liberman, M.C.; Morton, C.C.
Methylthioadenosine phosphorylase (MTAP) in hearing: gene disruption by chromosomal rearrangement in a hearing impaired individual and model organism analysis
Am. J. Med. Genet. A
143A
1630-1639
2007
Homo sapiens (Q13126)
Alhebshi, H.M.; Pant, I.; Kaur, G.; Hashim, H.; Mabruk, M.J.
Methylthioadenosine phosphorylase expression in cutaneous squamous cell carcinoma
Asian Pac. J. Cancer Prev.
9
291-294
2008
Homo sapiens
Fernandez-Irigoyen, J.; Santamaria, M.; Sanchez-Quiles, V.; Latasa, M.U.; Santamaria, E.; Munoz, J.; Sanchez Del Pino, M.M.; Valero, M.L.; Prieto, J.; Avila, M.A.; Corrales, F.J.
Redox regulation of methylthioadenosine phosphorylase in liver cells: molecular mechanism and functional implications
Biochem. J.
411
457-465
2008
Homo sapiens, Mus musculus (Q9CQ65)
Miyazaki, S.; Nishioka, J.; Shiraishi, T.; Matsumine, A.; Uchida, A.; Nobori, T.
Methylthioadenosine phosphorylase deficiency in Japanese osteosarcoma patients
Int. J. Oncol.
31
1069-1076
2007
Homo sapiens
Basu, I.; Cordovano, G.; Das, I.; Belbin, T.J.; Guha, C.; Schramm, V.L.
A transition state analogue of 5-methylthioadenosine phosphorylase induces apoptosis in head and neck cancers
J. Biol. Chem.
282
21477-21486
2007
Homo sapiens
Watanabe, F.; Takao, M.; Inoue, K.; Nishioka, J.; Nobori, T.; Shiraishi, T.; Kaneda, M.; Sakai, T.; Yada, I.; Shimpo, H.
Immunohistochemical diagnosis of methylthioadenosine phosphorylase (MTAP) deficiency in non-small cell lung carcinoma
Lung Cancer
63
39-44
2008
Homo sapiens
Sommer, J.; Itani, D.M.; Homlar, K.C.; Keedy, V.L.; Halpern, J.L.; Holt, G.E.; Schwartz, H.S.; Coffin, C.M.; Kelley, M.J.; Cates, J.M.
Methylthioadenosine phosphorylase and activated insulin-like growth factor-1 receptor/insulin receptor: potential therapeutic targets in chordoma
J. Pathol.
220
608-617
2010
Homo sapiens
Lubin, M.; Lubin, A.
Selective killing of tumors deficient in methylthioadenosine phosphorylase: a novel strategy
PLoS ONE
4
e5735
2009
Homo sapiens
Guan, R.; Ho, M.C.; Brenowitz, M.; Tyler, P.C.; Evans, G.B.; Almo, S.C.; Schramm, V.L.
Entropy-driven binding of picomolar transition state analogue inhibitors to human 5-methylthioadenosine phosphorylase
Biochemistry
50
10408-10417
2011
Homo sapiens (Q13126), Homo sapiens
Guan, R.; Tyler, P.C.; Evans, G.B.; Schramm, V.L.
Thermodynamic analysis of transition-state features in picomolar inhibitors of human 5'-methylthioadenosine phosphorylase
Biochemistry
52
8313-8322
2013
Homo sapiens (Q13126), Homo sapiens
Lv, X.; Zhang, Y.; Rao, S.; Su, D.; Feng, D.; Wang, M.; Li, X.; Li, D.; Guo, H.; Zuo, X.; Xia, M.; Ouyang, H.; Ling, W.; Qiu, J.
Association between rs10118757(A/G) in methylthioadenosine phosphorylase gene and coronary artery disease in Chinese Hans
Gene
526
344-346
2013
Homo sapiens (Q13126), Homo sapiens
Bistulfi, G.; Affronti, H.C.; Foster, B.A.; Karasik, E.; Gillard, B.; Morrison, C.; Mohler, J.; Phillips, J.G.; Smiraglia, D.J.
The essential role of methylthioadenosine phosphorylase in prostate cancer
Oncotarget
7
14380-14393
2016
Homo sapiens (Q13126), Homo sapiens
Becker, A.P.; Scapulatempo-Neto, C.; Menezes, W.P.; Clara, C.; Machado, H.R.; Oliveira, R.S.; Neder, L.; Reis, R.M.
Expression of methylthioadenosine phosphorylase (MTAP) in pilocytic astrocytomas
Pathobiology
82
84-89
2015
Homo sapiens
Czech, B.; Dettmer, K.; Valletta, D.; Saugspier, M.; Koch, A.; Stevens, A.P.; Thasler, W.E.; Mueller, M.; Oefner, P.J.; Bosserhoff, A.K.; Hellerbrand, C.
Expression and function of methylthioadenosine phosphorylase in chronic liver disease
PLoS ONE
8
e80703
2013
Homo sapiens
EXTERNAL LINKS (specific for EC-Number 2.4.2.28)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
