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Enzyme Nomenclature
Information on EC 2.4.2.28 - S-methyl-5'-thioadenosine phosphorylase
for references in articles please use BRENDA:EC2.4.2.28
Word Map on EC 2.4.2.28
- 2.4.2.28
- purine
-
polyamine
-
salvage
-
mtap-deficient
-
phosphorolysis
-
l-alanosine
-
codeletion
-
nucleosidase
-
enzyme-deficient
-
p14arf
-
p15ink4b
-
mtans
-
cdkn2b
-
phosphorylase-deficient
- 5-methylthioribose
- drug development
- 5'-deoxyadenosine
- analysis
- medicine
- diagnostics
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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EC NUMBER 
COMMENTARY 
2.4.2.28
-
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RECOMMENDED NAME
GeneOntology No.
S-methyl-5'-thioadenosine phosphorylase
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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
phosphorolytic mechanism
-
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
phosphorolytic mechanism
Caldariella acidophila
-
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
equilibrium-ordered reaction, 5'-methylthioadenosine is the first substrate to bind and 5-methylthioribose 1-phosphate is the first product to be released; phosphorolytic mechanism
-
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
sequential mechanism
-
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
ordered bisubstrate biproduct reaction with methylthioadenosine the first substrate to add and adenine the last product to leave the enzyme
-
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
sequential mechanism
Caldariella acidophila
-
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
phosphorolytic mechanism
-
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
active and substrate-binding sites, three-dimensional structures; 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; catalytic mechanism; subunit structure, model
-
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
-
S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pentosyl group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
61970-06-7
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
none of MTAN deletion mutants interact with calcineurin B-like 3
malfunction
-
mice homozygous for a MTAP null allele (MtaplacZ) have an embryonic lethal phenotype dying around day 8 postconception. Mtap/MtaplacZ heterozygotes are born at Mendelian frequencies and appear indistinguishable from wild-type mice during the first year of life, but tend to die prematurely with a median survival of 585 days. These animals have greatly enlarged spleens, altered thymic histology, and lymphocytic infiltration of their livers, consistent with lymphoma
malfunction
-
there is increased deoxyadenosine sensitivity in Trypanosoma brucei methylthioadenosine phosphorylase knockdown cells
malfunction
-
enzyme knockdown both genetically and pharmacologically, blocks androgen sensitive prostate cancer growth in vivo
malfunction
-
there is increased deoxyadenosine sensitivity in Trypanosoma brucei methylthioadenosine phosphorylase knockdown cells
-
physiological function
-
Mtap is essential during embryogenesis. Mtap is a tumor suppressor gene independent of CDKN2A and ARF
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
physiological function
-
the enzyme is associated with coronary artery disease risk in a Chinese Han population
physiological function
-
the enzyme protects Trypanosoma brucei from the antitrypanosomal effect of deoxyadenosine
physiological function
-
the enzyme protects Trypanosoma brucei from the antitrypanosomal effect of deoxyadenosine
-
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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
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-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-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'-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'-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'-iodo-5'-deoxyadenosine + phosphate
adenine + 5-iodo-5-deoxy-D-ribose 1-phosphate
-
-
-
-
r
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 + S-methyl-5-thio-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
-
-
-
-
?
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
-
-
?
S-adenosyl-L-homocysteine + phosphate
?
0.81% activity compared to activity with 5'-methylthioadenosine
-
-
?
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
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
-
-
-
-
?
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
-
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
-
-
-
?
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
-
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
-
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
-
-
-
-
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
-
-
-
-
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
2.1% activity compared to activity with 5'-methylthioadenosine
-
-
?
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
-
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
-
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
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
?
-
-
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.
NATURAL SUBSTRATES
NATURAL PRODUCTS
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'-(hydroxyethylthio)adenosine + phosphate
adenine + 5-hydroxyethylthio-D-ribose 1-phosphate
inosine + phosphate
hypoxanthine + D-ribose 1-phosphate
P50389
-
-
-
-
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
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
-
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
P50389
-
-
-
-
S-methyl-5'-thioadenosine + phosphate
adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
Q8YBL1
-
-
-
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
-
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
C6KFA4
-
-
-
?
additional information
?
-
Q13126
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
?
-
P50389
involved in the catabolism of 5'-methylthioadenosine, adenosine, guanosine and inosine
-
-
-
additional information
?
-
-
involved in the catabolism of 5'-methylthioadenosine, adenosine, guanosine and inosine
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
no requirement for metal ion, e.g. Mg2+, Mn2+ or Ca2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(+/-)-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-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-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-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-(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-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
-
-
5'-ethylthio-DADMe-ImmucillinA
-
inhibits quorum sensing induction completely at 0.001 mM
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
-
MT-ImmA
-
i.e. (3R,4S)-1-[(9-deazaadenin-9-yl)methyl]-3-hydroxy-4-methylthiomethylpyrrolidine
proteinase K
-
recombinant enzyme, 10% remaining activity after 4 h at 37°C, phosphate protects
-
Subtilisin
-
recombinant enzyme, 24% remaining activity after 4 h at 37°C, phosphate protects
-
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'-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
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
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
MTAP is inactivated in the liver of lipopolysaccharide-challenged mice
-
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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
imidazole buffer is the best buffer, whereas phosphate and HEPES buffers result in enzyme velocities that are only 50-60% of those for imidazole; imidazole buffer is the best buffer, whereas phosphate and HEPES buffers result in enzyme velocities that are only 50-60% of those for imidazole
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.009
5'-methylthioadenosine
pH and temperature not specified in the publication, co-substrate: 50 mM phosphate
0.024
5'-methylthioadenosine
-
recombinant enzyme; wild-type and recombinant enzyme
0.125
phosphate
-
recombinant enzyme; wild-type and recombinant enzyme
0.26
phosphate
pH and temperature not specified in the publication, co-substrate: 0.2 mM 5'-methylthioadenosine
0.0022
S-methyl-5'-thioadenosine
wild type enzyme, at pH 7.0 and 25°C
0.0031
S-methyl-5'-thioadenosine
mutant enzyme A15M, at pH 7.0 and 25°C
0.0044
S-methyl-5'-thioadenosine
mutant enzyme S167A, at pH 7.0 and 25°C
0.0045
S-methyl-5'-thioadenosine
mutant enzyme V34I, at pH 7.0 and 25°C
0.0048
S-methyl-5'-thioadenosine
mutant enzyme R85H, at pH 7.0 and 25°C
0.0053
S-methyl-5'-thioadenosine
mutant enzyme V34A, at pH 7.0 and 25°C
0.0054
S-methyl-5'-thioadenosine
mutant enzyme R85A, at pH 7.0 and 25°C; mutant enzyme W179A, at pH 7.0 and 25°C
0.0074
S-methyl-5'-thioadenosine
mutant enzyme W179F, at pH 7.0 and 25°C
0.028
S-methyl-5'-thioadenosine
mutant enzyme Y134A, at pH 7.0 and 25°C
0.0301
S-methyl-5'-thioadenosine
mutant enzyme Y134F, at pH 7.0 and 25°C
0.0351
S-methyl-5'-thioadenosine
mutant enzyme M144A, at pH 7.0 and 25°C
8
S-methyl-5'-thioadenosine
mutant enzyme R164A, at pH 7.0 and 25°C
additional information
additional information
-
nonlinear kinetics with 5'-methylthioadenosine, 2 Km-values, probably due to 2 enzyme activities or 2 interconvertible forms
-
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
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.26
phosphate
pH and temperature not specified in the publication, co-substrate: 0.2 mM 5'-methylthioadenosine
0.4
5'-methylthioadenosine
pH and temperature not specified in the publication, co-substrate: 50 mM phosphate
0.51
S-methyl-5'-thioadenosine
mutant enzyme M144A, at pH 7.0 and 25°C
0.58
S-methyl-5'-thioadenosine
mutant enzyme S167A, at pH 7.0 and 25°C; mutant enzyme W179F, at pH 7.0 and 25°C
0.69
S-methyl-5'-thioadenosine
mutant enzyme W179A, at pH 7.0 and 25°C
0.71
S-methyl-5'-thioadenosine
mutant enzyme Y134F, at pH 7.0 and 25°C
0.78
S-methyl-5'-thioadenosine
mutant enzyme Y134A, at pH 7.0 and 25°C
1.3
S-methyl-5'-thioadenosine
mutant enzyme R85H, at pH 7.0 and 25°C
1.4
S-methyl-5'-thioadenosine
mutant enzyme R85A, at pH 7.0 and 25°C
1.8
S-methyl-5'-thioadenosine
mutant enzyme A15M, at pH 7.0 and 25°C
2.5
S-methyl-5'-thioadenosine
mutant enzyme V34I, at pH 7.0 and 25°C
2.7
S-methyl-5'-thioadenosine
mutant enzyme V34A, at pH 7.0 and 25°C
8
S-methyl-5'-thioadenosine
mutant enzyme R164A, at pH 7.0 and 25°C
8.8
S-methyl-5'-thioadenosine
wild type enzyme, at pH 7.0 and 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15
S-methyl-5'-thioadenosine
mutant enzyme M144A, at pH 7.0 and 25°C
24
S-methyl-5'-thioadenosine
mutant enzyme Y134F, at pH 7.0 and 25°C
28
S-methyl-5'-thioadenosine
mutant enzyme Y134A, at pH 7.0 and 25°C
79
S-methyl-5'-thioadenosine
mutant enzyme W179F, at pH 7.0 and 25°C
130
S-methyl-5'-thioadenosine
mutant enzyme S167A, at pH 7.0 and 25°C; mutant enzyme W179A, at pH 7.0 and 25°C
250
S-methyl-5'-thioadenosine
mutant enzyme R85A, at pH 7.0 and 25°C
280
S-methyl-5'-thioadenosine
mutant enzyme R85H, at pH 7.0 and 25°C
510
S-methyl-5'-thioadenosine
mutant enzyme V34A, at pH 7.0 and 25°C
560
S-methyl-5'-thioadenosine
mutant enzyme V34I, at pH 7.0 and 25°C
580
S-methyl-5'-thioadenosine
mutant enzyme A15M, at pH 7.0 and 25°C
600
S-methyl-5'-thioadenosine
mutant enzyme R164A, at pH 7.0 and 25°C
4000
S-methyl-5'-thioadenosine
wild type enzyme, at pH 7.0 and 25°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.00000003
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
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000001
5'-butylthio-DADMe-ImmucillinA
Vibrio harveyi
-
suppression of light induction in strain BB120
0.000000014
5'-butylthio-DADMe-ImmucillinA
Vibrio harveyi
-
suppression of light induction in strain BB170
0.000125
5'-butylthio-DADMe-ImmucillinA
Escherichia coli
-
in 50 mM phosphate buffer, pH 7.9, 10 mM KCl, at 25°C, inhibition of autoinducer-2 production
0.00000011
5'-ethylthio-DADMe-ImmucillinA
Vibrio harveyi
-
suppression of light induction in strain BB170
0.00000014
5'-ethylthio-DADMe-ImmucillinA
Vibrio harveyi
-
suppression of light induction in strain BB120
0.000025
5'-methylthio-DADMe-immucillin A
Mycobacterium tuberculosis
O06401
pH and temperature not specified in the publication, in the presence of 10 microM 5'-methylthioadenosine
0.000075
5'-methylthio-DADMe-immucillin A
Mycobacterium tuberculosis
O06401
pH and temperature not specified in the publication, in the presence of 100 microM 5'-methylthioadenosine
0.000000105
5'-methylthio-DADMe-ImmucillinA
Vibrio harveyi
-
suppression of light induction in strain BB120
0.00000094
5'-methylthio-DADMe-ImmucillinA
Vibrio harveyi
-
suppression of light induction in strain BB170
0.0006
5'-methylthio-DADMe-ImmucillinA
Escherichia coli
-
in 50 mM phosphate buffer, pH 7.9, 10 mM KCl, at 25°C, inhibition of autoinducer-2 production
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.092
-
partially purified enzyme, forward reaction, substrate 5'-methylthioadenosine
0.17
-
substrate 5'-methyladenosine or 5'-deoxy-5'-(hydroxyethylthio)adenosine
0.365
-
substrate 5'-deoxy-5'-(hydroxyethylthio)adenosine, preincubation with substrate
2.12
5.28
-
70°C, pH 7.4, mutant enzyme C259S/C261S/C262S/C200S/C205S/C138S/C164S
6.24
-
70°C, pH 7.4, mutant enzyme C259S/C261S/C262S/C200S/C205S/C138S
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.2
7.4
7.4
7.5
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9
pH 6.5: about 55% of maximal activity, pH 9.0: about 55% of maximal activity
6.5 - 8.5
-
considerable decrease of activity below pH 6.5 and above pH 8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
70
80
114
-
mutant enzyme C259S/C261S/C262S/C200S/C205S and mutant enzyme C259S/C261S/C262S
120
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 120
-
60°C: about 40% of maximal activity, 120°C: about 40% of maximal activity, recombinant enzyme
86 - 95
90 - 130
-
90°C: about 50% of maximal activity, 130°C: about 70% of maximal activity
95 - 140
-
95°C: about 50% of maximal activity, 140°C: about 45% of maximal activity, wild-type enzyme
86 - 95
Caldariella acidophila
-
86°C: 50% of activity maximum, 95°C: activity maximum, no activity at 40°C
86 - 95
-
2 different activation energy-dependent processes occur below and above 100°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.7
-
isoelectric focusing on polyacrylamide gel in the pH ranges 3-10 and 4.5-6.0
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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 is deficient in patients with T-cell acute lymphoblastic leukemia, no activity in enzyme-deficient CEM cells
additional information
-
enzyme defect is associated with but not responsible for methionine-dependent tumor cell growth
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
-
immunohistochemical enzyme expression analysis in tumor tissues, overview
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
localized at the plasma membrane, in the cytoplasm and in the nucleus of transgenic tobacco plants. Abundant in the membrane structure and weak in the cytoplasm of onion epidermal cells
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27000
30000