Information on EC 3.3.1.1 - adenosylhomocysteinase and Organism(s) Homo sapiens

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


The taxonomic range for the selected organisms is: Homo sapiens

EC NUMBER
COMMENTARY hide
3.3.1.1
-
RECOMMENDED NAME
GeneOntology No.
adenosylhomocysteinase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioether
-
-
-
-
synthesis of thioether
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-methionine degradation I (to L-homocysteine)
-
-
S-adenosyl-L-methionine cycle II
-
-
methionine metabolism
-
-
Cysteine and methionine metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-homocysteine hydrolase
The enzyme contains one tightly bound NAD+ per subunit. This appears to bring about a transient oxidation at C-3' of the 5'-deoxyadenosine residue, thus labilizing the thioether bond [2] (for mechanism, click here), cf. EC 5.5.1.4, inositol-3-phosphate synthase.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-54-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
treatment with 50 microg/ml N-nitrosomethylbenzylamine results in twenty-eight differentially expressed protein spots in HEEC cells. Two tumor suppressor proteins, prohibitin and c-Myc binding protein, are down-regulated in NMBA-treated HEEC cells. S-adenosylhomocysteine hydrolase, is up-regulated in NMBA-treated HEEC cells
physiological function
-
the enzyme can promote apoptosis, inhibit migration and adhesion of esophageal squamous cell carcinoma cells suggesting that it may be involved in carcinogenesis of the esophagus
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4',5'-dehydroadenosine + H2O
adenosine
show the reaction diagram
-
favors formation of 4',5'-dehydroadenosine, precursor reaction
-
r
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine
show the reaction diagram
DL-homocysteine + adenosine
S-adenosyl-DL-homocysteine + H2O
show the reaction diagram
L-homocysteine + adenosine + H2O
S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
-
r
S-adenosyl-DL-homocysteine + H2O
DL-homocysteine + adenosine
show the reaction diagram
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
show the reaction diagram
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
show the reaction diagram
S-adenosyl-L-homocysteine + H2O
S-inosyl-L-homocysteine + NH3
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-homocysteine + adenosine + H2O
S-adenosyl-L-homocysteine
show the reaction diagram
-
-
-
-
r
S-adenosyl-L-homocysteine + H2O
adenosine + L-homocysteine
show the reaction diagram
S-adenosyl-L-homocysteine + H2O
L-homocysteine + adenosine
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R,2S,3R)-3-(6-amino-4,5-dihydro-9H-purin-9-yl)cyclopentane-1,2-diol
-
-
(1R,2S,3R,5R)-3-(6-amino-4,5-dihydro-9H-purin-9-yl)-5-(hydroxymethyl)cyclopentane-1,2-diol
-
-
(1R,2S,3S)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-4-fluorocyclopentane-1,2-diol
-
-
(1R,2S,3S)-3-(8-aminoimidazo[1,2-a]pyrazin-3-yl)cyclopentane-1,2-diol
-
-
(1R,2S,3S,5S)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-5-methylcyclopentane-1,2-diol
-
-
(1R,2S,4r)-4-(4-amino-6,7-difluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
-
-
(1R,2S,4r)-4-(4-amino-6-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
-
-
(1R,2S,4r)-4-(4-amino-7-chloro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
-
-
(1R,2S,4r)-4-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
-
-
(1R,2S,4r)-4-(4-amino-7-methyl-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
-
-
(1R,2S,4r)-4-(6-amino-2-fluoro-9H-purin-9-yl)cyclopentane-1,2-diol
-
-
(1S,2R,3S,4S)-4-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2,3-triol
-
-
(1S,2R,5R)-5-(6-amino-4,5-dihydro-9H-purin-9-yl)-3-(chloromethyl)cyclopent-3-ene-1,2-diol
-
-
(1S,2R,5R)-5-(6-amino-4,5-dihydro-9H-purin-9-yl)cyclopent-3-ene-1,2-diol
-
-
(1S,2R,5S)-5-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-4-fluorocyclopent-3-ene-1,2-diol
-
-
(1S,2R,5S)-5-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopent-3-ene-1,2-diol
-
-
(1S,2S,3S,5S)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-5-fluorocyclopentane-1,2-diol
-
-
(E)-6-chloro-6-cyano-5,6-didehydro-6-deoxyhomoadenosine
-
mechanism-based inhibitor, covalent labeling of enzyme. Inactivation results in 28% loss of NAD+
(E)-6-cyano-5,6-didehydro-6-deoxyhomoadenosine
-
mechanism-based inhibitor, type I inhibitor. Inactivation results in 66% loss of NAD+
(Z)-6-cyano-5,6-didehydro-6-deoxyhomoadenosine
-
mechanism-based inhibitor, covalent labeling of enzyme. Inactivation results in 27% loss of NAD+
1,2,4,triazole-3-carboxamide riboside
-
ribavirin
1-[(1S,4R,5S)-2-fluoro-4,5-dihydroxycyclopent-2-en-1-yl]pyrimidine-2,4(1H,3H)-dione
-
-
2'-deoxyadenosine
-
-
2'3'-dideoxyadenosine
-
-
2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-[(piperidin-2-ylmethyl)amino]ethyl]amino)-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-([5-chloro-2-(4-chlorophenoxy)phenyl]{2-[(2,3-dihydro-1H-inden-2-yl)amino]-2-oxoethyl}amino)-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-amino-4'-alpha-fluoro-(9-((1'R,2'S,3'R)-2',3'-dihydroxy-cyclopentan-1'-yl)adenine)
-
slight inhibition
2-aminoaristeromycin
-
20fold selectivity for Plasmodium falciparum over human enzyme, resisitant to adenosine deaminase
2-chloroadenosine
-
-
2-Deoxycoformycin
-
-
2-fluoroaristeromycin
-
24fold selectivity for Plasmodium falciparum over human enzyme, resisitant to adenosine deaminase
2-fluoronoraristeromycin
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[(2R)-pyrrolidin-2-ylmethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[(2S)-pyrrolidin-2-ylmethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(piperidin-1-yl)ethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(propan-2-ylamino)ethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-(1,3-dihydro-2H-isoindol-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-(3,4-dihydroisoquinolin-2(1H)-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-cyclohexyl-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(1,2,3,4-tetrahydronaphthalen-2-yl)acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(2-phenylethyl)acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(piperidin-4-yl)acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(trans-4-phenylcyclohexyl)acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-phenylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-[1-(methylsulfonyl)piperidin-4-yl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-[4-(methylsulfonyl)piperazin-1-yl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[3-(pyrrolidin-1-yl)propyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[2-(dimethylamino)ethyl]amino]-2-oxoethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[2-(ethylamino)ethyl]amino]-2-oxoethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[2-(methylamino)ethyl]amino]-2-oxoethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-(1,3-dihydro-2H-isoindol-2-yl)-2-oxoethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-(3,4-dihydroisoquinolin-2(1H)-yl)-2-oxoethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(4-phenylpiperidin-1-yl)ethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(piperidin-3-ylamino)ethyl]amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(pyrrolidin-3-ylamino)ethyl]amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
-
-
2-{[5-chloro-2-(4-chlorophenoxy)phenyl](2-{[(2-fluorophenyl)methyl]amino}-2-oxoethyl)amino}-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
-
-
2-{[5-chloro-2-(4-chlorophenoxy)phenyl](2-{[2-(methylamino)ethyl]amino}-2-oxoethyl)amino}-N-(1,3-dihydro-2H-isoindol-2-yl)-N-methylacetamide
-
-
3'-deoxyadenosine
-
-
3-deazaadenosine
-
-
4',5'-dehydroadenosine
-
-
4'-beta-fluoro-(9-((1'R,2'S,3'R)-2',3'-dihydroxy-cyclopentan-1'-yl)adenine)
-
slight inhibition
5'-deoxy,5'-methylthioadenosine
-
-
5'-iodo-5'-deoxyadenosine
-
-
5'-S-cyano-5'-thioadenosine
-
-
5'-S-ethynyl-5'-thioadenosine
-
-
5'-S-vinyl-5'-thioadenosine
-
-
5,5'-dithiobis-(2-nitrobenzoate)
-
-
5-(6-aminopurin-9-yl)-3-hydroxymethylcyclopent-3-ene-1,2-diol
-
-
5-(6-aminopurin-9-yl)-4-fluoro-3-hydroxymethylcyclopent-3-ene-1,2-diol
-
i.e. fluoroneplanocin A, mechanism-based inhibitor, crystallization data
5-(6-aminopurin-9-yl)-4-fluorocyclopent-3-ene-1,2-diol
-
-
5-(6-aminopurin-9-yl)-cyclopent-3-ene-1,2-diol
-
-
5-amino-4-imidazole carboxamide riboside
-
-
9-(2-deoxy-beta-D-erythro-pentodialdo-1,4-furanosyl)adenine
-
-
-
9-(2-deoxy-beta-D-erythro-pentodialdo-1,4-furanosyl)adenine oximes
-
(E/Z)
-
9-(3-deoxy-beta-D-erythro-pentodialdo-1,4-furanosyl)adenine
-
-
-
9-(3-deoxy-beta-D-erythro-pentodialdo-1,4-furanosyl)adenine oximes
-
(E/Z)
-
9-(5,6-dideoxy-6-iodo-beta-D-ribo-hex-5-ynofuranosyl)-9H-purin-6-amine
-
i.e. 5',5',6',6'-tetradehydro-6'-deoxy-6'-iodohomoadenosine, strong
9-(6-bromo-5,6-dideoxy-beta-D-ribo-hex-5-ynofuranosyl)-9H-purin-6-amine
-
i.e. 5',5',6',6'-tetradehydro-6'-deoxy-6'-bromohomoadenosine, partial, 2 mol of the inhibitor is covalently bound to Lys318 of the two subunits of the homotetramer
9-(alpha-L-lyxo-pentodialdo-1,4-furanosyl)adenine
-
-
-
9-(alpha-L-lyxo-pentodialdo-1,4-furanosyl)adenine oximes
-
(E/Z)
-
9-(beta-D-arabino-pentodialdo-1,4-furanosyl)adenine
-
-
-
9-(beta-D-arabino-pentodialdo-1,4-furanosyl)adenine oximes
-
(E/Z)
-
9-(beta-D-ribo-pentodialdo-1,4-furanosyl)adenine
-
-
-
9-(beta-D-ribo-pentodialdo-1,4-furanosyl)adenine (adenosine-5'-carboxaldehyde)
-
-
-
9-(beta-D-ribo-pentodialdo-1,4-furanosyl)adenine O-benzyloximes
-
(E/Z)
-
9-(beta-D-ribo-pentodialdo-1,4-furanosyl)adenine O-ethyloximes
-
(E/Z)
-
9-(beta-D-ribo-pentodialdo-1,4-furanosyl)adenine O-methyloximes
-
(E/Z)
-
9-(beta-D-ribo-pentodialdo-1,4-furanosyl)adenine oximes
-
(E/Z)
-
9-beta-D-arabinofuranosyladenine
-
-
9-[(1'R,2'S,3'R,5'R)-3',4'-epoxy-2'-hydroxy-cyclopentan-1'-yl]-9-H-2-fluoroadenine
-
-
9-[(1'R,2'S,3'S,4'R)-3',4'-epoxy-2'-hydroxy-cyclopentan-1'-yl]-9-H-adenine
-
-
9-[5,6,7,8-tetradeoxy-8-iodo-beta-D-ribo-oct-5(E)-en-7-yno-furanosyl]adenine
-
-
9-[5,6,7,8-tetradeoxy-beta-D-ribo-oct-5(E)-en-7-ynofuranosyl]adenine
-
-
9H-purin-6-amine, 9-(6-chloro-5,6-dideoxy-beta-D-ribo-hex-5-ynofuranosyl)-9H-purin-6-amine
-
i.e. 5',5',6',6'-tetradehydro-6'-deoxy-6'-chlorohomoadenosine partial, 2 mol of the inhibitor is covalently bound to Lys318 of the two subunits of the homotetramer
adenine arabinoside
-
-
adenosine
-
-
adenosine-2',3'-dialdehyde
-
; inhibition of the enzyme, mimicks the induction of caspase-like activity and DNA fragmentation induced by adenosine
adenosylornithine
-
sinefungin
beta-thionicotinamide adenine dinucleotide
-
binding affinity 40 nM, 30% loss of activity after 12 h
beta-thionicotinamide adenine dinucleotide, reduced form
-
binding affinity 40 nM, 30% loss of activity after 12 h
Cu2+
-
noncompetitive, binding of Cu2+ results in release of NAD+ cofactors. Cu2+ binds at the central channel and interrupts subunit interactions
dithiothreitol
-
together with adenosine
iodoacetamide
-
-
iodoacetate
-
-
Isothiocyanate
-
fluorescent isothiocyanate
MDL-28842
-
-
methyl 4-(adenin-9-yl)-2-hydroxybutanoate
-
i.e. DZ2002, potent reversible type III inhibitor, blocks S-adenosylhomocysteine hydrolase more effectively than type I inhibitor, but cytotoxicity is greatly reduced
methyl 4-[([[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]acetyl)(methyl)amino]piperazine-1-carboxylate
-
-
methyl 4-[([[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]acetyl)(methyl)amino]piperidine-1-carboxylate
-
-
N-(1-acetylpiperidin-4-yl)-2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methylacetamide
-
-
N-benzyl-2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methylacetamide
-
-
neplanocin A
noraristeromycin
-
-
p-chloromercuribenzoate
-
-
ribavirin
-
binds to adenosine-binding site of enzyme and reduces the NAD+ cofactor to NADH. Selective for trypanosomal enzyme over human enzyme, as the slow inactivation step is 5fold faster with the trypanosomal enzyme
S-adenosyl-L-methionine
-
-
tubercidin
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-nitrosomethylbenzylamine
-
treatment with 50 microg/ml N-nitrosomethylbenzylamine results in twenty-eight differentially expressed protein spots in HEEC cells. Two tumor suppressor proteins, prohibitin and c-Myc binding protein, are down-regulated in NMBA-treated HEEC cells. S-adenosylhomocysteine hydrolase, is up-regulated in NMBA-treated HEEC cells
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11
4',5'-dehydroadenosine
-
-
0.0009 - 0.111
adenosine
0.0014
DL-homocysteine
-
pH 7.2, 30°C
0.2
L-homocysteine
-
-
0.0007 - 0.017
S-adenosyl-DL-homocysteine
0.0076 - 0.0334
S-adenosyl-L-homocysteine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6666
adenosine
-
pH 7.2, 30°C
6666
DL-homocysteine
-
pH 7.2, 30°C
1 - 1908
S-adenosyl-DL-homocysteine
0.4 - 0.79
S-adenosyl-L-homocysteine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2000
L-homocysteine
-
recombinant wild type enzyme, at pH 7.2 and 37°C
17 - 57
S-adenosyl-L-homocysteine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017
(E)-6-chloro-6-cyano-5,6-didehydro-6-deoxyhomoadenosine
-
-
0.00006 - 0.0168
2-fluoronoraristeromycin
0.067
5'-S-cyano-5'-thioadenosine
-
pH 7.5, 37°C
0.01
5'-S-ethynyl-5'-thioadenosine
-
pH 7.5, 37°C
0.004
5'-S-vinyl-5'-thioadenosine
-
pH 7.5, 37°C
0.0203
9-[(1'R,2'S,3'R,5'R)-3',4'-epoxy-2'-hydroxy-cyclopentan-1'-yl]-9-H-2-fluoroadenine
-
-
0.0124
9-[(1'R,2'S,3'S,4'R)-3',4'-epoxy-2'-hydroxy-cyclopentan-1'-yl]-9-H-adenine
-
-
0.1185
9-[5,6,7,8-tetradeoxy-8-iodo-beta-D-ribo-oct-5(E)-en-7-yno-furanosyl]adenine
-
37°C, pH 7.2
0.00055
9-[5,6,7,8-tetradeoxy-beta-D-ribo-oct-5(E)-en-7-ynofuranosyl]adenine
-
37°C, pH 7.2
0.000028 - 0.00041
noraristeromycin
0.266
ribavirin
-
pH 7.2, 22°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000055
(1R,2S,3R)-3-(6-amino-4,5-dihydro-9H-purin-9-yl)cyclopentane-1,2-diol
Homo sapiens;
-
pH and temperature not specified in the publication
0.000303
(1R,2S,3R,5R)-3-(6-amino-4,5-dihydro-9H-purin-9-yl)-5-(hydroxymethyl)cyclopentane-1,2-diol
Homo sapiens;
-
pH and temperature not specified in the publication
0.000455
(1R,2S,3S)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-4-fluorocyclopentane-1,2-diol
Homo sapiens;
-
pH and temperature not specified in the publication
0.00025
(1R,2S,3S)-3-(8-aminoimidazo[1,2-a]pyrazin-3-yl)cyclopentane-1,2-diol
Homo sapiens;
-
pH and temperature not specified in the publication
0.001223
(1R,2S,3S,5S)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-5-methylcyclopentane-1,2-diol
Homo sapiens;
-
pH and temperature not specified in the publication
0.003644
(1R,2S,4r)-4-(4-amino-6,7-difluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
Homo sapiens;
-
pH and temperature not specified in the publication
0.004827
(1R,2S,4r)-4-(4-amino-6-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
Homo sapiens;
-
pH and temperature not specified in the publication
0.000016
(1R,2S,4r)-4-(4-amino-7-chloro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
Homo sapiens;
-
pH and temperature not specified in the publication
0.000041
(1R,2S,4r)-4-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
Homo sapiens;
-
pH and temperature not specified in the publication
0.000236
(1R,2S,4r)-4-(4-amino-7-methyl-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2-diol
Homo sapiens;
-
pH and temperature not specified in the publication
0.002124
(1R,2S,4r)-4-(6-amino-2-fluoro-9H-purin-9-yl)cyclopentane-1,2-diol
Homo sapiens;
-
pH and temperature not specified in the publication
0.000024
(1S,2R,3S,4S)-4-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopentane-1,2,3-triol
Homo sapiens;
-
pH and temperature not specified in the publication
0.000195
(1S,2R,5R)-5-(6-amino-4,5-dihydro-9H-purin-9-yl)-3-(chloromethyl)cyclopent-3-ene-1,2-diol
Homo sapiens;
-
pH and temperature not specified in the publication
0.004125
(1S,2R,5R)-5-(6-amino-4,5-dihydro-9H-purin-9-yl)cyclopent-3-ene-1,2-diol
Homo sapiens;
-
pH and temperature not specified in the publication
0.000976
(1S,2R,5S)-5-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-4-fluorocyclopent-3-ene-1,2-diol
Homo sapiens;
-
pH and temperature not specified in the publication
0.00969
(1S,2R,5S)-5-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)cyclopent-3-ene-1,2-diol
Homo sapiens;
-
pH and temperature not specified in the publication
0.000269
(1S,2S,3S,5S)-3-(4-amino-7-fluoro-1H-imidazo[4,5-c]pyridin-1-yl)-5-fluorocyclopentane-1,2-diol
Homo sapiens;
-
pH and temperature not specified in the publication
0.00853
1-[(1S,4R,5S)-2-fluoro-4,5-dihydroxycyclopent-2-en-1-yl]pyrimidine-2,4(1H,3H)-dione
Homo sapiens;
-
37°C
0.00015
2-([5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-[(piperidin-2-ylmethyl)amino]ethyl]amino)-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.01136
2-([5-chloro-2-(4-chlorophenoxy)phenyl]{2-[(2,3-dihydro-1H-inden-2-yl)amino]-2-oxoethyl}amino)-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.0907
2-aminoaristeromycin
Homo sapiens;
-
pH 7.2, 30°C
0.0472
2-fluoroaristeromycin
Homo sapiens;
-
pH 7.2, 30°C
0.0006
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[(2R)-pyrrolidin-2-ylmethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.00011
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[(2S)-pyrrolidin-2-ylmethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.00032
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(piperidin-1-yl)ethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.000049
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(propan-2-ylamino)ethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.000013
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-(1,3-dihydro-2H-isoindol-2-yl)-N-methylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.000052
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.0002
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-(3,4-dihydroisoquinolin-2(1H)-yl)-N-methylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.00038
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-cyclohexyl-N-methylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.000081
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(1,2,3,4-tetrahydronaphthalen-2-yl)acetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.00034
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(2-phenylethyl)acetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.1
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(piperidin-4-yl)acetamide
Homo sapiens;
-
IC50 above 0.1 mM, at pH 7.2 and 37°C
0.00053
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-(trans-4-phenylcyclohexyl)acetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.0027
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-phenylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.00023
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-[1-(methylsulfonyl)piperidin-4-yl]acetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.000049
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methyl-N-[4-(methylsulfonyl)piperazin-1-yl]acetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.00033
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[3-(pyrrolidin-1-yl)propyl]amino]ethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.00013
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[2-(dimethylamino)ethyl]amino]-2-oxoethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.00006
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[2-(ethylamino)ethyl]amino]-2-oxoethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.00007
2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-[[2-(methylamino)ethyl]amino]-2-oxoethyl)amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.1
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-(1,3-dihydro-2H-isoindol-2-yl)-2-oxoethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens;
-
IC50 above 0.1 mM, at pH 7.2 and 37°C
0.017
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-(3,4-dihydroisoquinolin-2(1H)-yl)-2-oxoethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.00097
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(4-phenylpiperidin-1-yl)ethyl]amino]-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.0012
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(piperidin-3-ylamino)ethyl]amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.0015
2-[[5-chloro-2-(4-chlorophenoxy)phenyl][2-oxo-2-(pyrrolidin-3-ylamino)ethyl]amino]-N-(2,3-dihydro-1H-inden-2-yl)-N-methylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.00878
2-{[5-chloro-2-(4-chlorophenoxy)phenyl](2-{[(2-fluorophenyl)methyl]amino}-2-oxoethyl)amino}-N-[2-(pyrrolidin-1-yl)ethyl]acetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.000005
2-{[5-chloro-2-(4-chlorophenoxy)phenyl](2-{[2-(methylamino)ethyl]amino}-2-oxoethyl)amino}-N-(1,3-dihydro-2H-isoindol-2-yl)-N-methylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.00087
5-(6-aminopurin-9-yl)-3-hydroxymethylcyclopent-3-ene-1,2-diol
Homo sapiens;
-
pH 7.2, 37°C
0.00048
5-(6-aminopurin-9-yl)-4-fluoro-3-hydroxymethylcyclopent-3-ene-1,2-diol
Homo sapiens;
-
pH 7.2, 37°C
0.00767
5-(6-aminopurin-9-yl)-4-fluorocyclopent-3-ene-1,2-diol
Homo sapiens;
-
pH 7.2, 37°C
0.00583
5-(6-aminopurin-9-yl)-cyclopent-3-ene-1,2-diol
Homo sapiens;
-
pH 7.2, 37°C
0.000044
methyl 4-[([[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]acetyl)(methyl)amino]piperazine-1-carboxylate
Homo sapiens;
-
at pH 7.2 and 37°C
0.00089
methyl 4-[([[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]acetyl)(methyl)amino]piperidine-1-carboxylate
Homo sapiens;
-
at pH 7.2 and 37°C
0.0046
N-(1-acetylpiperidin-4-yl)-2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.00053
N-benzyl-2-[[5-chloro-2-(4-chlorophenoxy)phenyl](2-oxo-2-[[2-(pyrrolidin-1-yl)ethyl]amino]ethyl)amino]-N-methylacetamide
Homo sapiens;
-
at pH 7.2 and 37°C
0.0000015 - 0.000047
neplanocin A
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.05
-
mutant R49C
0.116
-
mutant D86G
0.17
-
mutant A89V, hydrolysis of S-adenosyl-DL-homocysteine
0.185
-
mutant Y143C, hydrolysis of S-adenosyl-DL-homocysteine
0.4
-
mutant A89V, synthesis of S-adenosyl-DL-homocysteine
0.42
-
mutant Y143C, synthesis of S-adenosyl-DL-homocysteine
0.5
-
mutant E115L, hydrolysis of S-adenosyl-DL-homocysteine
0.525
-
mutant D86E
0.59
-
mutant A89V/T84S, hydrolysis of S-adenosyl-DL-homocysteine
0.74
-
mutant T84S, hydrolysis of S-adenosyl-DL-homocysteine
0.75
-
mutant E115L, synthesis of S-adenosyl-DL-homocysteine
1.23
-
wild-type, synthesis of S-adenosyl-DL-homocysteine
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
assay at
7.2
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
pH 6.0: about 60% of maximal activity, pH 8.0: about 60% of maximal activity, hydrolysis of S-adenosyl-DL-homocysteine
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
37
-
assay at
50
-
hydrolysis of S-adenosyl-DL-homocysteine
additional information
-
assay at room temperature
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 55
-
35°C: about 60% of maximal activity, 55°C: about 75% of maximal activity, hydrolysis of S-adenosyl-DL-homocysteine
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
human kidney fibroblast cell line 293T cells: AdoHcyase protein levels and enzymatic activities are significantly higher in human cells infected with the Streptococcus pyogenes SW510 speB mutant strain than in cells infected with the NZ131 wild-type strain
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
diffuse in nonmotile amoebae. Concentration with F-actin in pseudopods at the front of motile, chemotaxing cells, but not present in filopodia or at the very leading edge
Manually annotated by BRENDA team
PDB
SCOP
CATH
UNIPROT
ORGANISM
Homo sapiens;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43000
-
4 * 43000, SDS-PAGE
49000
-
4 * 47000-48000, SDS-PAGE, 4 * 49000, amino acid determination
150000
-
gel filtration
189000
-
analytical ultrafiltration
190000
-
gel filtration
196000
-
gel filtration
260000
-
gel filtration, wild-type
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 48000, SDS-PAGE
homotetramer
-
4 * 48000, SDS-PAGE
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
-
Lys401 and Lys408 acetylation of the enzyme changes hydrogen bonding patterns in its NAD+ binding regions and reduces its catalytic activity
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 200 mM sodium formate, 5-20% (w/v) PEG 3350, and 100 mM BisTris, pH 6.0-6.5
-
hanging-drop vapor-diffusion method, complex of the enzyme with neplanocin A
-
in complex with mechanism-based inhibitor fluoroneplanocin A. The crystallized enzyme complex shows the closed conformation and turns out to be the intermediate of mechanism-based inhibition. The cofactor depletion by 3'-oxidation of fluoroneplanocin A contributes to the enzyme inhibition along with the irreversible covalent modification of enzyme
-
performance of Brownian dynamics simulations by building a coarse-grained model based on the holo and ligand-bound structures, in order to study the link between the allosteric communication and functional dynamics. Upon ligand-induced transition, the signal of intra-subunit closure dynamics is transmitted to form inter-subunit contacts, which in turn invoke a precise alignment of active site, followed by the dimer-dimer rotation that compacts the whole tetrameric structure. Analysis provides evidence of both induced fit and population shift mechanisms, and also shows that the transition state ensemble is akin to the ligand-bound state. Besides the formation of enzyme-ligand contacts at the active site, the allosteric couplings from the residues distal to the active site is vital to the enzymatic function
-
substrate-free wild-type enzyme exhibits reorientational motions on time scales of 10-20 and 80-90 ns. The faster motion is attributed to the domain motion, and the slower motion is attributed to the tumbling of enzyme. The domain motion is present in enzyme complexes with NADH/3'-keto-adenosine and NAD+/3'-deoxyadenosine, but absent in complexwith NADH/3-keto-neplaocin A
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
97% of activity is lost
50
-
15 min, wild-type, stable, mutant E115L, 43% loss of activity, mutant Y143C, 50% loss of activity
55
-
15 min, wild-type, 50% loss of activity, complete loss of activity for mutants Y143C and E115L
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, wild-type enzyme is robust and retains activity for at least one year with several freeze-thaw cycles. Mutant A89V, stable for about 1 month
-
-70°C, 1-2 mg enzyme per ml, loss of less than 10% of activity over 6 months
-
4°C, mutant A89V, half-life of 1-2 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2200fold to homogeneity
-
chitin bead chromatography and Superdex 200 gel filtration
-
partial, 500fold
-
to homogeneity
-
using affinity chromatography
-
using Ni-NTA chromatography and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expression of mutant enzymes T60C, T60S, T60A and Q85A in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is downregulated in esophageal squamous cell carcinoma cells compared with normal esophageal epithelial cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A89V
-
more than 70% decrease in enzyme activity and decrease in unfolding temperature by 5.5°C. Subunits assemble similarly to wild-type, but electrophoretic mobility is faster than wild-type
A89V/T84S
-
restores most of the catalytic activity of mutant A89V due to loss of sterical incompatibility of V89 and T84
D190A
-
strong decrease in hydrolytic activity
D293A
-
the mutant shows reduced catalytic efficiency with S-adenosyl-L-homocysteine compared to the wild type enzyme and no reaction with L-homocysteine
D422K
-
inactive
D86E
-
replacing Asp86 with negatively charged Glu86 in mutant protein maintains enzymatic activity to 70% of wild-type, Km (mM) (S-adenosyl-L-homocysteine) similar to wild-type
D86G
-
protein tends to form enzymatically inactive aggregates and the loss of a single negative charge as a result of the mutation is involved in enzyme inactivation
D86K
-
inactive mutant
D86L
-
inactive mutant
E115L
-
about 30-40% loss of activity both for hydrolysis and synthesis of S-adenosylhomocysteine
E156A
-
strong decrease in hydrolytic activity
H353A
mutation changes the hinge-dynamics of enzyme, domain motion cannot be detected
K186A
-
strong decrease in hydrolytic activity
M351P
binding of inhibitor neplanocin A similar to wild-type
N181A
-
strong decrease in hydrolytic activity
N191A
-
strong decrease in hydrolytic activity
N27K
-
the mutant shows reduced catalytic efficiency with S-adenosyl-L-homocysteine compared to the wild type enzyme and no reaction with L-homocysteine
P354A
binding of inhibitor neplanocin A similar to wild-type
Q85A
-
kcat/Km is 13.45fold lower then wild-type value. Ki-value for noraristeromycin is 4.46fold higher than wild-type value, Ki-value for 2-fluoronoraristeromycin is 5.6fold higher than wild-type value
R49C
-
mutant shows dramatically reduced AHCY activity, mutant protein forms intermolecular disulfide bonds, leading to macromolecular structures that can be prevented by reducing agent DTT
R49C/D86G
-
a new missense mutation is found in the AHCY gene from a case of AHCY deficiency in an infant girl who died at age four months
T60A
-
kcat/Km is 1.23 fold lower then wild-type value. Ki-value for noraristeromycin is 3.3fold lower than wild-type value, Ki-value for 2-fluoronoraristeromycin is 23fold lower than wild-type value
T60C
-
kcat/Km is 2.3fold lower then wild-type value. Ki-value for noraristeromycin is 1.2fold higher than wild-type value, Ki-value for 2-fluoronoraristeromycin 11fold lower than wild-type value
T60S
-
kcat/Km is 1.6fold higher then wild-type value. Ki-value for noraristeromycin is 2.3fold lower than wild-type value, Ki-value for 2-fluoronoraristeromycin is 50fold lower than wild-type value
T84L
-
inactivation
T84Q
-
inactivation
T84S
-
activity similar to wild-type
W112stop
-
complete loss of activity
Y143C
-
about 70% loss of activity both for hydrolysis and synthesis of S-adenosylhomocysteine
Y430A
-
mutation alters the NAD+ association and dissociation kinetics, increasing the cofactor equilibrium dissociation constant from approximately 10 nM to about 800 nM
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
molecular biology