4.2.1.22: cystathionine beta-synthase
This is an abbreviated version!
For detailed information about cystathionine beta-synthase, go to the full flat file.
Word Map on EC 4.2.1.22
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4.2.1.22
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h2s
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sulfide
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homocystinuria
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hyperhomocysteinemia
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artery
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spacer
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corticobasal
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candida
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mthfr
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carotid
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folate
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transsulfuration
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conidia
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cajal
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nahs
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dextrose
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methylenetetrahydrofolate
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bismuth
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hallucinations
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anamorphic
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palsy
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supranuclear
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charles
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remethylation
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reisolated
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conidiophore
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gamma-lyase
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biodiversity
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hyaline
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chemoreceptor
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gasotransmitter
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3-mercaptopyruvate
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frontotemporal
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sulfurtransferase
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thromboembolic
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ascospore
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rinsed
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aminooxyacetic
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apraxia
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snrnps
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symptomless
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hydrosulfide
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marxianus
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visuospatial
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5,10-methylenetetrahydrofolate
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voxel-based
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appressoria
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naocl
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medicine
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diagnostics
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ascus
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phytopathological
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analysis
- 4.2.1.22
- h2s
- sulfide
- homocystinuria
- hyperhomocysteinemia
- artery
-
spacer
-
corticobasal
- candida
- mthfr
-
carotid
- folate
-
transsulfuration
- conidia
-
cajal
- nahs
- dextrose
- methylenetetrahydrofolate
-
bismuth
- hallucinations
-
anamorphic
- palsy
-
supranuclear
-
charles
-
remethylation
-
reisolated
-
conidiophore
-
gamma-lyase
-
biodiversity
-
hyaline
-
chemoreceptor
-
gasotransmitter
- 3-mercaptopyruvate
-
frontotemporal
- sulfurtransferase
-
thromboembolic
- ascospore
-
rinsed
-
aminooxyacetic
- apraxia
-
snrnps
-
symptomless
- hydrosulfide
- marxianus
-
visuospatial
- 5,10-methylenetetrahydrofolate
-
voxel-based
-
appressoria
- naocl
- medicine
- diagnostics
- ascus
-
phytopathological
- analysis
Reaction
Synonyms
Beta-thionase, CBS, CBS424, CDCP2, CNNM2, Cys4, CysB, cystathionine beta synthase, cystathionine beta-synthase, cystathionine beta-synthase domain-containing protein, cystathionine-beta-synthase, Cysteine synthase, EC 4.2.1.21, hCBS, Hemoprotein H-450, LbrM.17.0230, Methylcysteine synthase, osmoprotectant transporter OpuC, PF1953, PH0267, Serine sulfhydrase, Serine sulfhydrylase, Serine sulphhydrase, TA0289, TM0935, TV1335, yCBS, ytCBS
ECTree
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Activating Compound
Activating Compound on EC 4.2.1.22 - cystathionine beta-synthase
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AdoMet
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allosteric regulator, 1mol per mole of monomeric subunit activates the enzyme 2fold
delta-aminolevulinic acid
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activates, effects on wild-type and mutant enzymes, overview
Ethionine
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i.e. 2-amino-4-(ethylthio)butyric acid, an methionine analogue, which is converted to S-adenosyl-ethionine in vivo and activates CBS, treatment increased liver CBS activity 4.0fold in wild-type mice
sodium nitroprusside
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enhances activity by interacting with cysteine residues, N-ethylmaleimide abolishes this effect
tumor necrosis factor-alpha
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leads to cleavage of the enzyme to a truncated form and therefore increases the activity, 50% increase of activity after treatment of HepG2 cells for 16 h
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structure of the regulatory, energy-sensing CBS domains and mechanism for allosteric activation by S-adenoyl-L-methionine, overview
S-adenosyl-L-methionine
3fold activation, allosteric regulator of the full length enzyme, does not activate the truncated enzyme
S-adenosyl-L-methionine
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activates full length enzyme, but not the truncated core, 4 S-adenosyl-L-methionine molecules per tetramer
S-adenosyl-L-methionine
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the enzyme is allosterically activated by S-adenosyl-L-methionine under normal conditions but is destabilized under pathological conditions
S-adenosyl-L-methionine
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about 4fold increase of specific activity in the presence of 0.25 mM S-adenosyl-L-methionine
S-adenosyl-L-methionine
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allosteric activator. Binding of AdoMet to wild-type CBS moderately increases the protein stability toward urea, while it does not influence the unfolding cooperativity
S-adenosyl-L-methionine
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the addition of S-adenosyl-L-methionine nearly doubles enzyme activity
S-adenosyl-L-methionine
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the enzyme is allosterically activated (2-3fold) by S-adenosyl-L-methionine
S-adenosyl-L-methionine
AdoMet binding significantly enhances CBS inhibition by CO. NO radical binding to reduced CBS i also enhanced by AdoMet, although to a lesser as compared with CO. CO and NOradical binding is unchanged by AdoMet in a truncated form of CBS lacking the C-terminal regulatory domain
S-adenosyl-L-methionine
allosteric activator, in the presence of AdoMet, the autoinhibition exerted by the regulatory region is eliminated
S-adenosyl-L-methionine
half-activation of wild-type at 0.0258 mM, mutant D444N 1.234 mM, mutant S500L 0.063 mM, respectively
S-adenosyl-L-methionine
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the enzyme is allosterically activated by S-adenosyl-L-methionine under normal conditions but is destabilized under pathological conditions
enzyme is not allosterically regulated by AdoMet
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additional information
enzyme is more active under oxidizing conditions
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additional information
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treatment with 0.2 M trimethylamine-N-oxide results in rescuing expression as well as activity of CBS to 82% of human wild type CBS produced in a yeast heme-deficient strain
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additional information
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taurine activates some cystathionine beta-synthase mutants slightly, while it slightly inhibits the wild-type enzyme and other cystathionine beta-synthase mutants
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additional information
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oxidizing conditions increase the enzyme activity by 2fold
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additional information
S-adenosyl-L-methionine does not activate
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additional information
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S-adenosyl-L-methionine does not activate
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additional information
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enzyme can not be activated by S-adenosyl-L-methionine
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