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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Inhibitors
Inhibitors on EC 4.2.1.22 - cystathionine beta-synthase
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(5Z)-5-[(4-hydroxy-3-methoxyphenyl)methylidene]-3-methyl-2-(methylsulfanyl)-3,5-dihydro-4H-imidazol-4-one
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compound derived from polyandrocarpamines A and B, i.e. 2-aminoimidazolone compounds isolated from the ascidian Polyandrocarpa sp.
2-methoxy-4-[(Z)-(5-oxo-2-sulfanylideneimidazolidin-4-ylidene)methyl]phenyl acetate
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compound derived from polyandrocarpamines A and B, i.e. 2-aminoimidazolone compounds isolated from the ascidian Polyandrocarpa sp.
Dithionite
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2fold decrease in enzyme activity due to altered oxidation state of the heme
Hg2+
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reactivity of Co(III) hCBS with HgCl2 is consistent with a loss of the cysteine(thiolate) ligand. 2-Mercaptoethanol is unable to reverse the Hg-induced ligand switch, in contrast to some other heme-thiolate proteins
peroxynitrite
exposure to peroxynitrite does not modify bound pyridoxal 5'-phosphate but leads to nitration of Trp208, Trp43 and Tyr223 and alterations in the heme environment including loss of thiolate coordination, conversion to high-spin and bleaching, with no detectable formation of oxoferryl compounds nor promotion of one-electron processes
regulatory domain
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exerts an inhibitory effect on the enzyme, deletion is correlated with a 1fold increase in catalytic activity
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titanium citrate
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2fold decrease in enzyme activity due to altered oxidation state of the heme
carbon monoxide
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binds to the prosthetic heme, stabilizing 6-coordinated CO-Fe(II)-histidine complex to block the activity
carbon monoxide
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binds to the prosthetic heme, stabilizing 6-coordinated CO-Fe(II)-histidine complex to block the activity
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reversible competitive with respect to homocysteine, complete loss of activity at 0.06 mM
CO
can bind to the cofactor heme, resulting in enzyme inhibition. CBS exhibits strong anticooperativity in CO binding
CO
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CO binding is found to induce a tautomeric shift of the pyridoxal 5'-phosphate from the ketoenamine to the enolimine form. The ketoenamine is key to pyridoxal 5'-phosphate reactivity because its imine C-N bond is protonated, facilitating attack by the nucleophilic substrate, serine
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the alternation of heme environment inactivates the enzyme
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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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the CBS activity is significantly reduced in kidneys subjected to ischemia alone (15-60 min) or subjected to ischemia followed by reperfusion for 1-24 h, injection of alkaline solution into the kidney partially restores the CBS activity during ischemia, reduction of CBS activity during reperfusion is accompanied by an elevation of nitrate and nitrite in the kidney tissue, injection of 2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide restores the CBS activity in the kidneys subjected to ischemia-reperfusion
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