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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Cofactor
Cofactor on EC 4.2.1.22 - cystathionine beta-synthase
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heme
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heme
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the heme favors the ferric state at lower pH and, in the presence of reductants, attains the ferric state via transient formation of the ferrous state. Fe(II)-enzyme and Fe(III)-enzyme are apparently interconverted by a proton-controlled internal electron transfer process
heme
carbon monoxide or nitric oxide can bind to the cofactor, resulting in enzyme inhibition
heme
the in vitro activity of cystathionine beta-synthase is sensitive to the redox state of the heme and is higher in the ferric form. Both carbon monoxide and nitric oxide bind to ferrous heme and inhibit the enzyme. The crystal structure of the protein reveals that the heme is about 20 A away from the active site
heme
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heme in CBS is six-coordinate, low spin, and contains cysteine and histidine as axial ligands, the unusual heme in CBS represents a potential source of cytosolic superoxide radical
heme
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requires a heme cofactor for maximal activity, heme plays a key role in proper CBS folding and assembly
heme
the specific activity of CBS improves 1.8-2.8fold under truncation of R51A and R224A when the heme iron is in the ferric state
heme
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the specific activity of the alkaline form is approximately 25% of that for the intact CBS enzyme when the heme iron is in the ferric state
heme
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vibrational coherence spectroscopy is used to probe the low-frequency vibrational motions of the heme and how they depend on structural distortions that are induced by the CBS protein environment
heme
enzyme possesses a noncatalytic heme cofactor with cysteine and histidine as ligands. Nitrite is reduced by Fe(II)-CBS to form Fe(II)NO radical-CBS. Reoxidation of Fe(II)NO radical-CBS by O2 shows complex kinetic behavior and leads to peroxynitrite (ONOO-) formation
pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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Lys119 is eesential for the formation of the internal aldimine with pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
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forms a series of intermediates during the reaction, gem-diamine and external aldimine of aminoacrylate are the primary intermediates in the forward half-reaction with L-serine and the external aldimine of aminoacrylate or its complex with L-homocysteine is the primary intermediate in the reverse half-reaction with L-cystathionine
pyridoxal 5'-phosphate
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reacts with L-allothreonine to form a stable 3-methyl aminoacrylate intermediate
pyridoxal 5'-phosphate
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Km-value for wild-type enzyme: 0.00118 mM, KM-value for mutant enzyme I278T: 0.00084 mM, KM-value for mutant enzyme R266K: 0.00339 mM
pyridoxal 5'-phosphate
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i.e. PLP, serves in the catalytic chemistry of CBS via a well-established mechanism
pyridoxal 5'-phosphate
A0A1J9VES8
cofactor is highly flexible due to the active site being wide open
S-adenosyl-L-methionine
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allosterical regulation, increase of the enzyme's affinity for homocysteine
additional information
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yeast cystathionine beta-synthase does not have a heme cofactor
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