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2 L-cysteine
(2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid) + H2S
beta-Chloro-DL-alanine + DL-homocysteine
?
-
-
-
-
?
beta-Cyano-DL-alanine + DL-homocysteine
?
-
-
-
-
?
DL-Serine-O-sulfate + DL-homocysteine
?
-
-
-
-
?
L-allothreonine + homocysteine
? + H2O
-
-
-
?
L-cysteine
H2S + L-serine
-
-
-
?
L-Cysteine + 1-butanethiol
?
L-Cysteine + 1-mercapto-2-propanol
HOOC-CH(NH2)-CH2-S-CH2-CH(OH)-CH3 + H2S
L-Cysteine + 1-pentanethiol
?
L-Cysteine + 2-mercaptoethanol
HOOC-CH(NH2)-CH2-S-CH2-CH2OH + H2S
L-cysteine + 2-mercaptoethanol
S-hydroxyethyl-L-cysteine + H2S
L-Cysteine + cysteamine
?
L-Cysteine + dithioerythritol
?
L-Cysteine + dithiothreitol
?
L-Cysteine + DL-homocysteine
Cystathionine + H2S
L-cysteine + H2O
L-serine + H2S
A0A1J9VES8
-
-
-
?
L-cysteine + L-homocysteine
L-cystathionine + acetate
A0A1J9VES8
-
-
-
?
L-cysteine + L-homocysteine
L-cystathionine + H2S
L-cysteine + L-serine
lanthionine + H2O
-
-
-
?
L-Cysteine + monothioglycerol
?
L-serine + cysteamine
L-thialysine
-
-
-
-
?
L-serine + H2O
NH3 + pyruvate
-
wild-type enzyme shows no beta-elimination reaction, beta elimination is only detectable in the following mutants: T81A, S82A, T85A, Q157A, Q157E, Q157H, Y158F
-
?
L-serine + H2S
L-cysteine
-
-
-
?
L-Serine + homocysteine
?
L-Serine + homocysteine
Cystathionine + H2O
L-Serine + HS-
Cysteine + OH-
L-serine + L-cysteine
?
-
-
-
-
?
L-serine + L-homocysteine
?
-
-
-
-
r
L-serine + L-homocysteine
cystathionine + H2O
L-serine + L-homocysteine
L-cystathionine + H2O
o-acetyl-L-serine + H2S
L-cysteine + acetate
O-acetyl-L-serine + H2S
L-cysteine + acetic acid
A0A1J9VES8
-
-
-
?
O-acetyl-L-serine + H2S
pyruvate + acetate + NH3
O-acetyl-L-serine + L-homocysteine
?
-
poor substrate for both the wild type and the N- and C-terminally truncated enzyme 71â400 CBS
-
-
?
O-acetyl-L-serine + L-homocysteine
cystathionine + acetate
S-Methyl-L-cysteine + DL-homocysteine
?
-
-
-
-
?
additional information
?
-
2 L-cysteine

(2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid) + H2S
-
-
-
?
2 L-cysteine
(2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid) + H2S
-
-
-
?
cysteine + ?

H2S + ?
-
-
-
-
?
cysteine + ?
H2S + ?
-
-
-
-
?
L-Cysteine + 1-butanethiol

?
-
-
-
-
?
L-Cysteine + 1-butanethiol
?
-
-
-
-
?
L-Cysteine + 1-mercapto-2-propanol

HOOC-CH(NH2)-CH2-S-CH2-CH(OH)-CH3 + H2S
-
-
-
-
?
L-Cysteine + 1-mercapto-2-propanol
HOOC-CH(NH2)-CH2-S-CH2-CH(OH)-CH3 + H2S
-
-
-
-
?
L-Cysteine + 1-mercapto-2-propanol
HOOC-CH(NH2)-CH2-S-CH2-CH(OH)-CH3 + H2S
-
-
-
-
?
L-Cysteine + 1-mercapto-2-propanol
HOOC-CH(NH2)-CH2-S-CH2-CH(OH)-CH3 + H2S
-
activated L-serine sulfhydrase
-
?
L-Cysteine + 1-pentanethiol

?
-
-
-
-
?
L-Cysteine + 1-pentanethiol
?
-
-
-
-
?
L-Cysteine + 2-mercaptoethanol

HOOC-CH(NH2)-CH2-S-CH2-CH2OH + H2S
-
-
-
-
?
L-Cysteine + 2-mercaptoethanol
HOOC-CH(NH2)-CH2-S-CH2-CH2OH + H2S
-
-
-
?
L-Cysteine + 2-mercaptoethanol
HOOC-CH(NH2)-CH2-S-CH2-CH2OH + H2S
-
-
-
-
?
L-Cysteine + 2-mercaptoethanol
HOOC-CH(NH2)-CH2-S-CH2-CH2OH + H2S
-
-
-
?
L-Cysteine + 2-mercaptoethanol
HOOC-CH(NH2)-CH2-S-CH2-CH2OH + H2S
-
-
-
-
?
L-Cysteine + 2-mercaptoethanol
HOOC-CH(NH2)-CH2-S-CH2-CH2OH + H2S
Steinernema bibionis
-
-
-
-
?
L-Cysteine + 2-mercaptoethanol
HOOC-CH(NH2)-CH2-S-CH2-CH2OH + H2S
-
-
-
-
?
L-cysteine + 2-mercaptoethanol

S-hydroxyethyl-L-cysteine + H2S
-
-
-
-
?
L-cysteine + 2-mercaptoethanol
S-hydroxyethyl-L-cysteine + H2S
-
-
?
L-Cysteine + cysteamine

?
-
-
-
-
?
L-Cysteine + cysteamine
?
-
-
-
-
?
L-Cysteine + dithioerythritol

?
-
-
-
-
?
L-Cysteine + dithioerythritol
?
-
-
-
-
?
L-Cysteine + dithiothreitol

?
-
-
-
-
?
L-Cysteine + dithiothreitol
?
-
-
-
-
?
L-Cysteine + DL-homocysteine

Cystathionine + H2S
-
-
-
-
?
L-Cysteine + DL-homocysteine
Cystathionine + H2S
-
full-length enzyme and truncated enzyme form lacking the C-terminal regulatory domain
-
-
?
L-Cysteine + DL-homocysteine
Cystathionine + H2S
-
-
-
-
?
L-Cysteine + DL-homocysteine
Cystathionine + H2S
-
-
-
?
L-Cysteine + DL-homocysteine
Cystathionine + H2S
-
-
-
?
L-Cysteine + DL-homocysteine
Cystathionine + H2S
-
-
-
?
L-Cysteine + DL-homocysteine
Cystathionine + H2S
-
-
-
-
?
L-cysteine + L-homocysteine

L-cystathionine + H2S
A0A1J9VES8
-
-
-
?
L-cysteine + L-homocysteine
L-cystathionine + H2S
-
-
-
-
r
L-cysteine + L-homocysteine
L-cystathionine + H2S
-
-
-
?
L-cysteine + L-homocysteine
L-cystathionine + H2S
-
-
-
?
L-cysteine + L-homocysteine
L-cystathionine + H2S
-
-
-
?
L-cysteine + L-homocysteine
L-cystathionine + H2S
-
-
-
-
r
L-Cysteine + monothioglycerol

?
-
-
-
-
?
L-Cysteine + monothioglycerol
?
-
-
-
-
?
L-Cysteine + monothioglycerol
?
-
-
-
-
?
L-Serine + homocysteine

?
-
-
-
-
?
L-Serine + homocysteine
?
-
-
-
-
?
L-Serine + homocysteine
?
-
synthesis of cystathionine
-
-
?
L-Serine + homocysteine
?
-
-
-
-
?
L-Serine + homocysteine
?
-
-
-
-
?
L-Serine + homocysteine
?
-
irreversible step in transsulfuration pathway
-
-
?
L-Serine + homocysteine
?
-
reduced activity of EC 4.2.1.22 in patients with homocystinuria due to mutations in the CBS gene
-
-
?
L-Serine + homocysteine
?
-
-
-
-
?
L-Serine + homocysteine
?
-
-
-
-
?
L-Serine + homocysteine
?
-
-
-
-
?
L-Serine + homocysteine
?
-
initial step in transsulfuration forming cysteine. Homocysteine is a relatively toxic amino acid, which levels have to be kept low
-
-
?
L-Serine + homocysteine
?
-
synthesis of cystathionine
-
-
?
L-Serine + homocysteine
?
-
-
-
-
?
L-Serine + homocysteine
?
-
reverse trans-sulfuration pathway
-
-
?
L-Serine + homocysteine
?
Steinernema bibionis
-
-
-
-
?
L-Serine + homocysteine
?
-
-
-
-
?
L-Serine + homocysteine

Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
r
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
r
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
r
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
r
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
r
L-Serine + homocysteine
Cystathionine + H2O
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
ir
-
?
L-Serine + homocysteine
Cystathionine + H2O
beta-replacement reaction
-
?
L-Serine + homocysteine
Cystathionine + H2O
catalyzes a beta-replacement reaction in which an electronegative substituent in the beta-position of the amino acid substrate is replaced by a nucleophile, binding of L-serine as the external aldimine is faster than formation of the aminoacrylate intermediate, the rate-limiting step is the reaction of aminoacrylate with L-homocysteine to form L-cystathione, rate of the forward reaction is 38fold greater than the reverse reaction
-
r
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
r
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
r
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
r
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
r
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
r
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
r
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
r
L-Serine + homocysteine
Cystathionine + H2O
-
hydroxylgroup of serine is replaced by the thiol of homocysteine
-
r
L-Serine + homocysteine
Cystathionine + H2O
-
in the forward direction an external aldimine of serine and an aminoacrylate intermediate are formed, the aminoacrylate binds to homocysteine and converts to cystathione, in the reverse reaction cystathione binds to the enzyme and is rapidly converted to the aminoacrylate without accumulation of the external aldimine
-
r
L-Serine + homocysteine
Cystathionine + H2O
Steinernema bibionis
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
Steinernema bibionis
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
?
L-Serine + homocysteine
Cystathionine + H2O
-
-
-
r
L-Serine + HS-

Cysteine + OH-
-
-
-
?
L-Serine + HS-
Cysteine + OH-
-
-
-
?
L-Serine + HS-
Cysteine + OH-
-
-
-
?
L-Serine + HS-
Cysteine + OH-
-
-
-
?
L-Serine + HS-
Cysteine + OH-
-
-
-
?
L-Serine + HS-
Cysteine + OH-
-
-
-
?
L-Serine + HS-
Cysteine + OH-
-
-
-
?
L-Serine + HS-
Cysteine + OH-
Steinernema bibionis
-
-
-
?
L-Serine + HS-
Cysteine + OH-
-
-
-
?
L-serine + L-homocysteine

cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
cystathionine + H2O
-
-
-
?
L-serine + L-homocysteine
cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
cystathionine + H2O
the enzyme participates in the process of oocyte maturation
-
-
?
L-serine + L-homocysteine

L-cystathionine + H2O
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
electrostatic stabilization of the zwitterionic carbanion intermediate is afforded by the close positioning of an active site lysine residue that is initially used for Schiff base formation in the internal aldimine and later as a general base, and additional stabilizing interactions between active site residues and the catalytic intermediates
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
696253, 697295, 698182, 698850, 701064, 704664, 714179, 714912, 715808, 715809, 728933, 728945, 730143, 730146, 730755 -
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
ir
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
?
o-acetyl-L-serine + H2S

L-cysteine + acetate
A0A1J9VES8
-
-
-
?
o-acetyl-L-serine + H2S
L-cysteine + acetate
-
-
-
?
o-acetyl-L-serine + H2S
L-cysteine + acetate
-
-
-
?
O-acetyl-L-serine + H2S

pyruvate + acetate + NH3
-
-
-
?
O-acetyl-L-serine + H2S
pyruvate + acetate + NH3
-
-
-
?
O-acetyl-L-serine + L-homocysteine

cystathionine + acetate
-
-
-
?
O-acetyl-L-serine + L-homocysteine
cystathionine + acetate
-
-
-
?
additional information

?
-
O-acetylserine sulfhydrylase isozyme A, OASSAp, EC 2.5.1.65, exhibits both O-acetylserine sulfhydrylase and cystathionine beta-synthase activities
-
-
?
additional information
?
-
A0A1J9VES8
no substrate: L-serine
-
-
?
additional information
?
-
-
no substrate: L-serine
-
-
?
additional information
?
-
-
key enzyme involved in intracellular metabolism of homocysteine
-
?
additional information
?
-
-
elevated total plasma homocysteine is an independent risk factor in the development of vascular disease in humans. Elevating cystathionine beta-synthase level is an effective method to lower plasma homocysteine levels
-
-
?
additional information
?
-
-
the enzyme may have additional in vivo functions beyond its role as a homocysteine metabolizing enzyme
-
-
?
additional information
?
-
-
the overexpression of cystathionine beta-synthase may cause the developmental abnormality in cognition in Down's syndrome children and may lead to Alzheimer type of disease in Down's syndrom adults
-
-
?
additional information
?
-
-
the cystathionine beta-synthase variant c.844_845ins68 protects against CNS demyelination in X-linked adrenoleukodystrophy
-
-
?
additional information
?
-
-
the oxidation of CBS by dioxygen appears to proceed directly from the ferrous to the ferric state, presumably via an outer sphere electron transfer reaction
-
-
?
additional information
?
-
-
CBS also catalyze H2S production in vitro
-
-
?
additional information
?
-
-
the enzyme performs L-cysteine sythesis from L-serine
-
-
?
additional information
?
-
-
the enzyme performs L-cysteine sythesis from L-serine
-
-
?
additional information
?
-
cysteine is able to partially compete with serine on CBS, thus leading to generation of appreciable amounts of H2S. The leading H2S-producing reaction is condensation of cysteine with homocysteine, while cysteine desulfuration plays a dominant role when cysteine is more abundant than serine and homocysteine is limited. The serine-to-cysteine ratio is the main determinant of CBS H2S productivity. Abundance of cysteine over serine, for example, in blood plasma, allows for up to 43% of CBS activity being responsible for H2S production, while excess of serine typical for intracellular levels effectively limited such activity to less than 1.5%. CBS also produces lanthionine from serine and cysteine
-
-
?
additional information
?
-
-
first step in transsulfuration pathway
-
?
additional information
?
-
-
cystathionine beta-synthase is a key enzyme for homocysteine metabolism, it is associated with the generation and/or differentiation of the radial glia/astrocyte linage cells in the developing central nervous system
-
-
?
additional information
?
-
-
hyperhomocysteinaemia is a metabolic disorder associated with the development of premature atherosclerosis. Cystathionine beta-synthase activity is significantly decreased in mice with a plasma homocysteine value greater than 0.015 mg
-
-
?
additional information
?
-
-
role for CBS as a mediator in interactions between oocyte and granulosa cells
-
-
?
additional information
?
-
-
CBS also catalyze H2S production in vitro
-
-
?
additional information
?
-
-
no L-serine sulfhydrase activity
-
-
?
additional information
?
-
-
cystathionine-beta-synthase domains in the ATP-binding component of OpuC are required for transporter function
-
-
?
additional information
?
-
-
plasma albumin cysteinylation is regulated by cystathionine beta-synthase
-
-
?
additional information
?
-
-
CBS also catalyze H2S production in vitro
-
-
?
additional information
?
-
-
no substrate: L-threonine
-
?
additional information
?
-
-
no substrates: D-, L-allo- and D-allo-cystathionine
-
?
additional information
?
-
-
cystathionine beta-synthase also catalyze H2S production. The most efficient route for H2S generation by cystathionine beta-synthase is the beta-replacement of the cysteine thiol with homocysteine. In this reaction, cystathionine beta-synthase first reacts with cysteine to release H2S and forms an aminoacrylate intermediate. Homocysteine binds to the E 3 aminoacrylate intermediate with a bimolecular rate constant of 142 mM/s and rapidly condenses to form the enzyme-bound external aldimine of cystathionine. The reactions could be partially rate limited by release of the products, cystathionine and H2S
-
-
?
additional information
?
-
-
key enzyme in the trans-sulfuration pathway. Cystathionine beta-synthase may be an oxidative defense enzyme in the eye tissue, in particular in the segments of the eye where constant environmental oxidative stress is imposed
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-Serine + homocysteine
?
L-serine + L-homocysteine
cystathionine + H2O
L-serine + L-homocysteine
L-cystathionine + H2O
additional information
?
-
L-Serine + homocysteine

?
-
-
-
-
?
L-Serine + homocysteine
?
-
-
-
-
?
L-Serine + homocysteine
?
-
synthesis of cystathionine
-
-
?
L-Serine + homocysteine
?
-
-
-
-
?
L-Serine + homocysteine
?
-
-
-
-
?
L-Serine + homocysteine
?
-
irreversible step in transsulfuration pathway
-
-
?
L-Serine + homocysteine
?
-
reduced activity of EC 4.2.1.22 in patients with homocystinuria due to mutations in the CBS gene
-
-
?
L-Serine + homocysteine
?
-
-
-
-
?
L-Serine + homocysteine
?
-
-
-
-
?
L-Serine + homocysteine
?
-
-
-
-
?
L-Serine + homocysteine
?
-
initial step in transsulfuration forming cysteine. Homocysteine is a relatively toxic amino acid, which levels have to be kept low
-
-
?
L-Serine + homocysteine
?
-
synthesis of cystathionine
-
-
?
L-Serine + homocysteine
?
-
-
-
-
?
L-Serine + homocysteine
?
-
reverse trans-sulfuration pathway
-
-
?
L-Serine + homocysteine
?
Steinernema bibionis
-
-
-
-
?
L-Serine + homocysteine
?
-
-
-
-
?
L-serine + L-homocysteine

cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
cystathionine + H2O
the enzyme participates in the process of oocyte maturation
-
-
?
L-serine + L-homocysteine

L-cystathionine + H2O
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
-
?
L-serine + L-homocysteine
L-cystathionine + H2O
-
-
-
?
additional information

?
-
-
key enzyme involved in intracellular metabolism of homocysteine
-
?
additional information
?
-
-
elevated total plasma homocysteine is an independent risk factor in the development of vascular disease in humans. Elevating cystathionine beta-synthase level is an effective method to lower plasma homocysteine levels
-
-
?
additional information
?
-
-
the enzyme may have additional in vivo functions beyond its role as a homocysteine metabolizing enzyme
-
-
?
additional information
?
-
-
the overexpression of cystathionine beta-synthase may cause the developmental abnormality in cognition in Down's syndrome children and may lead to Alzheimer type of disease in Down's syndrom adults
-
-
?
additional information
?
-
-
the cystathionine beta-synthase variant c.844_845ins68 protects against CNS demyelination in X-linked adrenoleukodystrophy
-
-
?
additional information
?
-
-
the oxidation of CBS by dioxygen appears to proceed directly from the ferrous to the ferric state, presumably via an outer sphere electron transfer reaction
-
-
?
additional information
?
-
-
first step in transsulfuration pathway
-
?
additional information
?
-
-
cystathionine beta-synthase is a key enzyme for homocysteine metabolism, it is associated with the generation and/or differentiation of the radial glia/astrocyte linage cells in the developing central nervous system
-
-
?
additional information
?
-
-
hyperhomocysteinaemia is a metabolic disorder associated with the development of premature atherosclerosis. Cystathionine beta-synthase activity is significantly decreased in mice with a plasma homocysteine value greater than 0.015 mg
-
-
?
additional information
?
-
-
role for CBS as a mediator in interactions between oocyte and granulosa cells
-
-
?
additional information
?
-
-
cystathionine-beta-synthase domains in the ATP-binding component of OpuC are required for transporter function
-
-
?
additional information
?
-
-
plasma albumin cysteinylation is regulated by cystathionine beta-synthase
-
-
?
additional information
?
-
-
key enzyme in the trans-sulfuration pathway. Cystathionine beta-synthase may be an oxidative defense enzyme in the eye tissue, in particular in the segments of the eye where constant environmental oxidative stress is imposed
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
heme

-
-
heme
-
-
649869, 649888, 649914, 650105, 650154, 652695, 697850, 701064, 704974, 713958, 715172
heme
-
2 mol per mol of tetrameric enzyme
heme
-
ferrous CBS can form a complex with isonitriles
heme
-
ferruous CBS can form a complex with isonitriles
heme
-
iron protoporphyrin IX
heme
-
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
-
cystathionine beta-synthase binds one mole of heme per subunit
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
-
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
-
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
-
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
-
CO binding displaces Cys52 from the heme
heme
-
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
-
role of heme in cystathionine beta-synthase folding
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

-
-
pyridoxal 5'-phosphate
-
-
649869, 649914, 650105, 650154, 652695, 664020, 686517, 687896, 696253, 697295, 697850, 698182, 701064, 701750, 704177, 704974, 705345, 706024, 706620, 714179, 714912, 715172, 715808, 715809
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
dependent on
pyridoxal 5'-phosphate
-
requirement
pyridoxal 5'-phosphate
-
requirement
pyridoxal 5'-phosphate
-
requirement
pyridoxal 5'-phosphate
-
requirement
pyridoxal 5'-phosphate
-
requirement
pyridoxal 5'-phosphate
-
Lys119 is eesential for the formation of the internal aldimine with pyridoxal 5'-phosphate
pyridoxal 5'-phosphate
-
2 mol per mol of tetrameric enzyme
pyridoxal 5'-phosphate
-
dependent
pyridoxal 5'-phosphate
-
dependent
pyridoxal 5'-phosphate
-
dependent
pyridoxal 5'-phosphate
dependent
pyridoxal 5'-phosphate
dependent
pyridoxal 5'-phosphate
-
4 pyridoxal phosphate molecules per tetramer
pyridoxal 5'-phosphate
-
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
-
reacts with L-allothreonine to form a stable 3-methyl aminoacrylate intermediate
pyridoxal 5'-phosphate
-
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
-
CBS is a pyridoxal 5'-phosphate-dependent enzyme
pyridoxal 5'-phosphate
-
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

-
-
S-adenosyl-L-methionine
-
stimulates
S-adenosyl-L-methionine
-
activation
S-adenosyl-L-methionine
-
allosterical regulation, increase of the enzyme's affinity for homocysteine
additional information

-
heme is no cofactor
-
additional information
-
heme is no cofactor
-
additional information
no dependence on heme
-
additional information
-
no dependence on heme
-
additional information
-
yeast cystathionine beta-synthase does not have a heme cofactor
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ca2+
-
contains 0.38 Ca atoms/subunit
Co2+
-
97.1% Fe2+ and 2.9% Co2+ in wild-type FeCBS enzyme, 8% Fe2+ and 92% Co2+ in the CoCBS enzyme variant
Co3+
-
cobalt-substituted variant of hCBS, i.e. Co hCBS, in which CoPPIX replaces FePPIX, i.e. heme. Co(III) hCBS is a unique Co-substituted heme protein: the Co(III) ion is 6-coordinate, low-spin, diamagnetic, and bears a cysteine(thiolate) as one of its axial ligands. Electronic absorption and MCD spectra of the Co-substituted heme protein, overview. Co(III) hCBS is slowly reduced to Co(II) hCBS, which contains a 5-coordinate, low-spin, S = 1/2 Co-porphyrin that does not retain the cysteine(thiolate) ligand. This form of Co(II)hCBS binds NO but not CO. Co(II) hCBS is reoxidized in the air to form a new Co(III) form, which does not contain a cysteine(thiolate) ligand. Maintaining the native heme ligation motif of wild-type Fe hCBS (Cys/His) is essential in maintaining maximal activity in Co hCBS
Zn2+
-
contains 0.35 Zn atoms/subunit
Fe

-
contains 0.67 Fe atoms/subunit, in minimal medium
Fe
-
contains 0.13 Fe atoms/subunit
Fe2+

-
ferrous human cystathionine beta-synthase loses activity during enzyme assay due to a ligand switch process
Fe2+
-
heme enzyme, 97.1% Fe2+ and 2.9% Co2+ in wild-type FeCBS enzyme, 8% Fe2+ and 92% Co2+ in the CoCBS enzyme variant
Fe2+
-
wild-type FePPIX, i.e. heme
Fe2+
-
contains 0.16 Fe atoms/subunit
Zn

-
contains 0.17 Zn atoms/subunit, in minimal medium
Zn
-
contains 0.25 Zn atoms/subunit
additional information

-
construction of a cobalt CBS, CoCBS, by metalloporphyrin replacement, which results in a high yield of fully active, high purity enzyme, in which heme is substituted by Co-protoporphyrin IX, CoPPIX. the enzyme contains 92% cobalt and 8% iron. CoCBS is indistinguishable from wild-type FeCBS in its activity, tetrameric oligomerization, PLP saturation and responsiveness to the allosteric activator, S-adenosyl-L-methionine
additional information
-
maintaining the native heme ligation motif of wild-type Fe hCBS (Cys/His) is essential in maintaining maximal activity in Co hCBS
additional information
-
Na+, K+, Li+, Ca2+, Mg2+, Zn2+, Co2+, no effect on activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(5Z)-5-[(4-hydroxy-3-methoxyphenyl)methylidene]-3-methyl-2-(methylsulfanyl)-3,5-dihydro-4H-imidazol-4-one
-
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
-
compound derived from polyandrocarpamines A and B, i.e. 2-aminoimidazolone compounds isolated from the ascidian Polyandrocarpa sp.
Amino-oxyacetate
-
complete inhibition at 0.05 mM
beta-chloro-L-alanine
-
-
Co3+
-
Co3+ has 30-60% of the specific activity of Fe3+-CBS
Dithionite
-
2fold decrease in enzyme activity due to altered oxidation state of the heme
Hg2+
-
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
L-cystathione
-
product inhibition
Mn3+
-
Mn3+ has 30-60% of the specific activity of Fe3+-CBS
p-chloromercuribenzoate
-
-
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
-
exerts an inhibitory effect on the enzyme, deletion is correlated with a 1fold increase in catalytic activity
-
titanium citrate
-
2fold decrease in enzyme activity due to altered oxidation state of the heme
2,4-Dichlorophenol

-
-
alizarin

-
-
aminooxyacetic acid

-
-
bithionol

-
-
carbon monoxide

-
carbon monoxide
-
binds to the prosthetic heme, stabilizing 6-coordinated CO-Fe(II)-histidine complex to block the activity
carbon monoxide
-
binds to the prosthetic heme, stabilizing 6-coordinated CO-Fe(II)-histidine complex to block the activity
closantel

-
-
CO

-
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
-
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
Dichlorophene

-
-
ellagic acid

-
-
Hexachlorophene

-
-
HgCl2

-
inhibits enzyme activity by interacting with the heme
hydroxylamine

-
-
hydroxylamine
-
complete inhibition at 1 mM
L-homocysteine

-
substrate inhibition
nitric oxide

-
nitric oxide
-
irreversible inhibition
NO

-
inhibits full length enzyme
purpurogallin

-
-
quercetin

-
-
Rafoxanide

-
-
additional information

-
the alternation of heme environment inactivates the enzyme
-
additional information
-
taurine activates some cystathionine beta-synthase mutants slightly, while it slightly inhibits the wild-type enzyme and other cystathionine beta-synthase mutants
-
additional information
-
not inhibited by nitric oxide
-
additional information
-
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
-
additional information
-
not inhibited by nitric oxide
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
AdoMet
-
allosteric regulator, 1mol per mole of monomeric subunit activates the enzyme 2fold
betaine
-
activates, effects on wild-type and mutant enzymes, overview
delta-aminolevulinic acid
-
activates, effects on wild-type and mutant enzymes, overview
Ethionine
-
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
glycerol
-
activates, effects on wild-type and mutant enzymes, overview
S-adenosylhomocysteine
-
stimulates activity 1.1fold at 0.48 mM
sinefungin
-
stimulates activity 1.28fold at 1 mM
sodium nitroprusside
-
enhances activity by interacting with cysteine residues, N-ethylmaleimide abolishes this effect
tumor necrosis factor-alpha
-
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
-
pyridoxal 5'-phosphate

-
-
pyridoxal 5'-phosphate
-
-
S-adenosyl-L-methionine

structure of the regulatory, energy-sensing CBS domains and mechanism for allosteric activation by S-adenoyl-L-methionine, overview
S-adenosyl-L-methionine
-
-
S-adenosyl-L-methionine
-
S-adenosyl-L-methionine
-
-
S-adenosyl-L-methionine
-
S-adenosyl-L-methionine
-
stimulates
S-adenosyl-L-methionine
-
activates
S-adenosyl-L-methionine
-
allosteric activation
S-adenosyl-L-methionine
-
allosteric activator
S-adenosyl-L-methionine
-
2fold activation, allosteric regulator
S-adenosyl-L-methionine
3fold activation, allosteric regulator of the full length enzyme, does not activate the truncated enzyme
S-adenosyl-L-methionine
activates 2fold
S-adenosyl-L-methionine
-
activates full length enzyme, but not the truncated core, 4 S-adenosyl-L-methionine molecules per tetramer
S-adenosyl-L-methionine
-
induces conformational change
S-adenosyl-L-methionine
-
the enzyme is allosterically activated by S-adenosyl-L-methionine under normal conditions but is destabilized under pathological conditions
S-adenosyl-L-methionine
-
an allosteric activator
S-adenosyl-L-methionine
-
about 4fold increase of specific activity in the presence of 0.25 mM S-adenosyl-L-methionine
S-adenosyl-L-methionine
-
activity increases in the presence of
S-adenosyl-L-methionine
-
activates CBS by 13.6fold in Hep-G2 cell lysate
S-adenosyl-L-methionine
-
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
-
the addition of S-adenosyl-L-methionine nearly doubles enzyme activity
S-adenosyl-L-methionine
-
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
AdoMet is a V-type allosteric activator
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
-
-
S-adenosyl-L-methionine
-
the enzyme is allosterically activated by S-adenosyl-L-methionine under normal conditions but is destabilized under pathological conditions
S-adenosyl-L-methionine
-
-
S-adenosyl-L-methionine
-
S-adenosyl-L-methionine
-
3fold activation, allosteric regulator
additional information

enzyme is not allosterically regulated by AdoMet
-
additional information
-
enzyme is not allosterically regulated by AdoMet
-
additional information
enzyme is more active under oxidizing conditions
-
additional information
-
enzyme is more active under oxidizing conditions
-
additional information
-
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
-
additional information
-
taurine activates some cystathionine beta-synthase mutants slightly, while it slightly inhibits the wild-type enzyme and other cystathionine beta-synthase mutants
-
additional information
-
oxidizing conditions increase the enzyme activity by 2fold
-
additional information
-
enzyme is not dependent on heme
-
additional information
S-adenosyl-L-methionine does not activate
-
additional information
-
S-adenosyl-L-methionine does not activate
-
additional information
-
enzyme can not be activated by S-adenosyl-L-methionine
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1.72 - 24
2-mercaptoethanol
68
DL-homocysteine
-
cosubstrate L-Ser
0.083 - 0.9
L-cystathionine
additional information
additional information
-
pre-steady-state kinetic analysis of enzyme-monitored turnover during cystathionine beta-synthase-catalyzed H2S generation, overview
-
1.72
2-mercaptoethanol

-
-
5.58
2-mercaptoethanol
-
-
24
2-mercaptoethanol
-
cosubstrate L-Cys
5.6
cysteamine

-
pH 8.0, 37°C, UV assay
6.6
cysteamine
-
pH 8.0, 37°C, Mudd assay
4.7
H2S

cosubstrate L-serine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
5.02
H2S
cosubstrate L-serine, pH 7.4, 37°C
0.05
homocysteine

-
S466L mutant, 37°C, absence of S-adenosyl-L-methionine
0.08
homocysteine
-
wild-type enzyme, 37°C, presence of S-adenosyl-L-methionine
0.1
homocysteine
-
I435T mutant, 37°C, absence of S-adenosyl-L-methionine
0.17
homocysteine
-
wild-type enzyme, 37°C, absence of S-adenosyl-L-methionine
0.2
homocysteine
-
I435T mutant, 37°C, presence of S-adenosyl-L-methionine
0.8
homocysteine
-
enzyme composed of MW 48000 subunits
1.1
homocysteine
-
absence of S-adenosyl-L-methionine
1.2
homocysteine
-
37°C, L-serine pre-treatment
2
homocysteine
-
37°C, pH 8.6, mutant enzyme I278T
2.3
homocysteine
-
37°C, homocysteine pre-treatment
3.41
homocysteine
-
enzyme form beta
3.98
homocysteine
-
enzyme form alpha
4.8
homocysteine
-
absence of S-adenosyl-L-methionine, recombinant enzyme
5
homocysteine
-
presence of S-adenosyl-L-methionine, recombinant enzyme
5
homocysteine
-
pH 6.8, 37°C, full length enzyme after L-serine pre-treatment
7.17
homocysteine
-
37°C, pH 8.6, mutant enzyme R266K
7.17
homocysteine
-
37°C, pH 8.6, wild-type enzyme
9.7
homocysteine
-
pH 6.8, 37°C, deltaC143 mutant after L-serine pre-treatment
15
homocysteine
-
pH 6.8, 37°C, full length enzyme after homocysteine pre-treatment
18
homocysteine
-
cosubstrate L-Ser
25
homocysteine
-
enzyme composed of MW 68000 subunits
67
homocysteine
-
pH 6.8, 37°C, deltaC143 mutant after homocysteine pre-treatment
0.13
L-Cys

-
-
36
L-Cys
-
cosubstrate 2-mercaptoethanol
0.083
L-cystathionine

-
pH 8.6, 37°C, reverse reaction
0.13
L-cystathionine
-
recombinant 6-His-tagged enzyme, in 50 mM Tris (pH 8.6), at 25°C
0.14
L-cystathionine
-
reverse reaction (L-cystathionine hydrolysis), wild-type
0.9
L-cystathionine
-
reverse reaction (L-cystathionine hydrolysis), mutant S289A
2
L-cysteine

-
wild-type
3
L-cysteine
formation of L-cystathionine, mutant A70S, pH 7.5, 37°C
3.59
L-cysteine
-
37°C, pH 8.6, mutant enzyme I278T
4.3
L-cysteine
-
37°C, pH 8.6, mutant enzyme R266K
4.4
L-cysteine
-
mutant R266K
5.4
L-cysteine
-
mutant H67A
5.5
L-cysteine
-
mutant R266K
5.9
L-cysteine
formation of L-cystathionine, wild-type, pH 7.5, 37°C
6.11
L-cysteine
-
37°C, pH 8.6, wild-type enzyme
8.11
L-cysteine
cosubstrate H2O, pH 7.4, 37°C
8.41
L-cysteine
cosubstrate H2O, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
8.9
L-cysteine
formation of (2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid), wild-type, pH 7.5, 37°C
13.41
L-cysteine
cosubstrate L-homocysteine, pH 7.4, 37°C
15.92
L-cysteine
cosubstrate L-homocysteine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
37
L-cysteine
formation of (2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid), mutant E223G, pH 7.5, 37°C
37
L-cysteine
formation of L-cystathionine, mutant E223G, pH 7.5, 37°C
0.16
L-homocysteine

-
mutant S289A
0.21
L-homocysteine
-
wild-type
0.29
L-homocysteine
wild-type, 37°C, pH not specified in the publication
0.3
L-homocysteine
-
pH 8.6, 37°C
0.31
L-homocysteine
mutant K523Sfs?18, 37°C, pH not specified in the publication
0.32
L-homocysteine
mutant S500L, 37°C, pH not specified in the publication
0.32
L-homocysteine
A0A1J9VES8
wild-type, production of H2S, pH 8.2, 37°C
0.35
L-homocysteine
mutant V449G, 37°C, pH not specified in the publication
0.4
L-homocysteine
formation of L-cystathionine, mutant E223G, pH 7.5, 37°C
0.4
L-homocysteine
mutant D444N, 37°C, pH not specified in the publication
0.43
L-homocysteine
-
recombinant 6-His-tagged enzyme, in 50 mM Tris (pH 8.6), at 25°C
0.47
L-homocysteine
mutant L540Q, 37°C, pH not specified in the publication
0.54
L-homocysteine
formation of L-cystathionine, wild-type, pH 7.5, 37°C
0.69
L-homocysteine
mutant P427L, 37°C, pH not specified in the publication
1
L-homocysteine
-
37°C, pH 8.0, wild-type enzyme, with S-adenosyl-L-methionine
1
L-homocysteine
synthesis of L-cystathionine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
1.04
L-homocysteine
-
37°C, pH 8.0, wild-type enzyme, without S-adenosyl-L-methionine
1.04
L-homocysteine
synthesis of L-cystathionine, pH 7.4, 37°C
1.1
L-homocysteine
-
mutant enzyme S466L, in the presence of 0.25 mM S-adenosyl-L-methionine
1.3
L-homocysteine
-
mutant R266K
1.51
L-homocysteine
A0A1J9VES8
mutant E220R, pH 8.2, 37°C
1.6
L-homocysteine
-
mutant R266K
2.5
L-homocysteine
-
wild type enzyme, in the presence of 0.25 mM S-adenosyl-L-methionine
2.73
L-homocysteine
A0A1J9VES8
wild-type, pH 8.2, 37°C
3.4
L-homocysteine
-
mutant H67A
3.59
L-homocysteine
A0A1J9VES8
mutant A72S, pH 8.2, 37°C
3.7
L-homocysteine
-
pH 8.0, 37°C
4.31
L-homocysteine
cosubstrate L-cysteine, pH 7.4, 37°C
4.48
L-homocysteine
cosubstrate L-cysteine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
5
L-homocysteine
-
wild-type
20
L-homocysteine
formation of L-cystathionine, mutant A70S, pH 7.5, 37°C
0.91
L-Ser

-
-
2
L-Ser
-
no influence of S-adenosyl-L-methionine, recombinant enzyme
3.1
L-Ser
-
absence of S-adenosyl-L-methionine
6
L-Ser
-
value is reduced 8fold by S-adenosyl-L-methionine
0.7
L-serine

-
wild-type
0.77
L-serine
-
mutant enzyme S466L, in the presence of 0.25 mM S-adenosyl-L-methionine
0.78
L-serine
-
wild type enzyme, in the presence of 0.25 mM S-adenosyl-L-methionine
1.2
L-serine
-
pH 8.6, 37°C
1.2
L-serine
-
pH 8.0, 37°C, reaction with cysteamine, continous UV assay
1.27
L-serine
cosubstrate H2S, pH 7.4, 37°C
1.32
L-serine
cosubstrate H2S, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
1.41
L-serine
-
37°C, pH 8.0, wild-type enzyme, without -adenosyl-L-methionine
1.41
L-serine
-
37°C, pH 8.6, mutant enzyme I278T
1.41
L-serine
synthesis of L-cystathionine, pH 7.4, 37°C
1.74
L-serine
-
37°C, pH 8.6, wild-type enzyme
1.9
L-serine
mutant L540Q, 37°C, pH not specified in the publication
2
L-serine
-
pH 6.8, 37°C, full length enzyme after L-serine pre-treatment
2
L-serine
mutant P427L, 37°C, pH not specified in the publication
2.1
L-serine
mutant S500L, 37°C, pH not specified in the publication
2.13
L-serine
-
37°C, pH 8.0, wild-type enzyme, with S-adenosyl-L-methionine
2.13
L-serine
synthesis of L-cystathionine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
2.2
L-serine
-
pH 8.0, 37°C, reaction with cysteamine, Mudd assay
2.7
L-serine
mutant V449G, 37°C, pH not specified in the publication
2.76
L-serine
-
37°C, pH 8.6, mutant enzyme R266K
2.9
L-serine
mutant D444N, 37°C, pH not specified in the publication
3.5
L-serine
-
37°C, homocysteine pre-treatment
3.6
L-serine
-
wild-type enzyme, 37°C, presence of S-adenosyl-L-methionine
3.6
L-serine
wild-type, 37°C, pH not specified in the publication
3.7
L-serine
mutant K523Sfs?18, 37°C, pH not specified in the publication
4.2
L-serine
-
I435T mutant, 37°C, absence of S-adenosyl-L-methionine
4.5
L-serine
-
I435T mutant, 37°C, presence of S-adenosyl-L-methionine
4.9
L-serine
-
37°C, L-serine pre-treatment
4.9
L-serine
-
wild-type enzyme, 37°C, absence of S-adenosyl-L-methionine
4.9
L-serine
-
pH 8.0, 37°C, reaction with L-homocysteine
5
L-serine
-
recombinant 6-His-tagged enzyme, in 50 mM Tris (pH 8.6), at 25°C
5.5
L-serine
-
pH 6.8, 37°C, full length enzyme after homocysteine pre-treatment
7.2
L-serine
-
S466L mutant, 37°C, absence of S-adenosyl-L-methionine
14
L-serine
-
pH 6.8, 37°C, deltaC143 mutant after homocysteine pre-treatment
18
L-serine
-
pH 6.8, 37°C, deltaC143 mutant after L-serine pre-treatment
27.1
L-serine
-
mutant S289A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0045 - 6.08
L-cystathionine
0.024 - 26.78
L-homocysteine
additional information
additional information
-
the kcat for the generation of H2S by cystathionine beta-synthase of 55/s at 37°C, via the condensation of cysteine and homocysteine is 18fold faster than that for the beta-elimination and rehydration to form serine of 3/s-
-
0.35
H2S

cosubstrate L-serine, pH 7.4, 37°C
0.78
H2S
cosubstrate L-serine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
5.9
homocysteine

-
I435T mutant, 37°C, absence of S-adenosyl-L-methionine
6.2
homocysteine
-
wild-type enzyme, 37°C, absence of S-adenosyl-L-methionine
15.5
homocysteine
-
S466L mutant, 37°C, absence of S-adenosyl-L-methionine
32.1
homocysteine
-
I435T mutant, 37°C, presence of S-adenosyl-L-methionine
34
homocysteine
-
wild-type enzyme, 37°C, presence of S-adenosyl-L-methionine
0.0045
L-cystathionine

-
reverse reaction (L-cystathionine hydrolysis), mutant S289A
0.083
L-cystathionine
-
S82A mutant, pH 8.6, 37°C
0.133
L-cystathionine
-
T85A mutant, pH 8.6, 37°C
0.418
L-cystathionine
-
Y158F mutant, pH 8.6, 37°C
0.56
L-cystathionine
-
pH 8.6, 37°C
0.56
L-cystathionine
-
wild-type enzyme, pH 8.6, 37°C
1.03
L-cystathionine
-
reverse reaction (L-cystathionine hydrolysis), wild-type
6.08
L-cystathionine
-
pH 8.6, 37°C
6.08
L-cystathionine
-
wild-type enzyme, pH 8.6, 37°C
0.022
L-cysteine

formation of (2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid), mutant E223G, pH 7.5, 37°C
0.04
L-cysteine
-
37°C, pH 8.6, mutant enzyme I278T
0.6
L-cysteine
formation of L-cystathionine, mutant E223G, pH 7.5, 37°C
1.06
L-cysteine
cosubstrate H2O, pH 7.4, 37°C
1.1
L-cysteine
formation of (2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid), wild-type, pH 7.5, 37°C
1.41
L-cysteine
cosubstrate H2O, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
1.95
L-cysteine
-
37°C, pH 8.6, mutant enzyme R266K
2
L-cysteine
formation of L-cystathionine, mutant A70S, pH 7.5, 37°C
3.13
L-cysteine
-
37°C, pH 8.6, wild-type enzyme
4.39
L-cysteine
-
37°C, pH 8.6, wild-type enzyme
7.09
L-cysteine
cosubstrate L-homocysteine, pH 7.4, 37°C
7.6
L-cysteine
formation of L-cystathionine, wild-type, pH 7.5, 37°C
31.34
L-cysteine
cosubstrate L-homocysteine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
0.024
L-homocysteine

-
recombinant 6-His-tagged enzyme, in 50 mM Tris (pH 8.6), at 25°C
0.031 - 0.51
L-homocysteine
-
37°C, pH 8.6, wild-type enzyme
0.04 - 1.97
L-homocysteine
-
37°C, pH 8.6, mutant enzyme R266K
0.09
L-homocysteine
-
37°C, pH 8.6, mutant enzyme I278T
0.85
L-homocysteine
-
cosubstrate: L-serine, mutant S289A
3.3
L-homocysteine
-
37°C, pH 8.0, wild-type enzyme, without S-adenosyl-L-methionine
3.38
L-homocysteine
A0A1J9VES8
wild-type, production of H2S, pH 8.2, 37°C
4.66
L-homocysteine
-
37°C, pH 8.0, wild-type enzyme, without S-adenosyl-L-methionine
4.66
L-homocysteine
cosubstrate L-serine, pH 7.4, 37°C
5.74
L-homocysteine
A0A1J9VES8
mutant E220R, pH 8.2, 37°C
7.93
L-homocysteine
-
37°C, pH 8.6, wild-type enzyme
8.17
L-homocysteine
cosubstrate L-cysteine, pH 7.4, 37°C
8.39
L-homocysteine
A0A1J9VES8
wild-type, pH 8.2, 37°C
9.06
L-homocysteine
-
37°C, pH 8.6, mutant enzyme R266K
10.91
L-homocysteine
A0A1J9VES8
mutant A72S, pH 8.2, 37°C
12.7
L-homocysteine
-
37°C, pH 8.0, wild-type enzyme, with S-adenosyl-L-methionine
12.7
L-homocysteine
cosubstrate L-serine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
17
L-homocysteine
-
cosubstrate: L-serine, wild-type
21.5
L-homocysteine
-
pH 8.6, 37°C
26.78
L-homocysteine
cosubstrate L-cysteine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
0.052 - 2.1
L-serine

-
37°C, pH 8.6, wild-type enzyme
0.082
L-serine
-
Q157H mutant, pH 8.6, 37°C
0.15
L-serine
-
37°C, pH 8.6, mutant enzyme I278T
0.39
L-serine
cosubstrate H2S, pH 7.4, 37°C
0.45
L-serine
-
T81A mutant, pH 8.6, 37°C
0.52
L-serine
-
37°C, pH 8.0, wild-type enzyme, with S-adenosyl-L-methionine
0.62
L-serine
cosubstrate H2S, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
0.85
L-serine
-
cosubstrate: L-homocysteine, mutant S289A
1.3
L-serine
-
pH 8.0, 37°C, reaction with cysteamine, continous UV assay
1.67
L-serine
-
recombinant 6-His-tagged enzyme, in 50 mM Tris (pH 8.6), at 25°C
2.5
L-serine
-
pH 8.0, 37°C, reaction with cysteamine, Mudd assay
2.9
L-serine
-
37°C, pH 8.6, mutant enzyme R266K
3.67
L-serine
-
37°C, pH 8.0, wild-type enzyme, without S-adenosyl-L-methionine
3.67
L-serine
cosubstrate L-homocysteine, pH 7.4, 37°C
5.3
L-serine
-
S82A mutant, pH 8.6, 37°C
5.4
L-serine
-
wild-type enzyme, 37°C, absence of S-adenosyl-L-methionine
5.9
L-serine
-
I435T mutant, 37°C, absence of S-adenosyl-L-methionine
7.5
L-serine
-
pH 8.0, 37°C, reaction with L-homocysteine
8.2
L-serine
-
Y158F mutant, pH 8.6, 37°C
10.19
L-serine
-
37°C, pH 8.6, wild-type enzyme
13.2
L-serine
-
T85A mutant, pH 8.6, 37°C
14.01
L-serine
-
37°C, pH 8.0, wild-type enzyme, with S-adenosyl-L-methionine
14.01
L-serine
cosubstrate L-homocysteine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
14.6
L-serine
-
S466L mutant, 37°C, absence of S-adenosyl-L-methionine
14.7
L-serine
-
37°C, L-serine pre-treatment
15.8
L-serine
-
I435T mutant, 37°C, presence of S-adenosyl-L-methionine
16.8
L-serine
-
37°C, homocysteine pre-treatment
17
L-serine
-
cosubstrate: L-homocysteine, wild-type
19
L-serine
-
pH 6.8, 37°C, deltaC143 mutant after L-serine pre-treatment
19.7
L-serine
-
wild-type enzyme, 37°C, presence of S-adenosyl-L-methionine
21
L-serine
-
pH 6.8, 37°C, full length enzyme after L-serine pre-treatment
21.5
L-serine
-
wild-type enzyme, pH 8.6, 37°C
39
L-serine
-
pH 6.8, 37°C, full length enzyme after homocysteine pre-treatment
45
L-serine
-
pH 6.8, 37°C, deltaC143 mutant after homocysteine pre-treatment
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.005 - 7.5
L-cystathionine
0.07
H2S

cosubstrate L-serine, pH 7.4, 37°C
0.17
H2S
cosubstrate L-serine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
0.005
L-cystathionine

-
reverse reaction (L-cystathionine hydrolysis), mutant S289A
7.5
L-cystathionine
-
reverse reaction (L-cystathionine hydrolysis), wild-type
0.0006
L-cysteine

formation of (2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid), mutant E223G, pH 7.5, 37°C
0.12
L-cysteine
formation of (2R,2'R)-3,3'-sulfanediylbis(2-aminopropanoic acid), wild-type, pH 7.5, 37°C
0.13
L-cysteine
cosubstrate H2O, pH 7.4, 37°C
0.18
L-cysteine
cosubstrate H2O, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
0.53
L-cysteine
cosubstrate L-homocysteine, pH 7.4, 37°C
1.3
L-cysteine
formation of L-cystathionine, wild-type, pH 7.5, 37°C
1.5
L-cysteine
formation of L-cystathionine, mutant A70S, pH 7.5, 37°C
1.98
L-cysteine
cosubstrate L-homocysteine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
8.9
L-cysteine
formation of L-cystathionine, mutant E223G, pH 7.5, 37°C
0.15
L-homocysteine

formation of L-cystathionine, mutant A70S, pH 7.5, 37°C
0.83
L-homocysteine
formation of L-cystathionine, mutant E223G, pH 7.5, 37°C
1.93
L-homocysteine
cosubstrate L-cysteine, pH 7.4, 37°C
2.8
L-homocysteine
mutant D444N, 37°C, pH not specified in the publication
3
L-homocysteine
wild-type, 37°C, pH not specified in the publication
3.04
L-homocysteine
A0A1J9VES8
mutant A72S, pH 8.2, 37°C
3.06
L-homocysteine
A0A1J9VES8
wild-type, pH 8.2, 37°C
3.83
L-homocysteine
A0A1J9VES8
mutant E220R, pH 8.2, 37°C
4.61
L-homocysteine
synthesis of L-cystathionine, pH 7.4, 37°C
4.71
L-homocysteine
mutant V449G, 37°C, pH not specified in the publication
4.82
L-homocysteine
mutant S500L, 37°C, pH not specified in the publication
5.22
L-homocysteine
mutant K523Sfs?18, 37°C, pH not specified in the publication
5.23
L-homocysteine
mutant P427L, 37°C, pH not specified in the publication
6.02
L-homocysteine
cosubstrate L-cysteine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
6.3
L-homocysteine
-
mutant S289A
10.56
L-homocysteine
A0A1J9VES8
wild-type, production of H2S, pH 8.2, 37°C
11
L-homocysteine
mutant L540Q, 37°C, pH not specified in the publication
12.74
L-homocysteine
synthesis of L-cystathionine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
14
L-homocysteine
formation of L-cystathionine, wild-type, pH 7.5, 37°C
80
L-homocysteine
-
wild-type
0.031
L-serine

-
mutant S289A
0.28
L-serine
cosubstrate H2S, pH 7.4, 37°C
0.34
L-serine
wild-type, 37°C, pH not specified in the publication
0.46
L-serine
mutant D444N, 37°C, pH not specified in the publication
0.47
L-serine
cosubstrate H2S, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
0.71
L-serine
mutant K523Sfs?18, 37°C, pH not specified in the publication
0.83
L-serine
mutant V449G, 37°C, pH not specified in the publication
1.06
L-serine
mutant S500L, 37°C, pH not specified in the publication
1.93
L-serine
mutant P427L, 37°C, pH not specified in the publication
2.63
L-serine
synthesis of L-cystathionine, pH 7.4, 37°C
3.61
L-serine
mutant L540Q, 37°C, pH not specified in the publication
7.61
L-serine
synthesis of L-cystathionine, presence of S-adenosyl-L-methionine, pH 7.4, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.045
-
recombinant 6-His-tagged enzyme from crude extract, in 50 mM Tris (pH 8.6), at 25°C
0.68
-
without pyridoxal 5'-phosphate, without S-adenosyl-L-methionine, mutant R266M
1.91
-
without pyridoxal 5'-phosphate, without S-adenosyl-L-methionine, mutant R266K
10.3
full-length ferric wild type enzyme, at 37°C and pH 8
105.2
-
purified recombinant CoCBS, pH 8.6, 37°C
2.31
-
without pyridoxal 5'-phosphate, without S-adenosyl-L-methionine, mutant H67A
2.65
-
wild-type enzyme in the presence of S-adenosyl-L-methionine
2.8
full-length ferrous wild type enzyme, at 37°C and pH 8
3.17
-
recombinant 6-His-tagged enzyme after purification, in 50 mM Tris (pH 8.6), at 25°C
3.6
-
without pyridoxal 5'-phosphate, without S-adenosyl-L-methionine, wild-type
3.8
truncated ferrous mutant enzyme R224A, at 37°C and pH 8
3.9
-
with pyridoxal 5'-phosphate, with S-adenosyl-L-methionine, mutant R266M
3.95
-
D144N mutant in the presence of S-adenosyl-L-methionine
4
truncated ferric mutant enzyme R51A, at 37°C and pH 8
5.71
-
with pyridoxal 5'-phosphate, with S-adenosyl-L-methionine, mutant R266K
6
truncated ferric mutant enzyme R224A, at 37°C and pH 8
8
truncated ferrous wild type enzyme, at 37°C and pH 8
1.2

truncated ferrous mutant enzyme R51A, at 37°C and pH 8
1.3

full-length ferrous mutant enzyme R224A, at 37°C and pH 8
1.3
full-length ferrous mutant enzyme R51A, at 37°C and pH 8
2.2

full-length ferric mutant enzyme R224A, at 37°C and pH 8
2.2
full-length ferric mutant enzyme R51A, at 37°C and pH 8
5.2

truncated ferric wild type enzyme, at 37°C and pH 8
5.2
-
with pyridoxal 5'-phosphate, with S-adenosyl-L-methionine, mutant H67A
5.2
-
with pyridoxal 5'-phosphate, with S-adenosyl-L-methionine, wild-type
additional information

-
continous spectrometric assay for cystathionine beta-synthase
additional information
-
cystathionine synthesis activity of FeCBS and CoCBS
additional information
-
specific activities of wild-type and mutants in presence of activators, overview
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