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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

Reaction

L-serine
+
L-homocysteine
=
L-cystathionine
 +
H2O

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

     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.22 cystathionine beta-synthase

Cloned

Cloned on EC 4.2.1.22 - cystathionine beta-synthase

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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a mutant form of the human cystathionine beta-synthase protein, I278T, is expressed in Saccharomyces cerevisiae
-
a truncated form of CBS comprising the catalytic core is used for mutational analysis
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CBS gene encoding the truncated yCBS (residues 1-353), lacking the regulatory domain, is expressed with a C-terminal, 6-His affinity tag in Escherichia coli
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CDCP2 is expressed in Escherichia coli BL21 (DE3) cells, selenomethionine-substituted CDCP2 is expressed using B834 (DE3) cells
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eight CBS mutants are expressed in Escherichia coli in the presence of chemical chaperones such as ethanol, dimethyl sulfoxide, or trimethylamine-N-oxide
-
expressed as a GST-fusion protein in Escherichia coli
-
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli strain DH10B
-
expressed in heme-deficient strains of Saccharomyces cerevisiae and Escherichia coli
-
expression in CHO/duk- cell line
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expression in Escherichia coli
expression in yeast or in Escherichia coli
-
expression of cystathionine beta-synthase in Escherichia coli strain BL21(DE3)
-
expression of human mutant CBS proteins in Saccharomyces cerevisiae reveals that the disease causing mutation severely inhibits enzyme activity and cannot support growth of yeast on cysteine-free media. The osmolyte chemical chaperones glycerol, trimethylamine-N-oxide, dimethylsulfoxide, proline or sorbitol, when added to yeast media, allows growth on cysteine-free media and causes increased enzyme activity from I278T mutant protein. The increase in enzyme activity is associated with stabilization of the tetramer form of the enzyme. This effect is not specific to yeast, as addition of the chaperone glycerol results in increased I278T activity when the enzyme is produced either in Escherichia coli or in a coupled in vitro transcription/translation reaction. No stimulation of specific activity is observed when chaperones are added directly to purified I278T indicating that the presence of chemical chaperones is required during translation
-
expression of mutant 45CBS and wild-type CBS in Escherichia coli
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expression of wild type and truncated human cystathionine beta-synthase enzyme in Escherichia coli
-
expression of wild-type and Co-subsituted CBS as GST-tagged enzymes in Escherichia coli strain Rosetta 2 (DE3)
-
full-length CBS and truncated enzyme containing residues 1-397 are expressed in Escherichia coli BL21 cells
fusion protein with glutathione S-transferase
-
genotyping of wild-type and mutant CBSs, determination of mutations in patients with homocystinuria due to CBS deficiency, overview
in a recombinant expression system (pGEX4T1/hCBSDELTAC143) that produces a fusion protein with glutathione S-transferase
-
mutant enzymes K102N, P78R and P78R/K102N are expressed in Escherichia coli and purified as glutathione S-transferase fusion proteins using recombinant expression
-
N-terminal cystathionine beta-synthase domain fused to the C-terminal Zn ribbon domain is overexpressed in Escherichia coli
the truncated human CBS enzyme consisting of residue 1-397 is expressed in the glutathione S-transferase fusion expression system
-
transgenic mice that contain the human cystathionine beta-synthase cDNA under control of the zinc-inducible metallothionein promoter (Tg-CBS). In the presence of zinc, Tg-CBS mice have a 2fold to 4fold increase in liver and kidney cystathionine beta-synthase activity compared with nontransgenic littermates
-
truncated form fused with glutathione S-transferase
-
truncated human CBS lacking 143 amino acids at the C-terminus is expressed as a fusion protein with glutathione S-transferase in the Escherichia coli
truncated protein lacking the C-terminal domain is expressed
-
wild type enzyme is expressed in Mus musculus and mutant enzyme S466L is expressed in Saccharomyces cerevisiae strain WY35 and in Mus musculus
-