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Information on EC 4.2.1.22 - cystathionine beta-synthase and Organism(s) Drosophila melanogaster and UniProt Accession Q9VRD9

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.22 cystathionine beta-synthase
IUBMB Comments
A pyridoxal-phosphate protein. A multifunctional enzyme: catalyses beta-replacement reactions between L-serine, L-cysteine, cysteine thioethers, or some other beta-substituted alpha-L-amino acids, and a variety of mercaptans.
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This record set is specific for:
Drosophila melanogaster
UNIPROT: Q9VRD9
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Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
cbs, cystathionine beta-synthase, cystathionine-beta-synthase, cnnm2, cystathionine beta synthase, serine sulfhydrylase, serine sulfhydrase, ytcbs, hemoprotein h-450, cdcp2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Beta-thionase
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CBS
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-
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Cysteine synthase
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Hemoprotein H-450
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-
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Methylcysteine synthase
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-
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Serine sulfhydrase
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-
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Serine sulfhydrylase
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Serine sulphhydrase
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-
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-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-serine + L-homocysteine = L-cystathionine + H2O
show the reaction diagram
carbanion and aminacrylate intermediates in the CBS-catalyzed reaction, arrangement of the protein residues and pyridoxal 5'-phosphate cofactor in the active site pocket, and reaction mechanism, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
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C-S bond formation
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SYSTEMATIC NAME
IUBMB Comments
L-serine hydro-lyase (adding homocysteine; L-cystathionine-forming)
A pyridoxal-phosphate protein. A multifunctional enzyme: catalyses beta-replacement reactions between L-serine, L-cysteine, cysteine thioethers, or some other beta-substituted alpha-L-amino acids, and a variety of mercaptans.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-99-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-serine + L-homocysteine
L-cystathionine + H2O
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-serine + L-homocysteine
L-cystathionine + H2O
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
structure of the regulatory, energy-sensing CBS domains and mechanism for allosteric activation by S-adenoyl-L-methionine, overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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comparison of human, fruit fly and yeast enzymes. The fruit fly CBS and yeast CBS are not regulated by the allosteric activator of human CBS, S-adenosyl-L-methionine. The heme-containing Drosophila melanogaster CBS and human CBS show increased thermal stability and retention of the enzyme's catalytic activity
additional information
structural basis for substrate activation and regulation by cystathionine beta-synthase domains in cystathionine beta-synthase, allosteric regulation via the CBS domains, mechanism, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9VRD9_DROME
522
0
56882
TrEMBL
other Location (Reliability: 2)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme free or in complex with a carbanion and an aminoacrylate intermediate, X-ray diffraction structure determination and analysis at 1.70 A and 1.55 A resolution, respectively
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Koutmos, M.; Kabil, O.; Smith, J.L.; Banerjee, R.
Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine beta-synthase
Proc. Natl. Acad. Sci. USA
107
20958-20963
2010
Drosophila melanogaster (Q9VRD9)
Manually annotated by BRENDA team
Majtan, T.; Pey, A.L.; Fernandez, R.; Fernandez, J.A.; Martinez-Cruz, L.A.; Kraus, J.P.
Domain organization, catalysis and regulation of eukaryotic cystathionine beta-synthases
PLoS ONE
9
e105290
2014
Saccharomyces cerevisiae, Drosophila melanogaster, Homo sapiens
Manually annotated by BRENDA team