Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.5.1.134 - cystathionine beta-synthase (O-acetyl-L-serine) and Organism(s) Bacillus subtilis and UniProt Accession O05394

for references in articles please use BRENDA:EC2.5.1.134
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
A pyridoxal 5'-phosphate protein. The enzyme, purified from the bacterium Bacillus subtilis, also has a low activity with L-serine (cf. EC 4.2.1.22, cystathionine beta-synthase).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Bacillus subtilis
UNIPROT: O05394
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
cystathionine gamma-lyase, MCCB, O-acetylserine dependent cystathionine beta-synthase, YrhB, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cystathionine gamma-lyase
-
MCCB
-
-
-
-
O-acetylserine dependent cystathionine beta-synthase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
O-acetyl-L-serine:L-homocysteine 2-amino-2-carboxyethyltransferase
A pyridoxal 5'-phosphate protein. The enzyme, purified from the bacterium Bacillus subtilis, also has a low activity with L-serine (cf. EC 4.2.1.22, cystathionine beta-synthase).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-cystathionine + acetate
O-acetyl-L-serine + L-homocysteine
show the reaction diagram
-
-
-
?
additional information
?
-
enzyme displays both cystathionine lyase and homocysteine gamma-lyase activities in vitro
-
-
?
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-cystathionine + acetate
O-acetyl-L-serine + L-homocysteine
show the reaction diagram
-
-
-
?
additional information
?
-
enzyme displays both cystathionine lyase and homocysteine gamma-lyase activities in vitro
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
L-cystathionine
pH 7.5, 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cf. EC 4.4.1.1
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
mutants inactivated for yrhB grow similarly to the wild-type strain in the presence of methionine. The yrhB and yrhA genes form an operon together with yrrT, mtnN, and yrhC
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hullo, M.F.; Auger, S.; Soutourina, O.; Barzu, O.; Yvon, M.; Danchin, A.; Martin-Verstraete, I.
Conversion of methionine to cysteine in Bacillus subtilis and its regulation
J. Bacteriol.
189
187-197
2007
Bacillus subtilis (O05394), Bacillus subtilis 168 (O05394)
Manually annotated by BRENDA team