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Information on EC 4.1.1.100 - prephenate decarboxylase and Organism(s) Bacillus subtilis and UniProt Accession P39638

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.100 prephenate decarboxylase
IUBMB Comments
The enzyme, characterized from the bacterium Bacillus subtilis, is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. The enzyme isomerizes only the pro-R double bond in prephenate.
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Bacillus subtilis
UNIPROT: P39638
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The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
prephenate decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
non-aromatizing prephenate decarboxylase
-
SYSTEMATIC NAME
IUBMB Comments
prephenate carboxy-lyase (3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate-forming)
The enzyme, characterized from the bacterium Bacillus subtilis, is involved in the biosynthesis of the nonribosomally synthesized dipeptide antibiotic bacilysin, composed of L-alanine and L-anticapsin. The enzyme isomerizes only the pro-R double bond in prephenate.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
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
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
show the reaction diagram
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
prephenate
pH 8, 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.2
prephenate
pH 8, 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
45.2
prephenate
pH 8, 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme from the bacterium Bacillus subtilis is involved in the biosynthesis of the nonproteinogenic amino acid tetrahydrotyrosine a component of the dipeptide antibiotic bacilysin
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mahlstedt, S.A.; Walsh, C.T.
Investigation of anticapsin biosynthesis reveals a four-enzyme pathway to tetrahydrotyrosine in Bacillus subtilis
Biochemistry
49
912-923
2010
Bacillus subtilis (P39638), Bacillus subtilis, Bacillus subtilis 168 (P39638)
Manually annotated by BRENDA team
Parker, J.B., Walsh, C.T.
Olefin isomerization regiochemistries during tandem action of BacA and BacB on prephenate in bacilysin biosynthesis
Biochemistry
51
3241-3251
2012
Bacillus subtilis (P39638), Bacillus subtilis 168 (P39638)
Manually annotated by BRENDA team