Any feedback?
No. of entries
Information on EC 4.1.1.100 - prephenate decarboxylase
for references in articles please use BRENDA:EC4.1.1.100
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
prephenate decarboxylase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
bacA
non-aromatizing prephenate decarboxylase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
prephenate = 3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
bacilysin biosynthesis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
Substrates: -
Products: -
Products: -
?
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
Substrates: 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
Products: -
Products: -
?
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
Substrates: BacA isomerizes only the pro-R double bond in prephenate
Products: -
Products: -
?
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
Substrates: decarboxylation and protonation at C6', with a shift of the participating double bond from the C5'-6' position to the C4-9 position
Products: the product can undergo a nonenzymatic isomerization to produce 3-(4-hydroxycyclohex-2-enylidene)-2-oxopropanoate
Products: the product can undergo a nonenzymatic isomerization to produce 3-(4-hydroxycyclohex-2-enylidene)-2-oxopropanoate
?
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
Substrates: 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
Products: -
Products: -
?
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
Substrates: decarboxylation and protonation at C6', with a shift of the participating double bond from the C5'-6' position to the C4-9 position
Products: the product can undergo a nonenzymatic isomerization to produce 3-(4-hydroxycyclohex-2-enylidene)-2-oxopropanoate
Products: the product can undergo a nonenzymatic isomerization to produce 3-(4-hydroxycyclohex-2-enylidene)-2-oxopropanoate
?
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
Substrates: -
Products: -
Products: -
?
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
Substrates: BacA isomerizes only the pro-R double bond in prephenate
Products: -
Products: -
?
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
-
Substrates: -
Products: -
Products: -
?
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
-
Substrates: the enzyme is involved in the biosynthesis of the nonribosomal glycopeptides aeruginoside 126A and B. These natural products contain the unusual amino acid residue 2-carboxy-6-hydroxy-octahydroindole
Products: the product is non-enzymatically isomerized to the thermodynamically favored conjugated exocyclic diene 3-((1R,4R)-4-hydroxycyclohexa-2-enylidene)-2-oxopropanoate
Products: the product is non-enzymatically isomerized to the thermodynamically favored conjugated exocyclic diene 3-((1R,4R)-4-hydroxycyclohexa-2-enylidene)-2-oxopropanoate
?
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
-
Substrates: -
Products: -
Products: -
?
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
-
Substrates: the enzyme is involved in the biosynthetic pathway to the proteasome inhibitor salinosporamide A. SalX is relevant to the production of the nonproteinogenic amino acid building block cyclohexenylalanine
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
Substrates: -
Products: -
Products: -
?
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
Substrates: 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
Products: -
Products: -
?
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
Substrates: 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
Products: -
Products: -
?
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
Substrates: -
Products: -
Products: -
?
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
-
Substrates: the enzyme is involved in the biosynthesis of the nonribosomal glycopeptides aeruginoside 126A and B. These natural products contain the unusual amino acid residue 2-carboxy-6-hydroxy-octahydroindole
Products: the product is non-enzymatically isomerized to the thermodynamically favored conjugated exocyclic diene 3-((1R,4R)-4-hydroxycyclohexa-2-enylidene)-2-oxopropanoate
Products: the product is non-enzymatically isomerized to the thermodynamically favored conjugated exocyclic diene 3-((1R,4R)-4-hydroxycyclohexa-2-enylidene)-2-oxopropanoate
?
prephenate
3-[(4S)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
-
Substrates: the enzyme is involved in the biosynthetic pathway to the proteasome inhibitor salinosporamide A. SalX is relevant to the production of the nonproteinogenic amino acid building block cyclohexenylalanine
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
physiological function
-
the enzyme is involved in the biosynthesis of the nonribosomal glycopeptides aeruginoside 126A and B. These natural products contain the unusual amino acid residue 2-carboxy-6-hydroxy-octahydroindole
physiological function
-
the enzyme is involved in the biosynthetic pathway to the proteasome inhibitor salinosporamide A. SalX is relevant to the production of the nonproteinogenic amino acid building block cyclohexenylalanine
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A5A5S0Y9_MICAE
210
0
24139
TrEMBL
-
A0A402DEQ5_MICAE
210
0
24105
TrEMBL
-
A0A6H0H877_BACIU
204
0
23326
TrEMBL
-
A0A6M4JQA3_BACSU
Bacillus subtilis (strain 168)
204
0
23326
TrEMBL
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mahlstedt, S.; Fielding, E.N.; Moore, B.S.; Walsh, C.T.
Prephenate decarboxylases: a new prephenate-utilizing enzyme family that performs nonaromatizing decarboxylation en route to diverse secondary metabolites
Biochemistry
49
9021-9023
2010
Planktothrix agardhii, Salinispora tropica
brenda
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)
brenda
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)
brenda
EXTERNAL LINKS (specific for EC-Number 4.1.1.100)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
