| EC |
4.1.1.100 |
| Accepted name: |
prephenate decarboxylase |
| Reaction: |
prephenate = 3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2 |
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For diagram of bacilysin biosynthesis, click here |
| Glossary: |
L-anticapsin = 3-[(1R,2S,6R)-5-oxo-7-oxabicyclo[4.1.0]hept-2-yl]-L-alanine |
| Other name(s): |
BacA; AerD; SalX; non-aromatizing prephenate decarboxylase |
| Systematic name: |
prephenate carboxy-lyase (3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate-forming) |
| 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. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc |
| References: |
| 1. |
Mahlstedt, S.A. and Walsh, C.T. Investigation of anticapsin biosynthesis reveals a four-enzyme pathway to tetrahydrotyrosine in Bacillus subtilis. Biochemistry 49 (2010) 912–923. [DOI] [PMID: 20052993] |
| 2. |
Mahlstedt, S., Fielding, E.N., Moore, B.S. and Walsh, C.T. Prephenate decarboxylases: a new prephenate-utilizing enzyme family that performs nonaromatizing decarboxylation en route to diverse secondary metabolites. Biochemistry 49 (2010) 9021–9023. [DOI] [PMID: 20863139] |
| 3. |
Parker, J.B. and Walsh, C.T. Olefin isomerization regiochemistries during tandem action of BacA and BacB on prephenate in bacilysin biosynthesis. Biochemistry 51 (2012) 3241–3251. [DOI] [PMID: 22483065] |
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| [EC 4.1.1.100 created 2015] |
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