The Enzyme Database

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EC 4.1.1.100     
Accepted name: prephenate decarboxylase
Reaction: prephenate = 3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
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, 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. [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. [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. [PMID: 22483065]
[EC 4.1.1.100 created 2015]
 
 


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