KEGG   ENZYME: 4.1.1.100
Entry
EC 4.1.1.100                Enzyme                                 
Name
prephenate decarboxylase;
BacA;
AerD;
SalX;
non-aromatizing prephenate decarboxylase
Class
Lyases;
Carbon-carbon lyases;
Carboxy-lyases
Sysname
prephenate carboxy-lyase (3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate-forming)
Reaction(IUBMB)
prephenate = 3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2 [RN:R10934]
Reaction(KEGG)
R10934
Substrate
prephenate [CPD:C00254]
Product
3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate [CPD:C20953];
CO2 [CPD:C00011]
Comment
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.
History
EC 4.1.1.100 created 2015
Pathway
ec00998  Biosynthesis of various antibiotics
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K19546  prephenate decarboxylase
Genes
DAQDAQ1742_03406(bacA)
DICDpoa569_001039
DLCO1Q98_16235
LPAlpa_03409
BSUBSU37740(bacA)
BSRI33_3922
BSLA7A1_0193
BSHBSU6051_37740(bacA)
BSYI653_18515
BSUTBSUB_04010(bacA)
BSULBSUA_04010(bacA)
BSUSQ433_20785
BSOBSNT_10432
BSNBSn5_09860
BSQB657_37740(bacA)
BSXC663_3679(bacA)
BSPU712_19020
BSSBSUW23_18640(bacA)
BSTGYO_4160
BITBIS30_08585
BAYRBAM_034930
BAQBACAU_3522(bacA)
BYABANAU_3675(bacA)
BAMPB938_17925(bacA)
BQYMUS_4152(bacA)
BAMLBAM5036_3423(bacA)
BAMARBAU_3631(bacA)
BAMNBASU_3407(bacA)
BAMBBAPNAU_3689(bacA)
BAMTAJ82_19710
BAMYV529_37650(bacA)
BMPNG74_03668
BAOBAMF_3607(bacA)
BAZBAMTA208_19100(bacA)
BQLLL3_03918(bacA)
BXHBAXH7_03910(bacA)
BAMIKSO_001595
BAMCU471_36380
BAMFU722_18660
BSIACWD84_01660
BVMB9C48_17875
BHTDIC78_12105
BMOJHC660_36820(bacA)
BTEQG4P54_19460(bacA)
BIQAN935_19115
BSTRQI003_22375(bacA)
BPUBPUM_3420
BPUMBW16_18160
BPUSUP12_17605
BALTCFN77_18065
BAERBAE_05965
BSAFBSL056_18705
BCABEFK13_19430(bacA)
BRYM0696_19180(bacA)
BJSMY9_3866
BACWQR42_17160
BACPSB24_11230
BACBOY17_01130
BACYQF06_17310
BACLBS34A_40920(bacA)
BALMBsLM_3804
BACSAUL54_12230
BZHNF868_15795
BAEIRE735_02185
BGIBGM20_13130
BMURABE28_019115
PSOPKP014_17420
STRMM444_35590
SPHVF9278_21515
SCOECP976_00065
SDECL3078_20880
SXTKPP03845_106161(bacA)
SGKPET44_33055
MARMAE_56560
MPKVL20_295
MVZmyaer102_28820
PAGHNIES204_06210(aerD)
PPSUNO713_02126(aerD)
PRUNPCC7821_03672(aerD)
MPROBJP34_16215
HBQQI031_25715
NSPBMF81_03788(bacA_2)
NSPHBDGGKGIB_04044(suoD)
AFLOHEQ12_06185
 » show all
Reference
1  [PMID:20052993]
  Authors
Mahlstedt SA, Walsh CT
  Title
Investigation of anticapsin biosynthesis reveals a four-enzyme pathway to tetrahydrotyrosine in Bacillus subtilis.
  Journal
Biochemistry 49:912-23 (2010)
DOI:10.1021/bi9021186
Reference
2  [PMID:20863139]
  Authors
Mahlstedt S, Fielding EN, Moore BS, Walsh CT
  Title
Prephenate decarboxylases: a new prephenate-utilizing enzyme family that performs nonaromatizing decarboxylation en route to diverse secondary metabolites.
  Journal
Biochemistry 49:9021-3 (2010)
DOI:10.1021/bi101457h
Reference
3  [PMID:22483065]
  Authors
Parker JB, Walsh CT
  Title
Olefin isomerization regiochemistries during tandem action of BacA and BacB on prephenate in bacilysin biosynthesis.
  Journal
Biochemistry 51:3241-51 (2012)
DOI:10.1021/bi300254u
Other DBs
ExplorEnz - The Enzyme Database: 4.1.1.100
IUBMB Enzyme Nomenclature: 4.1.1.100
ExPASy - ENZYME nomenclature database: 4.1.1.100
BRENDA, the Enzyme Database: 4.1.1.100

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