KEGG   ENZYME: 4.1.1.72
Entry
EC 4.1.1.72                 Enzyme                                 
Name
branched-chain-2-oxoacid decarboxylase;
branched-chain oxo acid decarboxylase;
branched-chain alpha-keto acid decarboxylase;
branched-chain keto acid decarboxylase;
BCKA;
(3S)-3-methyl-2-oxopentanoate carboxy-lyase
Class
Lyases;
Carbon-carbon lyases;
Carboxy-lyases
Sysname
(3S)-3-methyl-2-oxopentanoate carboxy-lyase (2-methylbutanal-forming)
Reaction(IUBMB)
(3S)-3-methyl-2-oxopentanoate = 2-methylbutanal + CO2 [RN:R03894]
Reaction(KEGG)
R03894
Substrate
(3S)-3-methyl-2-oxopentanoate [CPD:C00671]
Product
2-methylbutanal [CPD:C02223];
CO2 [CPD:C00011]
Comment
Acts on a number of 2-oxo acids, with a high affinity towards branched-chain substrates. The aldehyde formed may be enzyme-bound, and may be an intermediate in the bacterial system for the biosynthesis of branched-chain fatty acids.
History
EC 4.1.1.72 created 1990
Orthology
K27601  branched-chain-2-oxoacid decarboxylase
Genes
SDOSD1155_03025
BANBA_2486
BARGBAA_2486
BATBAS2311
BAHBAMEG_2115
BAIBAA_2542
BAXH9401_2362
BANTA16_25150
BANRA16R_25440
BANSBAPAT_2379
BANHHYU01_12355
BANVDJ46_1269(kdcA)
BCEBC2433
BCABCE_2517
BCZBCE33L2232
BCRBCAH187_A2581
BCBBCB4264_A2440
BCUBCAH820_2507
BCQBCQ_2404
BNCBCN_2398
BCERBCK_22550
BTKBT9727_2279
BTBBMB171_C2188
BTTHD73_2698
BTHRYBT1520_13230
BTHIBTK_13385
BTCCT43_CH2391
BTFYBT020_12580
BTMMC28_1684
BTGBTB_c25110(ipdC)
BTHTH175_ch2431
BTHUYBT1518_13440
BTWBF38_3678
BTHYAQ980_17575
BBYCY96_11165
BWDCT694_13080
BTROFJR70_06885
BMOBMLA2C4_13260
BPACLMD38_14475
BPANNLJ82_11960
BALUQRY64_14660
BMQBMQ_1177
BEOBEH_10440
VIRX953_06620
VHLBME96_05715
PHJLC071_09445
STEAC0679_13600
SAUSA0182
SAVSAV0188
SAWSAHV_0187
SAHSaurJH1_0178
SAJSaurJH9_0173
SAMMW0162
SASSAS0163
SARSAR0189
SACSACOL0173(ipdC)
SAXUSA300HOU_0201
SAASAUSA300_0190(ipdC)
SAOSAOUHSC_00153
SAENWMN_0132(ipdC)
SADSAAV_0156(ipdC)
SUUM013TW_0175
SUVSAVC_00705
SUESAOV_0132(ipdC)
SUJSAA6159_00169
SUKSAA6008_00166(ipdC)
SUCECTR2_151
SUTSAT0131_00180
SUQHMPREF0772_10311
SUZMS7_0181(kdcA)
SUDST398NM01_0205
SUXSAEMRSA15_01530
SUWSATW20_01980
SUGSAPIG0205
SUFSARLGA251_01590
SAUASAAG_00670
SAUERSAU_000139(ipdC)
SAUNSAKOR_00168
SAUSSA40_0152
SAUUSA957_0167
SAUGSA268_0165
SAUZSAZ172_0197
SAUTSAI1T1_2001380
SAUJSAI2T2_1001380
SAUKSAI3T3_1001380
SAUQSAI4T8_1001380
SAUVSAI7S6_1001380
SAUWSAI5S5_1001370
SAUXSAI6T6_1001380
SAUYSAI8T7_1001380
SAUFX998_0170
SABSAB0128c
SUYSA2981_0189
SAUBC248_0179
SAUMBN843_1930
SAUCCA347_198
SAURSABB_01655(ipdC)
SAUIAZ30_00975
SAUDCH52_04785
SAMSNI36_00860
SUHSAMSHR1132_01630
SERSERP2242(ipdC)
SEPSE_2210
SEPPSEB_02211
SEPSDP17_1142
SHASH0376
SHHShL2_00289(ipdC)
SSPSSP0172
SCASCA_2166
SLGSLGD_00204
SLNSLUG_02020
SSDSPSINT_2139
SDTSPSE_0333
SDPNCTC12225_00405(ipdC)
SWAA284_01225
SPASSTP1_1151
SXYBE24_11145
SXLSXYLSMQ121_0189
SXOSXYL_00185(ipdC)
SHUSHYC_02210
SCAPAYP1020_1828(ipdC)
SSCHLH95_01960
SSCZRN70_02275
SAGQEP23_07925
SEQOSE1039_23940
SSIFAL483_11495
SCVA4G25_09380
SPETCEP67_10810
SLZB5P37_04325
SCOHBZ166_05470
SNLBJD96_00470
SKLC7J89_03480
SFQC7J90_04770
SHOMEGX58_05635
SCARDWB96_01355
SCHRDWB92_02035
SARLSAP2_04420
SPICSAMEA4384060_0379(ipdC)
SSHNCTC13712_00142(ipdC)
SDBCNQ82_02680
SLLOISP08_02230
SAULI6G39_10215
SSACI6I31_03100
SPSDJMB28_01485
STASHYI43_01705
SURYMUA21_11805
SEDAMNY58_01035
SCAQQMO72_01150
SDEVQ2T90_05655
SROTML435_00780
STAPAOB58_1999
SSCUCEP64_00525
SFFFOB90_05805
SSTESAMEA4384403_0231(ipdC)
MLENH3V22_07645
MVTI6J10_10050
MACRBHM04_02235
MARYLAU42_07465
MBRUMGG13_02055
MEPIKFV12_09050
MBOCQSV55_02100
MCLMCCL_1331
MCAKMCCS_17360(ipdC)
MBOEHT586_08520
SBACBVH56_00395
LGZNCTC10812_02441(ipdC)
BTHSCNY62_05050
LLAL138640(ipd)
LLKLLKF_1386(kivD)
LLTCVCAS_1270(ipd)
LLSlilo_1266(ipd)
LLDP620_07485
LLXNCDO2118_1349
LLJLG36_1080(kivD)
LLWkw2_1275(ipdC)
AAPIMOO46_04815
AAPNAAPFHON13_00980
FRUM3M36_03500
ESSATZ33_02490
MPSMPTP_1603
MPXMPD5_0448
CMLBN424_496(kdcA)
CDJBFC22_02680
CACCA_P0025(pdc)
CAESMB_P024(pdc)
CAYCEA_P0024(pdc)
STHRBXT84_13475
 » show all
Reference
1  [PMID:3142877]
  Authors
Oku H, Kaneda T.
  Title
Biosynthesis of branched-chain fatty acids in Bacillus subtilis. A decarboxylase is essential for branched-chain fatty acid synthetase.
  Journal
J Biol Chem 263:18386-96 (1988)
Reference
2  [PMID:15358422]
  Authors
de la Plaza M, Fernandez de Palencia P, Pelaez C, Requena T
  Title
Biochemical and molecular characterization of alpha-ketoisovalerate decarboxylase, an enzyme involved in the formation of aldehydes from amino acids  by Lactococcus lactis.
  Journal
FEMS Microbiol Lett 238:367-74 (2004)
DOI:10.1016/j.femsle.2004.07.057
  Sequence
[lla:L138640]
Reference
3  [PMID:15640202]
  Authors
Smit BA, van Hylckama Vlieg JE, Engels WJ, Meijer L, Wouters JT, Smit G
  Title
Identification, cloning, and characterization of a Lactococcus lactis branched-chain alpha-keto acid decarboxylase involved in flavor formation.
  Journal
Appl Environ Microbiol 71:303-11 (2005)
DOI:10.1128/AEM.71.1.303-311.2005
  Sequence
[llw:kw2_1275]
Other DBs
ExplorEnz - The Enzyme Database: 4.1.1.72
IUBMB Enzyme Nomenclature: 4.1.1.72
ExPASy - ENZYME nomenclature database: 4.1.1.72
BRENDA, the Enzyme Database: 4.1.1.72
CAS: 63653-19-0

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