KEGG ENZYME: 4.1.1.72

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

SDO:	SD1155_03025

BAN:

BA_2486

BAR:

GBAA_2486

BAT:

BAS2311

BAH:	BAMEG_2115

BAI:

BAA_2542

BAX:	H9401_2362

BANT:

A16_25150

BANR:

A16R_25440

BANS:

BAPAT_2379

BANH:

HYU01_12355

BANV:

DJ46_1269(kdcA)

BCE:

BC2433

BCA:

BCE_2517

BCZ:	BCE33L2232

BCR:	BCAH187_A2581

BCB:	BCB4264_A2440

BCU:	BCAH820_2507

BCQ:

BCQ_2404

BNC:

BCN_2398

BCER:

BCK_22550

BTK:	BT9727_2279

BTB:	BMB171_C2188

BTT:

HD73_2698

BTHR:

YBT1520_13230

BTHI:

BTK_13385

BTC:	CT43_CH2391

BTF:	YBT020_12580

BTM:

MC28_1684

BTG:	BTB_c25110(ipdC)

BTHT:

H175_ch2431

BTHU:

YBT1518_13440

BTW:

BF38_3678

BTHY:

AQ980_17575

BBY:	CY96_11165

BWD:	CT694_13080

BTRO:

FJR70_06885

BMOB:

MLA2C4_13260

BPAC:

LMD38_14475

BPAN:

NLJ82_11960

BALU:

QRY64_14660

BMQ:

BMQ_1177

BEO:

BEH_10440

VIR:	X953_06620

VHL:	BME96_05715

PHJ:	LC071_09445

STEA:

C0679_13600

SA0182

SAV:

SAV0188

SAW:

SAHV_0187

SAH:	SaurJH1_0178

SAJ:	SaurJH9_0173

SAM:

MW0162

SAS:

SAS0163

SAR:

SAR0189

SAC:	SACOL0173(ipdC)

SAX:	USA300HOU_0201

SAA:	SAUSA300_0190(ipdC)

SAO:	SAOUHSC_00153

SAE:	NWMN_0132(ipdC)

SAD:	SAAV_0156(ipdC)

SUU:	M013TW_0175

SUV:	SAVC_00705

SUE:	SAOV_0132(ipdC)

SUJ:	SAA6159_00169

SUK:	SAA6008_00166(ipdC)

SUC:

ECTR2_151

SUT:	SAT0131_00180

SUQ:	HMPREF0772_10311

SUZ:	MS7_0181(kdcA)

SUD:	ST398NM01_0205

SUX:	SAEMRSA15_01530

SUW:	SATW20_01980

SUG:

SAPIG0205

SUF:	SARLGA251_01590

SAUA:

SAAG_00670

SAUE:

RSAU_000139(ipdC)

SAUN:

SAKOR_00168

SAUS:

SA40_0152

SAUU:

SA957_0167

SAUG:

SA268_0165

SAUZ:

SAZ172_0197

SAUT:

SAI1T1_2001380

SAUJ:

SAI2T2_1001380

SAUK:

SAI3T3_1001380

SAUQ:

SAI4T8_1001380

SAUV:

SAI7S6_1001380

SAUW:

SAI5S5_1001370

SAUX:

SAI6T6_1001380

SAUY:

SAI8T7_1001380

SAUF:

X998_0170

SAB:

SAB0128c

SUY:	SA2981_0189

SAUB:

C248_0179

SAUM:

BN843_1930

SAUC:

CA347_198

SAUR:

SABB_01655(ipdC)

SAUI:

AZ30_00975

SAUD:

CH52_04785

SAMS:

NI36_00860

SUH:	SAMSHR1132_01630

SER:	SERP2242(ipdC)

SEP:

SE_2210

SEPP:

SEB_02211

SEPS:

DP17_1142

SHA:

SH0376

SHH:	ShL2_00289(ipdC)

SSP:

SSP0172

SCA:

SCA_2166

SLG:	SLGD_00204

SLN:	SLUG_02020

SSD:	SPSINT_2139

SDT:

SPSE_0333

SDP:	NCTC12225_00405(ipdC)

SWA:	A284_01225

SPAS:

STP1_1151

SXY:	BE24_11145

SXL:	SXYLSMQ121_0189

SXO:	SXYL_00185(ipdC)

SHU:	SHYC_02210

SCAP:

AYP1020_1828(ipdC)

SSCH:

LH95_01960

SSCZ:

RN70_02275

SAGQ:

EP23_07925

SEQO:

SE1039_23940

SSIF:

AL483_11495

SCV:	A4G25_09380

SPET:

CEP67_10810

SLZ:	B5P37_04325

SCOH:

BZ166_05470

SURY:

MUA21_11805

SNL:	BJD96_00470

SKL:	C7J89_03480

SFQ:	C7J90_04770

SHOM:

EGX58_05635

SCAR:

DWB96_01355

SCHR:

DWB92_02035

SARL:

SAP2_04420

SPIC:

SAMEA4384060_0379(ipdC)

SSH:	NCTC13712_00142(ipdC)

SDB:	CNQ82_02680

SLLO:

ISP08_02230

SAUL:

I6G39_10215

SSAC:

I6I31_03100

SPSD:

JMB28_01485

STAS:

HYI43_01705

SEDA:

MNY58_01035

SCAQ:

QMO72_01150

SDEV:

Q2T90_05655

SROT:

ML435_00780

STAP:

AOB58_1999

SHSI:

QQM35_02290

SSCU:

CEP64_00525

SFF:	FOB90_05805

SSTE:

SAMEA4384403_0231(ipdC)

MLEN:

H3V22_07645

MVT:	I6J10_10050

MACR:

BHM04_02235

MARY:

LAU42_07465

MBRU:

MGG13_02055

MEPI:

KFV12_09050

MBOC:

QSV55_02100

MCL:

MCCL_1331

MCAK:

MCCS_17360(ipdC)

MBOE:

HT586_08520

SBAC:

BVH56_00395

LGZ:	NCTC10812_02441(ipdC)

BTHS:

CNY62_05050

LLA:	L138640(ipd)

LLK:	LLKF_1386(kivD)

LLT:	CVCAS_1270(ipd)

LLS:	lilo_1266(ipd)

LLD:	P620_07485

LLX:	NCDO2118_1349

LLJ:	LG36_1080(kivD)

LLW:	kw2_1275(ipdC)

AAPI:

MOO46_04815

AAPN:

AAPFHON13_00980

FRU:	M3M36_03500

ESS:	ATZ33_02490

MPS:

MPTP_1603

MPX:

MPD5_0448

CML:	BN424_496(kdcA)

CDJ:	BFC22_02680

CAC:	CA_P0025(pdc)

CAE:	SMB_P024(pdc)

CAY:	CEA_P0024(pdc)

STHR:

BXT84_13475

DACT:

KZZ52_22860

» 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