| Entry |
|
|---|
| Name |
homocitrate synthase;
2-hydroxybutane-1,2,4-tricarboxylate 2-oxoglutarate-lyase
(CoA-acetylating);
acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase;
homocitrate synthetase;
HCS |
|---|
| Class |
Transferases;
Acyltransferases;
Acyl groups converted into alkyl groups on transfer
 |
|---|
| Sysname |
acetyl-CoA:2-oxoglutarate C-acetyltransferase
(thioester-hydrolysing, carboxymethyl forming) |
|---|
| Reaction(IUBMB) |
acetyl-CoA + H2O + 2-oxoglutarate =
(R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA [RN:R00271] |
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| Reaction(KEGG) |
R00271
 |
|---|
| Substrate |
acetyl-CoA [CPD:C00024];
H2O [CPD:C00001];
2-oxoglutarate [CPD:C00026] |
|---|
| Product |
(R)-2-hydroxybutane-1,2,4-tricarboxylate [CPD:C01251];
CoA [CPD:C00010] |
|---|
| Comment |
Belongs in the alpha-aminoadipate pathway of lysine synthesis, along
with EC 4.2.1.36, homoaconitate hydratase. The enzyme also acts with
oxaloacetate as substrate, but more slowly [2,3]. |
|---|
| Pathway |
PATH: ec00300 Lysine biosynthesis
PATH: ec00620 Pyruvate metabolism
PATH: ec01100 Metabolic pathways |
|---|
| Orthology |
KO: K01655 homocitrate synthase |
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| Genes |
SCE: YDL131W(LYS21) YDL182W(LYS20)
AGO: AGOS_ADR107W
KLA: KLLA0F05489g
DHA: DEHA0D14498g DEHA0F09405g
PIC: PICST_28701(LYS21) PICST_89386(LYS22)
CAL: CaO19.4506(LYS211)
CGR: CAGL0J06402g CAGL0J09240g
YLI: YALI0F31075g
SPO: SPBC1105.02c(lys4)
NCR: NCU05526
MGR: MGG_01092
ANI: AN1990.2
AFM: AFUA_4G10460
AOR: AO090003001165
ANG: An04g06210
CNE: CND01200
UMA: UM04115.1
ECA: ECA2944(nifV)
KPE: KPK_1704(nifV)
DDA: Dd703_0505
PSA: PST_1352(nifV)
AVN: Avin_01640(nifV)
TTU: TERTU_1590(nifV)
MCA: MCA0254(nifV)
HHA: Hhal_0279
TAU: Tola_2344
AFE: Lferr_1224
AFR: AFE_1506(nifV)
BVI: Bcep1808_5987
BXE: Bxe_B1438
BPH: Bphy_7741
PNA: Pnap_2310
LCH: Lcho_1366
AZO: azo0551(nifV)
DAR: Daro_1398
APP: CAP2UW1_4375
WSU: WS1396(nifV1)
GSU: GSU0937(aksA)
GME: Gmet_0692(aksA)
GUR: Gura_3368(aksA)
GLO: Glov_0424(aksA)
GBM: Gbem_2073(aksA)
GEO: Geob_2573
GEM: GM21_2146
PCA: Pcar_2110(aksA)
PPD: Ppro_3466(aksA)
DVM: DvMF_2612
DSA: Desal_0448
DBA: Dbac_0833
DAL: Dalk_1511
DAT: HRM2_09760(nifV1)
ADE: Adeh_1436
BRA: BRADO5390(nifV)
BBT: BBta_5875(nifV)
RPA: RPA4607(nifV)
RPB: RPB_0982
RPC: RPC_4450
RPD: RPD_1086
RPE: RPE_4520
RPT: Rpal_5088
XAU: Xaut_0150
AZC: AZC_3389
MET: M446_3580
BID: Bind_0485
MSL: Msil_3619
RSP: RSP_0529(nifV)
RSH: Rsph17029_2181
RSQ: Rsph17025_1258
RSK: RSKD131_1864
ZMO: ZMO1835
ZMN: Za10_1400
GDI: GDI_0449(nifV)
GDJ: Gdia_1557
RRU: Rru_A2269
RCE: RC1_3693(nifV)
MAG: amb1562
MGM: Mmc1_1190
CAC: CAC0261(nifV)
CDF: CD0832(aksA)
CDC: CD196_0781
CDL: CDR20291_0762
CBK: CLL_A0128(aksA)
CBT: CLH_0112(aksA)
CBE: Cbei_0069(aksA) Cbei_2012
CKL: CKL_1757(nifV1)
CKR: CKR_1630
AMT: Amet_1321 Amet_3515
SWO: Swol_0375(aksA)
DSY: DSY3883(aksA) DSY4262
DHD: Dhaf_1059 Dhaf_1522
DRM: Dred_2339(aksA)
DAE: Dtox_0785
PTH: PTH_2520(aksA)
DAU: Daud_1035(aksA)
HMO: HM1_0858(nifV) HM1_2993
TTE: TTE0472(aksA)
TEX: Teth514_0415(aksA)
TPD: Teth39_1820(aksA)
CHY: CHY_1104(aksA)
MTA: Moth_1938(aksA)
ADG: Adeg_1099
HOR: Hore_08050
SGR: SGR_3476
FRA: Francci3_4489
FRE: Franean1_4071
FAL: FRAAL6814(nifV)
APS: CFPG_473
MIN: Minf_1877(leuA)
EMI: Emin_0401
CYA: CYA_1820(aksA)
CYB: CYB_0424(aksA)
CYT: cce_0549(aksA)
CYP: PCC8801_1776(aksA)
CYC: PCC7424_2127(aksA)
CYN: Cyan7425_2367
CYH: Cyan8802_1804
ANA: alr1407(aksA) alr2968(aksA)
NPU: Npun_F0430(aksA)
AVA: Ava_0938(aksA) Ava_3956(aksA) Ava_4041(aksA)
CTE: CT1528(nifV)
CPC: Cpar_1614
CCH: Cag_1229
CPH: Cpha266_1918
CPB: Cphamn1_1747
CLI: Clim_0690
PVI: Cvib_1341
PLT: Plut_1526
PPH: Ppha_1919
PAA: Paes_1624
CTS: Ctha_1654
DET: DET1614
DEH: cbdb_A1708
DEB: DehaBAV1_1360
DEV: DhcVS_1496
DRA: DR_1238
DGE: Dgeo_1257
TTH: TTC1550
TTJ: TTHA1914
PMO: Pmob_1703(aksA)
DTH: DICTH_1519(aksA)
DTU: Dtur_1629(aksA)
TYE: THEYE_A1277
NPH: NP2994A(leuA_3)
 |
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| Structures |
PDB: 2ZTJ 2ZTK 2ZYF 3A9I 3IVS 3IVT 3IVU 3L90 |
|---|
Reference
Authors
Title
Journal
Organism
|
1 [PMID:5836514]
Strassman M, Ceci LN.
Enzymatic formation of homocitric acid, an intermediate in lysine
biosynthesis.
Biochem. Biophys. Res. Commun. 14 (1964) 262-7.
Escherichia coli [GN:eco] |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:12095615]
Wulandari AP, Miyazaki J, Kobashi N, Nishiyama M, Hoshino T, Yamane
H.
Characterization of bacterial homocitrate synthase involved in
lysine biosynthesis.
FEBS. Lett. 522 (2002) 35-40.
Thermus thermophilus [GN:tth] |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:15362863]
Andi B, West AH, Cook PF.
Kinetic mechanism of histidine-tagged homocitrate synthase from
Saccharomyces cerevisiae.
Biochemistry. 43 (2004) 11790-5.
Saccharomyces cerevisiae [GN:sce] |
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| Other DBs |
ExplorEnz - The Enzyme Database: 2.3.3.14
IUBMB Enzyme Nomenclature: 2.3.3.14
ExPASy - ENZYME nomenclature database: 2.3.3.14
BRENDA, the Enzyme Database: 2.3.3.14
CAS: 9075-60-9 |
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