KEGG   ENZYME: 4.1.3.24Help
Entry
EC 4.1.3.24                 Enzyme                                 

Name
malyl-CoA lyase;
malyl-coenzyme A lyase;
(3S)-3-carboxy-3-hydroxypropanoyl-CoA glyoxylate-lyase;
mclA (gene name);
mcl1 (gene name);
(3S)-3-carboxy-3-hydroxypropanoyl-CoA glyoxylate-lyase (acetyl-CoA-forming);
L-malyl-CoA lyase
Class
Lyases;
Carbon-carbon lyases;
Oxo-acid-lyases
BRITE hierarchy
Sysname
(S)-malyl-CoA glyoxylate-lyase (acetyl-CoA-forming)
Reaction(IUBMB)
(1) (S)-malyl-CoA = acetyl-CoA + glyoxylate [RN:R00473];
(2) (2R,3S)-2-methylmalyl-CoA = propanoyl-CoA + glyoxylate [RN:R00934]
Reaction(KEGG)
Substrate
(S)-malyl-CoA [CPD:C04348];
(2R,3S)-2-methylmalyl-CoA [CPD:C06027]
Product
acetyl-CoA [CPD:C00024];
glyoxylate [CPD:C00048];
propanoyl-CoA [CPD:C00100]
Comment
The enzyme from the bacterium Chloroflexus aurantiacus, which participates in the 3-hydroxypropanoate cycle for carbon assimilation, also has the activity of EC 4.1.3.25, (3S)-citramalyl-CoA lyase [2,4]. The enzymes from Rhodobacter species are part of acetate assimilation pathways [3,5]. The reactions are reversible.
History
EC 4.1.3.24 created 1972, modified 2014
Pathway
Glyoxylate and dicarboxylate metabolism
C5-Branched dibasic acid metabolism
Methane metabolism
Carbon fixation pathways in prokaryotes
Microbial metabolism in diverse environments
Orthology
K08691  
malyl-CoA/(S)-citramalyl-CoA lyase
K19281  
beta-methylmalyl-CoA/(S)-malyl-CoA lyase
K19282  
bifunctional (S)-malyl-CoA lyase/thioesterase
Genes
MCA: 
BLEP: 
RPJ: 
CNC: 
BGP: 
BPLA: 
BPH: 
BFN: 
BCAI: 
CBAB: 
MPT: 
APP: 
PLA: 
BRC: 
BOP: 
XAU: 
AZC: 
MEX: 
MEA: 
MDI: 
MCH: 
MRD: 
MET: 
MPO: 
MNO: 
MOR: 
META: 
MAQU: 
MSL: 
CHEL: 
HDN: 
HDT: 
HMC: 
HNI: 
RVA: 
FIL: 
FIY: 
BVR: 
RHZ: 
MSC: 
MCG: 
CCR: 
CCS: 
CAK: 
CSE: 
CHQ: 
SIL: 
SIT: 
RSP: 
RSH: 
RSQ: 
RSK: 
RCP: 
JAN: 
RDE: 
RD1_1001(citE) RD1_1160(mclA) RD1_4242(mclA)
RLI: 
PDE: 
PAMI: 
DSH: 
Dshi_3050(citE2)
PSF: 
PGA: 
PGL: 
PGD: 
OAT: 
OAR: 
OTM: 
OSB_28710(mcl1)
LMD: 
RED: 
PTP: 
CID: 
CMAR: 
MALG: 
CON: 
RSU: 
PPHR: 
HAT: 
LAP: 
HNE: 
HNE_0078(mclA)
HBA: 
GBE: 
GBH: 
GBC: 
GBS: 
RRU: 
RRF: 
RPM: 
MAG: 
MGY: 
MAGX: 
TMO: 
TMO_0350(citE)
TXI: 
MAGQ: 
PGV: 
SCT: 
SCY: 
SALU: 
SALL: 
STRE: 
SLD: 
ICA: 
ARS: 
NCA: 
PSIM: 
AER: 
FRA: 
FSY: 
AMD: 
AMED_0079(citE)
AMN: 
AMM: 
AMES_0076(citE)
AMZ: 
B737_0077(citE)
AOI: 
AJA: 
AMQ: 
ALU: 
KAL: 
KPHY: 
CWO: 
AYM: 
RRS: 
RCA: 
CAU: 
CAG: 
CHL: 
HMA: 
rrnAC0690(citE1) rrnAC1965(aceB)
HHI: 
HAH_1341(citE1) HAH_2476(aceB)
HHN: 
HAB: 
NPH: 
NP_4430A(aceB)
NMO: 
Nmlp_2357(aceB)
HMU: 
HWA: 
HQ_1720A(aceB)
HWC: 
Hqrw_1842(aceB)
HVO: 
HVO_1983(aceB1) HVO_B0200(aceB2)
HME: 
HFX_2078(aceB)
HBO: 
HTU: 
NMG: 
HXA: 
NAT: 
NPE: 
NGE: 
HRU: 
NOU: 
SALI: 
HLR: 
 » show all
Taxonomy
Reference
1  [PMID:14285256]
  Authors
TUBOI S, KIKUCHI G.
  Title
ENZYMIC CLEAVAGE OF MALYTL-COENZYME A INTO ACETYL-COENZYME A AND GLYOXYLIC ACID.
  Journal
Biochim. Biophys. Acta. 96 (1965) 148-53.
Reference
2  [PMID:12374834]
  Authors
Herter S, Busch A, Fuchs G.
  Title
L-Malyl-coenzyme A lyase/beta-methylmalyl-coenzyme A lyase from Chloroflexus aurantiacus, a bifunctional enzyme involved in autotrophic CO(2) fixation.
  Journal
J. Bacteriol. 184 (2002) 5999-6006.
  Sequence
[cau:Caur_0174]
Reference
3  [PMID:15687206]
  Authors
Meister M, Saum S, Alber BE, Fuchs G
  Title
L-malyl-coenzyme A/beta-methylmalyl-coenzyme A lyase is involved in acetate assimilation of the isocitrate lyase-negative bacterium Rhodobacter capsulatus.
  Journal
J. Bacteriol. 187 (2005) 1415-25.
  Sequence
Reference
4  [PMID:17259315]
  Authors
Friedmann S, Alber BE, Fuchs G
  Title
Properties of R-citramalyl-coenzyme A lyase and its role in the autotrophic 3-hydroxypropionate cycle of Chloroflexus aurantiacus.
  Journal
J. Bacteriol. 189 (2007) 2906-14.
Reference
5  [PMID:20047909]
  Authors
Erb TJ, Frerichs-Revermann L, Fuchs G, Alber BE
  Title
The apparent malate synthase activity of Rhodobacter sphaeroides is due to two paralogous enzymes, (3S)-Malyl-coenzyme A (CoA)/{beta}-methylmalyl-CoA lyase and  (3S)- Malyl-CoA thioesterase.
  Journal
J. Bacteriol. 192 (2010) 1249-58.
  Sequence
[rsp:RSP_1771]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
37290-67-8

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