KEGG   ENZYME: 4.1.3.43Help
Entry
EC 4.1.3.43                 Enzyme                                 

Name
4-hydroxy-2-oxohexanoate aldolase;
BphI
Class
Lyases;
Carbon-carbon lyases;
Oxo-acid-lyases
BRITE hierarchy
Sysname
(S)-4-hydroxy-2-oxohexanoate pyruvate-lyase (propanal-forming)
Reaction(IUBMB)
(S)-4-hydroxy-2-oxohexanoate = propanal + pyruvate
Reaction(KEGG)
(other) R05298
Show
Substrate
(S)-4-hydroxy-2-oxohexanoate
Product
propanal [CPD:C00479];
pyruvate [CPD:C00022]
Comment
Requires Mn2+ for maximal activity [1,2]. The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 4.1.3.39, 4-hydroxy-2-oxovalerate aldolase [1,2,6]. The enzyme forms a bifunctional complex with EC 1.2.1.87, propanal dehydrogenase (CoA-propanoylating), with a tight channel connecting the two subunits [3,4,6].
History
EC 4.1.3.43 created 2013
Pathway
Xylene degradation
Metabolic pathways
Microbial metabolism in diverse environments
Orthology
K18365  
4-hydroxy-2-oxovalerate/4-hydroxy-2-oxohexanoate aldolase
Genes
PSD: 
PRE: 
PPUT: 
PPUN: 
PP4_27280(mhpE)
PSC: 
PSTU: 
PBM: 
PPUU: 
PKC: 
PKB_4237(nahM)
PFZ: 
PALK: 
PPSY: 
AVN: 
AVL: 
AVD: 
AEI: 
SPL: 
SHL: 
SWD: 
PHA: 
PSHAa2143(mhpE)
PTN: 
LAL: 
TTU: 
SPOI: 
ZAL: 
CYQ: 
CZA: 
BLEP: 
AEH: 
MMW: 
GPB: 
TBN: 
RPI: 
RPF: 
REH: 
H16_B0595(bpHI)
CNC: 
RME: 
Rmet_1319(bphI)
CTI: 
CBW: 
BVI: 
BUR: 
BCJ: 
BCAM1615(bphI)
BCEN: 
DM39_3381(dmpG) DM39_4832(dmpG)
BCEO: 
I35_5475(bphI)
BCT: 
BCED: 
DM42_4991(dmpG) DM42_6343(dmpG)
BPYR: 
BCON: 
BUQ: 
BXE: 
Bxe_C1187(bphI)
BXB: 
DR64_8618(dmpG)
BFN: 
OI25_4591(dmpG)
PPK: 
PRB: 
AXY: 
CDN: 
RFR: 
PNA: 
AJS: 
VEI: 
CTT: 
CTES: 
ADN: 
ADK: 
MPT: 
MASW: 
LCH: 
AZO: 
azo1857(lapG) azo1972(mhpE) azo2431(nahM)
AZI: 
DAR: 
TMZ: 
THU: 
RBU: 
ARC: 
SHZ: 
CID: 
NPP: 
SJP: 
SJA_C1-11910(mhpE_xylK)
SYB: 
TXI: 
PGV: 
GJF: 
 » show all
Taxonomy
Reference
1  [PMID:19476337]
  Authors
Baker P, Pan D, Carere J, Rossi A, Wang W, Seah SY
  Title
Characterization of an aldolase-dehydrogenase complex that exhibits substrate channeling in the polychlorinated biphenyls degradation pathway.
  Journal
Biochemistry. 48 (2009) 6551-8.
  Sequence
[bxe:Bxe_C1187]
Reference
2  [PMID:20364820]
  Authors
Wang W, Baker P, Seah SY
  Title
Comparison of two metal-dependent pyruvate aldolases related by convergent evolution: substrate specificity, kinetic mechanism, and substrate channeling.
  Journal
Biochemistry. 49 (2010) 3774-82.
  Sequence
[bxe:Bxe_C1187]
Reference
3  [PMID:21425833]
  Authors
Baker P, Carere J, Seah SY
  Title
Probing the molecular basis of substrate specificity, stereospecificity, and catalysis in the class II pyruvate aldolase, BphI.
  Journal
Biochemistry. 50 (2011) 3559-69.
  Sequence
[bxe:Bxe_C1187]
Reference
4  [PMID:21838275]
  Authors
Carere J, Baker P, Seah SY
  Title
Investigating the molecular determinants for substrate channeling in BphI-BphJ, an aldolase-dehydrogenase complex from the polychlorinated biphenyls degradation  pathway.
  Journal
Biochemistry. 50 (2011) 8407-16.
  Sequence
[bxe:Bxe_C1187]
Reference
5  [PMID:22081904]
  Authors
Baker P, Seah SY
  Title
Rational design of stereoselectivity in the class II pyruvate aldolase BphI.
  Journal
J. Am. Chem. Soc. 134 (2012) 507-13.
  Sequence
[bxe:Bxe_C1187]
Reference
6  [PMID:22316175]
  Authors
Baker P, Hillis C, Carere J, Seah SY
  Title
Protein-protein interactions and substrate channeling in orthologous and chimeric aldolase-dehydrogenase complexes.
  Journal
Biochemistry. 51 (2012) 1942-52.
  Sequence
[ttj:TTHB246]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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