KEGG   ORTHOLOGY: K15404Help
Entry
K15404                      KO                                     

Name
K15404, CER1
Definition
aldehyde decarbonylase [EC:4.1.99.5]
Pathway
Cutin, suberine and wax biosynthesis
Brite
KEGG Orthology (KO) [BR:ko00001]
 Metabolism
  Lipid metabolism
   00073 Cutin, suberine and wax biosynthesis
    K15404  K15404, CER1; aldehyde decarbonylase
Enzymes [BR:ko01000]
 4. Lyases
  4.1  Carbon-carbon lyases
   4.1.99  Other carbon-carbon lyases
    4.1.99.5  aldehyde oxygenase (deformylating)
     K15404  K15404, CER1; aldehyde decarbonylase
BRITE hierarchy
Other DBs
RN: 
GO: 
Genes
ATH: 
ALY: 
CRB: 
EUS: 
BRP: 
BNA: 
THJ: 
CIT: 
CIC: 
TCC: 
GRA: 
GHI: 
EGR: 
GMX: 
PVU: 
VRA: 
VAR: 
CCAJ: 
MTR: 
CAM: 
ADU: 
AIP: 
LJA: 
Lj1g3v4156050.1(Lj1g3v4156050.1) Lj3g3v0618210.1(Lj3g3v0618210.1) Lj3g3v0618250.1(Lj3g3v0618250.1) Lj4g3v1120540.1(Lj4g3v1120540.1)
LANG: 
FVE: 
PPER: 
PMUM: 
MDM: 
PXB: 
ZJU: 
CSV: 
CMO: 
RCU: 
JCU: 
POP: 
VVI: 
SLY: 
SPEN: 
SOT: 
INI: 
SIND: 
BVG: 
NNU: 
OSA: 
4330012(OJ1234_B11.10)
DOSA: 
Os02t0621300-01(Os02g0621300) Os10t0471100-01(Os10g0471100)
OBR: 
BDI: 
ATS: 
SBI: 
ZMA: 
100273712(CER1) 100280261(cl3929_1)
SITA: 
PDA: 
EGU: 
MUS: 
ATR: 
SMO: 
 » show all
TaxonomyKoalaUniProt
Reference
PMID:8718622
  Authors
Aarts MG, Keijzer CJ, Stiekema WJ, Pereira A
  Title
Molecular characterization of the CER1 gene of arabidopsis involved in epicuticular wax biosynthesis and pollen fertility.
  Journal
Plant Cell 7:2115-27 (1995)
DOI:10.1105/tpc.7.12.2115
  Sequence
[ath:AT1G02205]

KEGG   ENZYME: 4.1.99.5Help
Entry
EC 4.1.99.5                 Enzyme                                 

Name
aldehyde oxygenase (deformylating);
decarbonylase;
aldehyde decarbonylase;
octadecanal decarbonylase;
octadecanal alkane-lyase
Class
Lyases;
Carbon-carbon lyases;
Other carbon-carbon lyases
BRITE hierarchy
Sysname
a long-chain aldehyde alkane-lyase
Reaction(IUBMB)
a long-chain aldehyde + O2 + 2 NADPH + 2 H+ = an alkane + formate + H2O + 2 NADP+ [RN:R03728]
Reaction(KEGG)
R03728;
(other) R09466
Show
Substrate
long-chain aldehyde [CPD:C00609];
O2 [CPD:C00007];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Product
alkane [CPD:C01371];
formate [CPD:C00058];
H2O [CPD:C00001];
NADP+ [CPD:C00006]
Comment
Contains a diiron center. Involved in the biosynthesis of alkanes. The enzyme from the cyanobacterium Nostoc punctiforme PCC 73102 is only active in vitro in the presence of ferredoxin, ferredoxin reductase and NADPH, and produces mostly C15 and C17 alkanes [2,3]. The enzyme from pea (Pisum sativum) produces alkanes of chain length C18 to C32 and is inhibited by metal-chelating agents [1]. The substrate for this enzyme is formed by EC 1.2.1.80, acyl-[acyl-carrier protein] reductase.
History
EC 4.1.99.5 created 1989, modified 2011, modified 2013
Pathway
Cutin, suberine and wax biosynthesis
Biosynthesis of secondary metabolites
Orthology
K14331  
fatty aldehyde decarbonylase
K15404  
aldehyde decarbonylase
Genes
ATH: 
ALY: 
CRB: 
EUS: 
BRP: 
BNA: 
THJ: 
CIT: 
CIC: 
TCC: 
GRA: 
GHI: 
EGR: 
GMX: 
PVU: 
VRA: 
VAR: 
CCAJ: 
MTR: 
CAM: 
ADU: 
AIP: 
LJA: 
Lj1g3v4156050.1(Lj1g3v4156050.1) Lj3g3v0618210.1(Lj3g3v0618210.1) Lj3g3v0618250.1(Lj3g3v0618250.1) Lj4g3v1120540.1(Lj4g3v1120540.1)
LANG: 
FVE: 
PPER: 
PMUM: 
MDM: 
PXB: 
ZJU: 
CSV: 
CMO: 
RCU: 
JCU: 
POP: 
VVI: 
SLY: 
SPEN: 
SOT: 
INI: 
SIND: 
BVG: 
NNU: 
OSA: 
4330012(OJ1234_B11.10)
DOSA: 
Os02t0621300-01(Os02g0621300) Os10t0471100-01(Os10g0471100)
OBR: 
BDI: 
ATS: 
SBI: 
ZMA: 
100273712(CER1) 100280261(cl3929_1)
SITA: 
PDA: 
EGU: 
MUS: 
ATR: 
SMO: 
PPJ: 
PBC: 
SYN: 
SYZ: 
SYY: 
SYNGTS_2252(sll0208)
SYT: 
SYNGTI_2251(sll0208)
SYS: 
SYNPCCN_2250(sll0208)
SYQ: 
SYNPCCP_2250(sll0208)
SYJ: 
SYW: 
SYC: 
SYF: 
SYD: 
SYE: 
SYG: 
SYR: 
SYX: 
CYA: 
CYB: 
SYNE: 
SYNP: 
SYNK: 
SYNR: 
SYND: 
SYU: 
SYH: 
SYNW: 
TEL: 
THN: 
CGC: 
CYI: 
DSL: 
CMP: 
LEN: 
LET: 
LBO: 
PSEU: 
PMA: 
PMM: 
PMT: 
PMN: 
PMI: 
PMB: 
PMC: 
PMF: 
PMG: 
PMH: 
PMJ: 
PME: 
PRC: 
PRM: 
AMR: 
MAR: 
MPK: 
CAN: 
HAO: 
CYU: 
GLP: 
GEE: 
CYT: 
CYP: 
CYN: 
CYH: 
TER: 
MIC: 
ARP: 
GEI: 
OAC: 
ONI: 
CEP: 
GVI: 
GLJ: 
ANA: 
NPU: 
NOS: 
NOP: 
NON: 
AVA: 
ANB: 
ACY: 
AWA: 
NAZ: 
CSG: 
CALO: 
CALT: 
CALH: 
RIV: 
FIS: 
NCN: 
CTHE: 
CEO: 
 » show all
Taxonomy
Reference
1  [PMID:6593720]
  Authors
Cheesbrough TM, Kolattukudy PE.
  Title
Alkane biosynthesis by decarbonylation of aldehydes catalyzed by a particulate preparation from Pisum sativum.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 81 (1984) 6613-7.
Reference
2  [PMID:20671186]
  Authors
Schirmer A, Rude MA, Li X, Popova E, del Cardayre SB
  Title
Microbial biosynthesis of alkanes.
  Journal
Science. 329 (2010) 559-62.
  Sequence
Reference
3  [PMID:21341652]
  Authors
Warui DM, Li N, Norgaard H, Krebs C, Bollinger JM Jr, Booker SJ
  Title
Detection of formate, rather than carbon monoxide, as the stoichiometric coproduct in conversion of fatty aldehydes to alkanes by a cyanobacterial aldehyde decarbonylase.
  Journal
J. Am. Chem. Soc. 133 (2011) 3316-9.
  Sequence
Reference
4  [PMID:22947199]
  Authors
Li N, Chang WC, Warui DM, Booker SJ, Krebs C, Bollinger JM Jr
  Title
Evidence for only oxygenative cleavage of aldehydes to alk(a/e)nes and formate by cyanobacterial aldehyde decarbonylases.
  Journal
Biochemistry. 51 (2012) 7908-16.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
94185-90-7

KEGG   REACTION: R09466Help
Entry
R09466                      Reaction                               

Name
aldehyde decarbonylase
Definition
Long-chain aldehyde <=> Alkane + CO
Equation
Enzyme
Pathway
Cutin, suberine and wax biosynthesis
Biosynthesis of secondary metabolites
Orthology
K15404  
aldehyde decarbonylase [EC:4.1.99.5]

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