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: 
CSAT: 
EUS: 
BRP: 
BNA: 
BOE: 
THJ: 
CPAP: 
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: 
MCHA: 
RCU: 
JCU: 
HBR: 
POP: 
VVI: 
SLY: 
SPEN: 
SOT: 
CANN: 
NTA: 
NSY: 
NTO: 
INI: 
SIND: 
HAN: 
BVG: 
SOE: 
NNU: 
OSA: 
DOSA: 
Os02t0621300-01(Os02g0621300) Os10t0471100-01(Os10g0471100)
OBR: 
BDI: 
SBI: 
ZMA: 
100273712(CER1) 100280261(cl3929_1) 100382841
SITA: 
PDA: 
EGU: 
MUS: 
DCT: 
ATR: 
SMO: 
PPP: 
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: 
CWA: 
GLP: 
GEE: 
CYT: 
CYP: 
CYN: 
CYH: 
TER: 
MIC: 
ARP: 
GEI: 
OAC: 
ONI: 
CEP: 
GVI: 
GLJ: 
ANA: 
NPU: 
NOS: 
NOP: 
NON: 
AVA: 
NAZ: 
ANB: 
ACY: 
AWA: 
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

DBGET integrated database retrieval system