KEGG   ENZYME: 4.1.99.5Help
Entry
EC 4.1.99.5                 Enzyme                                 
Name
octadecanal decarbonylase;
decarbonylase;
aldehyde decarbonylase
Class
Lyases;
Carbon-carbon lyases;
Other carbon-carbon lyases
BRITE hierarchy
Sysname
octadecanal alkane-lyase
Reaction(IUBMB)
octadecanal + O2 + 2 NADPH + 2 H+ = heptadecane + formate + H2O + 2 NADP+ [RN:R03728]
Reaction(KEGG)
R03728;
(other) R09466
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Substrate
octadecanal [CPD:C01838];
O2 [CPD:C00007];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Product
heptadecane [CPD:C01816];
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.
Pathway
Cutin, suberine and wax biosynthesis
Biosynthesis of secondary metabolites
Orthology
K14331  
fatty aldehyde decarbonylase
K15404  
aldehyde decarbonylase
Genes
ATH: 
AT1G02205(CER1)
ALY: 
GMX: 
MTR: 
CSV: 
RCU: 
POP: 
VVI: 
OSA: 
DOSA: 
Os02t0621300-01(Os02g0621300) Os10t0471100-01(Os10g0471100)
BDI: 
100833807 100833914
SBI: 
SORBI_01g019590(SORBIDRAFT_01g019590) SORBI_04g026320(SORBIDRAFT_04g026320)
ZMA: 
100280261(cl3929_1)
SMO: 
SELMODRAFT_129942(CER1-2) SELMODRAFT_230422(CER1-1)
BSUB: 
BEST7613_5507
SYN: 
sll0208
SYZ: 
MYO_122780
SYY: 
SYNGTS_2252(sll0208)
SYT: 
SYNGTI_2251(sll0208)
SYS: 
SYNPCCN_2250(sll0208)
SYQ: 
SYNPCCP_2250(sll0208)
SYW: 
SYNW1738
SYC: 
syc0050_d
SYF: 
Synpcc7942_1593
SYD: 
Syncc9605_0728
SYE: 
Syncc9902_1635
SYG: 
sync_1990
SYR: 
SynRCC307_1586
SYX: 
SynWH7803_0654
CYA: 
CYA_0415
CYB: 
CYB_2442
SYNE: 
Syn6312_2280
SYNP: 
Syn7502_03278
TEL: 
tll1313
MAR: 
MAE_53090
CYT: 
cce_0778
CYP: 
PCC8801_0455
CYN: 
Cyan7425_0398
CYH: 
Cyan8802_0468
AMR: 
AM1_4041
CGC: 
Cyagr_0039
CAN: 
Cyan10605_1692
DSL: 
Dacsa_2178
HAO: 
PCC7418_0961
GLP: 
Glo7428_0150
CMP: 
Cha6605_4153
CYU: 
UCYN_05810
GVI: 
gll3146
ANA: 
alr5283
NPU: 
Npun_R1711
NOS: 
Nos7107_1028
NOP: 
Nos7524_4304
AVA: 
Ava_2533
ANB: 
ANA_C11210
ACY: 
Anacy_3389
NAZ: 
Aazo_3371
CSG: 
Cylst_0697
CALO: 
Cal7507_5586
CALT: 
Cal6303_4369
RIV: 
Riv7116_3790
PMA: 
Pro0532
PMM: 
PMM0532
PMT: 
PMT1231
PMN: 
PMN2A_1863
PMI: 
PMT9312_0532
PMB: 
A9601_05881
PMC: 
P9515_05961
PMF: 
P9303_07791
PMG: 
P9301_05581
PMH: 
P9215_06131
PMJ: 
P9211_05351
PME: 
NATL1_05881
TER: 
Tery_2280
GEI: 
GEI7407_1564
OAC: 
Oscil6304_2075
ONI: 
Osc7112_0944
PSEU: 
Pse7367_3626
CEP: 
Cri9333_4418
MIC: 
Mic7113_4535
ARP: 
NIES39_M01940
CTHE: 
Chro_1554
 » 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.
  Organism
Pisum sativum
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.
  Organism
Synechococcus elongatus [GN:syf]
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.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
94185-90-7
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