KEGG   ENZYME: 1.2.1.80Help
Entry
EC 1.2.1.80                 Enzyme                                 

Name
long-chain acyl-[acyl-carrier-protein] reductase;
long-chain acyl-[acp] reductase;
fatty acyl-[acyl-carrier-protein] reductase;
acyl-[acp] reductase
Class
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
long-chain-aldehyde:NAD(P)+ oxidoreductase (acyl-[acyl-carrier protein]-forming)
Reaction(IUBMB)
a long-chain aldehyde + an [acyl-carrier protein] + NAD(P)+ = a long-chain acyl-[acyl-carrier protein] + NAD(P)H + H+ [RN:R09484 R09485]
Reaction(KEGG)
Substrate
long-chain aldehyde [CPD:C00609];
[acyl-carrier protein] [CPD:C00229];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006]
Product
long-chain acyl-[acyl-carrier protein] [CPD:C20683];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
Catalyses the reaction in the opposite direction. This enzyme, purified from the cyanobacterium Synechococcus elongatus PCC 7942, catalyses the NAD(P)H-dependent reduction of an activated fatty acid (acyl-[acp]) to the corresponding aldehyde. Together with EC 4.1.99.5, octadecanal decarbonylase, it is involved in alkane biosynthesis. The natural substrates of the enzyme are C16 and C18 activated fatty acids. Requires Mg2+.
History
EC 1.2.1.80 created 2011
Orthology
K14330  fatty aldehyde-generating acyl-ACP reductase
Genes
VFF: VITFI_CDS1482
SYN: sll0209
SYZ: MYO_122770
SYY: SYNGTS_2251(sll0209)
SYT: SYNGTI_2250(sll0209)
SYS: SYNPCCN_2249(sll0209)
SYQ: SYNPCCP_2249(sll0209)
SYJ: D082_05320
SYO: C7I86_11770
SYW: SYNW1737
SYC: syc0051_d
SYG: sync_1989
CYA: CYA_0414
CYB: CYB_2441
SYNR: KR49_12750
SYND: KR52_13295
SYNW: SynWH8103_01988(cACR)
TEL: tll1312
PMA: Pro_0533
PMM: PMM0533
PMT: PMT_1230
PRC: EW14_0579
PRM: EW15_0630
AMR: AM1_4042
MAR: MAE_53080
MPK: VL20_1524
CYT: cce_1430
TER: Tery_2279
GVI: gll3145
GLJ: GKIL_0726(hemA)
ANA: alr5284
AVA: Ava_2534
NAZ: Aazo_3370
CALH: IJ00_07395
CTHE: Chro_1553
CEO: ETSB_0189
 » show all
Taxonomy
Reference
1  [PMID:20671186]
  Authors
Schirmer A, Rude MA, Li X, Popova E, del Cardayre SB
  Title
Microbial biosynthesis of alkanes.
  Journal
Science 329:559-62 (2010)
DOI:10.1126/science.1187936
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.2.1.80
IUBMB Enzyme Nomenclature: 1.2.1.80
ExPASy - ENZYME nomenclature database: 1.2.1.80
BRENDA, the Enzyme Database: 1.2.1.80

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