1.2.1.50: long-chain acyl-protein thioester reductase

This is an abbreviated version!
For detailed information about long-chain acyl-protein thioester reductase, go to the full flat file.

Word Map on EC 1.2.1.50

Reaction

a long-chain aldehyde
+
[protein]-L-cysteine
+
NADP+
=
a [protein]-S-(long-chain fatty acyl)-L-cysteine
+
NADPH
+
H+

Synonyms

acyl coenzyme A reductase, acyl-CoA reductase, AmFAR1, CER4, CpFAS1-R, FACoAR, FAR1, FAR2, FAR3, FAR6, FAR8, fatty acyl-CoA reductase, fatty acyl-CoA reductase 1, fatty acyl-CoA reductase 2, fatty acyl-CoA reductase 3, fatty acyl-CoA reductase 6, fatty acyl-CoA reductase 8, long-chain-fatty-acyl-CoA reductase

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.1 With NAD+ or NADP+ as acceptor
                1.2.1.50 long-chain acyl-protein thioester reductase

Reference

Reference on EC 1.2.1.50 - long-chain acyl-protein thioester reductase

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wall, L.; Meighen, E.A.
Subunit structure of the fatty acid reductase complex from Photobacterium phosphoreum
Biochemistry
25
4315-4321
1986
Photobacterium phosphoreum
-
Manually annotated by BRENDA team
Riendeau, D.; Rodriguez, A.; Meighen, E.
Resolution of the fatty acid reductase from Photobacterium phosphoreum into acyl protein synthetase and acyl-CoA reductase activities. Evidence for an enzyme complex
J. Biol. Chem.
257
6908-6915
1982
Photobacterium phosphoreum
Manually annotated by BRENDA team
Rodriguez, A.; Wall, L.; Raptis, S.; Zarkadas, C.G.; Meighen, E.
Different sites for fatty acid activation and acyl transfer by the synthetase subunit of fatty acid reductase: acylation of a cysteinyl residue
Biochim. Biophys. Acta
964
266-275
1988
Photobacterium phosphoreum
-
Manually annotated by BRENDA team
Wang, X.; Kolattukudy, P.E.
Solubilization, purification and characterization of fatty acyl-CoA reductase from duck uropygial gland
Biochem. Biophys. Res. Commun.
208
210-215
1995
Anas platyrhynchos
Manually annotated by BRENDA team
Lee, C.Y.; Meighen, E.A.
Cysteine-286 as the site of acylation of the lux-specific fatty acyl-CoA reductase
Biochim. Biophys. Acta
1338
215-222
1997
Photobacterium leiognathi, Photobacterium phosphoreum
Manually annotated by BRENDA team
Vioque, J.; Kolattukudy, P.E.
Resolution and purification of an aldehyde-generating and an alcohol-generating fatty acyl-CoA reductase from pea leaves (Pisum sativum L.)
Arch. Biochem. Biophys.
340
64-72
1997
Pisum sativum
Manually annotated by BRENDA team
Ishige, T.; Tani, a.; Takabe, K.; Kawasaki, K.; Sakai, Y.; Kato, N.
Wax ester production from n-alkanes by Acinetobacter sp. strain M-1: ultrastructure of cellular inclusions and role of acyl coenzyme A reductase
Appl. Environ. Microbiol.
68
1192-1195
2002
Acinetobacter sp., Acinetobacter sp. (Q8RR58), Acinetobacter sp. M-1 (Q8RR58)
Manually annotated by BRENDA team
Metz, J.G.; Pollard, M.R.; Anderson, L.; Hayes, T.R.; Lassner, M.W.
Purification of a jojoba embryo fatty acyl-coenzyme A reductase and expression of its cDNA in high erucic acid rapeseed
Plant Physiol.
122
635-644
2000
Simmondsia chinensis
Manually annotated by BRENDA team
Wall, L.; Meighen, E.
Covalent reaction of cerulenin at the active site of acyl-CoA reductase of Photobacterium phosphoreum
Biochem. Cell Biol.
67
163-167
1989
Photobacterium phosphoreum
Manually annotated by BRENDA team
Rodriguez, A.; Wall, L.; Riendeau, D.; Meighen, E.
Fatty acid reductase from Photobacterium phosphoreum
Methods Enzymol.
133
172-182
1986
Photobacterium phosphoreum
-
Manually annotated by BRENDA team
Wall, L.; Rodriguez, A.; Meighen, E.
Intersubunit transfer of fatty acyl groups during fatty acid reduction
J. Biol. Chem.
261
15981-15988
1986
Photobacterium phosphoreum
Manually annotated by BRENDA team
Rodriguez, A.; Riendeau, D.; Meighen, E.
Purification of the acyl coenzyme A reductase component from a complex responsible for the reduction of fatty acids in bioluminescent bacteria. Properties and acyltransferase activity
J. Biol. Chem.
258
5233-5237
1983
Photobacterium phosphoreum
Manually annotated by BRENDA team
Riendeau, D.; Meighen, E.
Fatty acid reductase in bioluminescent bacteria. Resolution from aldehyde reductases and characterization of the aldehyde product
Can. J. Biochem.
59
440-446
1981
Photobacterium phosphoreum
Manually annotated by BRENDA team
Kalscheuer, R.; Stoeveken, T.; Luftmann, H.; Malkus, U.; Reichelt, R.; Steinbuechel, A.
Neutral lipid biosynthesis in engineered Escherichia coli: jojoba oil-like wax esters and fatty acid butyl esters
Appl. Environ. Microbiol.
72
1373-1379
2006
Simmondsia chinensis
Manually annotated by BRENDA team
Doan, T.T.; Carlsson, A.S.; Hamberg, M.; Buelow, L.; Stymne, S.; Olsson, P.
Functional expression of five Arabidopsis fatty acyl-CoA reductase genes in Escherichia coli
J. Plant Physiol.
166
787-796
2009
Arabidopsis thaliana (B9TSP7), Arabidopsis thaliana (Q08891), Arabidopsis thaliana (Q1PEI6), Arabidopsis thaliana (Q39152), Arabidopsis thaliana (Q93ZB9)
Manually annotated by BRENDA team
Willis, R.M.; Wahlen, B.D.; Seefeldt, L.C.; Barney, B.M.
Characterization of a fatty acyl-CoA reductase from Marinobacter aquaeolei VT8: a bacterial enzyme catalyzing the reduction of fatty acyl-CoA to fatty alcohol
Biochemistry
50
10550-10558
2011
Marinobacter hydrocarbonoclasticus
Manually annotated by BRENDA team
Zhu, G.; Shi, X.; Cai, X.
The reductase domain in a Type i fatty acid synthase from the apicomplexan Cryptosporidium parvum: Restricted substrate preference towards very long chain fatty acyl thioesters
BMC Biochem.
11
46
2010
Cryptosporidium parvum
Manually annotated by BRENDA team
Hofvander, P.; Doan, T.T.; Hamberg, M.
A prokaryotic acyl-CoA reductase performing reduction of fatty acyl-CoA to fatty alcohol
FEBS Lett.
585
3538-3543
2011
Marinobacter hydrocarbonoclasticus
Manually annotated by BRENDA team
Teerawanichpan, P.; Robertson, A.J.; Qiu, X.
A fatty acyl-CoA reductase highly expressed in the head of honey bee (Apis mellifera) involves biosynthesis of a wide range of aliphatic fatty alcohols
Insect Biochem. Mol. Biol.
40
641-649
2010
Apis mellifera, Apis mellifera (D9MWM7)
Manually annotated by BRENDA team