EzCatDB: S00028

DB codeS00028
RLCP classification10.21011.100.10210
CATH domainDomain 11.10.620.20Catalytic domain
E.C.1.14.19.2
CSA1afr
MACiEM0136

CATH domainRelated DB codes (homologues)
1.10.620.20M00151,M00204,M00205

Enzyme Name
Swiss-protKEGG

P22337
Protein nameAcyl-[acyl-carrier-protein] desaturase, chloroplasticacyl-[acyl-carrier-protein] desaturase
stearyl acyl carrier protein desaturase
stearyl-ACP desaturase
acyl-[acyl-carrier-protein], hydrogen-donor:oxygen oxidoreductase
SynonymsEC 1.14.19.2
Stearoyl-ACP desaturase
Delta(9) stearoyl-acyl carrier protein desaturase

KEGG pathways
MAP codePathways
MAP00061Fatty acid biosynthesis
MAP01040Biosynthesis of unsaturated fatty acids

Swiss-prot:Accession NumberP22337
Entry nameSTAD_RICCO
ActivityStearoyl-[acyl-carrier-protein] + reduced acceptor + O(2) = oleoyl-[acyl-carrier-protein] + acceptor + 2 H(2)O.
SubunitHomodimer.
Subcellular locationPlastid, chloroplast. Plastid. Note=In green tissue, found in chloroplasts. In non-photosynthetic tissue, found in plastids.
Cofactor


CofactorsSubstratesProducts
KEGG-idC99999C00007C00138C04088C00001C00139C01203
CompoundDiironO2Reduced ferredoxinStearoyl-[acyl-carrier protein]H2OOxidized ferredoxinOleoyl-[acyl-carrier protein]
Typeheavy metalothersheavy metal,peptide/protein,sulfide groupcarbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide groupH2Oheavy metal,peptide/protein,sulfide groupcarbohydrate,lipid,peptide/protein,phosphate group/phosphate ion,sulfide group
1afrABound:FE2-FE2UnboundUnboundUnbound
UnboundUnbound
1afrBBound:FE2-FE2UnboundUnboundUnbound
UnboundUnbound
1afrCBound:FE2-FE2UnboundUnboundUnbound
UnboundUnbound
1afrDBound:FE2-FE2UnboundUnboundUnbound
UnboundUnbound
1afrEBound:FE2-FE2UnboundUnboundUnbound
UnboundUnbound
1afrFBound:FE2-FE2UnboundUnboundUnbound
UnboundUnbound
1oq4ABound:_FE-_FEAnalogue:AZIUnboundUnbound
UnboundUnbound
1oq4BBound:_FE-_FEAnalogue:AZIUnboundUnbound
UnboundUnbound
1oq4CBound:_FE-_FEAnalogue:AZIUnboundUnbound
UnboundUnbound
1oq4DBound:_FE-_FEAnalogue:AZIUnboundUnbound
UnboundUnbound
1oq4EBound:_FE-_FEAnalogue:AZIUnboundUnbound
UnboundUnbound
1oq4FBound:_FE-_FEAnalogue:AZIUnboundUnbound
UnboundUnbound
1oq7AUnboundUnboundUnboundUnbound
UnboundUnbound
1oq7BUnboundUnboundUnboundUnbound
UnboundUnbound
1oq7CUnboundUnboundUnboundUnbound
UnboundUnbound
1oq7DUnboundUnboundUnboundUnbound
UnboundUnbound
1oq7EUnboundUnboundUnboundUnbound
UnboundUnbound
1oq7FUnboundUnboundUnboundUnbound
UnboundUnbound
1oq9ABound:_FE-_FEUnboundUnboundUnbound
UnboundUnbound
1oqbAAnalogue:FE2UnboundUnboundUnbound
UnboundUnbound
1oqbBAnalogue:FE2UnboundUnboundUnbound
UnboundUnbound
1oqbCAnalogue:FE2UnboundUnboundUnbound
UnboundUnbound
1oqbDAnalogue:FE2UnboundUnboundUnbound
UnboundUnbound
1oqbEAnalogue:FE2UnboundUnboundUnbound
UnboundUnbound
1oqbFAnalogue:FE2UnboundUnboundUnbound
UnboundUnbound

Active-site residues
resource
literature [1]
pdbCatalytic residuesCofactor-binding residues
1afrATRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1afrBTRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1afrCTRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1afrDTRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1afrETRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1afrFTRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oq4ATRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oq4BTRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oq4CTRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oq4DTRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oq4ETRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oq4FTRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oq7ATRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oq7BTRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oq7CTRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oq7DTRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oq7ETRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oq7FTRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oq9ATRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oqbATRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oqbBTRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oqbCTRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oqbDTRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oqbETRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)
1oqbFTRP 62;HIS 146;THR 199;ASP 228
GLU 143;GLU 229(both irons);GLU 196;HIS 232(Iron-1);GLU 105;HIS 146(Iron-2)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]p.4086-4088
[7]Fig.5, Fig.6, p.423-425

references
[1]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)
Medline ID97015109
PubMed ID8861937
JournalEMBO J
Year1996
Volume15
Pages4081-92
AuthorsLindqvist Y, Huang W, Schneider G, Shanklin J
TitleCrystal structure of delta9 stearoyl-acyl carrier protein desaturase from castor seed and its relationship to other di-iron proteins.
Related PDB1afr
Related Swiss-protP22337
[2]
PubMed ID9144157
JournalProc Natl Acad Sci U S A
Year1997
Volume94
Pages4872-7
AuthorsCahoon EB, Lindqvist Y, Schneider G, Shanklin J
TitleRedesign of soluble fatty acid desaturases from plants for altered substrate specificity and double bond position.
[3]
PubMed ID9778341
JournalBiochemistry
Year1998
Volume37
Pages14664-71
AuthorsBroadwater JA, Ai J, Loehr TM, Sanders-Loehr J, Fox BG
TitlePeroxodiferric intermediate of stearoyl-acyl carrier protein delta 9 desaturase: oxidase reactivity during single turnover and implications for the mechanism of desaturation.
[4]
PubMed ID9812895
JournalScience
Year1998
Volume282
Pages1315-7
AuthorsBroun P, Shanklin J, Whittle E, Somerville C
TitleCatalytic plasticity of fatty acid modification enzymes underlying chemical diversity of plant lipids.
[5]
PubMed ID11294879
JournalJ Biol Chem
Year2001
Volume276
Pages21500-5
AuthorsWhittle E, Shanklin J
TitleEngineering delta 9-16:0-acyl carrier protein (ACP) desaturase specificity based on combinatorial saturation mutagenesis and logical redesign of the castor delta 9-18:0-ACP desaturase.
[6]
CommentsX?|ray crystallography
PubMed ID12704186
JournalJ Biol Chem
Year2003
Volume278
Pages25072-80
AuthorsMoche M, Shanklin J, Ghoshal A, Lindqvist Y
TitleAzide and acetate complexes plus two iron-depleted crystal structures of the di-iron enzyme delta9 stearoyl-acyl carrier protein desaturase. Implications for oxygen activation and catalytic intermediates.
Related PDB1oq4,1oq7,1oq9,1oqb
[7]
PubMed ID15260504
JournalAcc Chem Res
Year2004
Volume37
Pages421-9
AuthorsFox BG, Lyle KS, Rogge CE
TitleReactions of the diiron enzyme stearoyl-acyl carrier protein desaturase.
[8]
PubMed ID15667224
JournalBiochemistry
Year2005
Volume44
Pages1309-15
AuthorsDavydov R, Behrouzian B, Smoukov S, Stubbe J, Hoffman BM, Shanklin J
TitleEffect of substrate on the diiron(III) site in stearoyl acyl carrier protein delta 9-desaturase as disclosed by cryoreduction electron paramagnetic resonance/electron nuclear double resonance spectroscopy.

comments
This enzyme was transferred from E.C.1.14.99.6 to E.C. 1.14.19.2.
According to the literature [1], Trp62, His146 & Asp228 might form a route for electron transfer from the enzyme surface to the diiron center. Moreover, Thr199 might be involved in activation of oxygen (see [1]).
According to the literature [7], this enzyme catalyzes three distinct redox reactions. However, this enzyme uses neither NADPH nor ferredoxin reductase directly, although Swissprot data suggested that they are cofactors for this enzyme.
(A) Electron transfer from Ferredoxin to this enzyme active site; Oxidation of ferredoxin (protein).
(B) Electron transfer from acyl-chain to diiron center, producing unsaturated acyl-chain:
(C) O2 reduction to H2O at diiron center: O2 + 4 e(-) + 4 H(+) => 2 H2O
The reaction proceeds as follows:
(A) Electron transfer from Ferredoxin to this enzyme active site; Oxidation of ferredoxin (protein).
(A1) Indirect transfer from [2Fe-2S] of ferredoxin to the diiron of active site of this enzyme through Trp62, Asp228 and His146.

createdupdated
2004-01-262012-06-01


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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