DB code: S00849
RLCP classification | 8.131.161950.140 : Isomerization | |
---|---|---|
8.11113.362040.140 : Isomerization | ||
CATH domain | 3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 | Catalytic domain |
E.C. | 5.3.3.8 | |
CSA | 1pjh | |
M-CSA | 1pjh | |
MACiE |
CATH domain | Related DB codes (homologues) |
---|---|
3.90.226.10 : 2-enoyl-CoA Hydratase; Chain A, domain 1 | M00145 M00122 D00254 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
---|---|---|---|---|
Q05871 |
3,2-trans-enoyl-CoA isomerase (EC 5.3.3.8) (Dodecenoyl-CoA isomerase) (Delta
|
3),Delta(2)-enoyl-CoA isomerase
D3,D2-enoyl-CoA isomerase |
NP_013386.1
(Protein)
NM_001182171.1 (DNA/RNA sequence) |
PF00378
(ECH)
[Graphical View] |
KEGG enzyme name |
---|
Dodecenoyl-CoA isomerase
Dodecenoyl-CoA Delta-isomerase Delta3-cis-Delta2-trans-enoyl-CoA isomerase Acetylene-allene isomerase Dodecenoyl-CoA Delta-isomerase Dodecenoyl-CoA Delta3-cis-Delta2-trans-isomerase |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
Q05871 | ECI1_YEAST | (3Z)-Dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl-CoA. | Homohexamer. Interacts with DCI1. | Peroxisome. This location is DCI1 dependent. |
KEGG Pathways | Map code | Pathways | E.C. |
---|
Compound table | ||||||||
---|---|---|---|---|---|---|---|---|
Substrates | Products | Intermediates | ||||||
KEGG-id | C02944 | C03221 | ||||||
E.C. | ||||||||
Compound | (3Z)-Dodec-3-enoyl-CoA | (2E)-Dodec-2-enoyl-CoA | ||||||
Type | amine group,carbohydrate,lipid,nucleotide ,peptide/protein,sulfide group | amine group,carbohydrate,lipid,nucleotide ,peptide/protein,sulfide group | ||||||
ChEBI |
27989 27989 |
15471 15471 |
||||||
PubChem |
11966217 5280554 11966217 5280554 |
11966110 5280578 11966110 5280578 |
||||||
1hnoA00 | Unbound | Unbound | ||||||
1hnuA00 | Unbound | Unbound | ||||||
1k39A00 | Analogue:CO8 | Unbound | ||||||
1k39B00 | Analogue:CO8 | Unbound | ||||||
1k39C00 | Analogue:CO8 | Unbound | ||||||
1pjhA00 | Unbound | Unbound | ||||||
1pjhB00 | Unbound | Unbound | ||||||
1pjhC00 | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
literature [3] |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1hnoA00 | GLU 158 | ALA 70;LEU 126 | ||||||||
1hnuA00 | GLU 158 | ALA 70;LEU 126 | ||||||||
1k39A00 | GLU 158 | ALA 70;LEU 126 | ||||||||
1k39B00 | GLU 158 | ALA 70;LEU 126 | ||||||||
1k39C00 | GLU 158 | ALA 70;LEU 126 | ||||||||
1pjhA00 | GLU 158 | ALA 70;LEU 126 | ||||||||
1pjhB00 | GLU 158 | ALA 70;LEU 126 | ||||||||
1pjhC00 | GLU 158 | ALA 70;LEU 126 |
References for Catalytic Mechanism | ||
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References | Sections | No. of steps in catalysis |
[3]
|
Figure 1, p.851 | |
[8]
|
Fig.4, p.2516 |
References | |
---|---|
[1] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9813046 |
Journal | J Biol Chem |
Year | 1998 |
Volume | 273 |
Pages | 31366-74 |
Authors | Gurvitz A, Mursula AM, Firzinger A, Hamilton B, Kilpelainen SH, Hartig A, Ruis H, Hiltunen JK, Rottensteiner H |
Title | Peroxisomal Delta3-cis-Delta2-trans-enoyl-CoA isomerase encoded by ECI1 is required for growth of the yeast Saccharomyces cerevisiae on unsaturated fatty acids. |
Related PDB | |
Related UniProtKB | |
[2] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10944342 |
Journal | Acta Crystallogr D Biol Crystallogr |
Year | 2000 |
Volume | 56 |
Pages | 1020-3 |
Authors | Mursula AM, van Aalten DM, Modis Y, Hiltunen JK, Wierenga RK |
Title | Crystallization and X-ray diffraction analysis of peroxisomal Delta3-Delta2-enoyl-CoA isomerase from Saccharomyces cerevisiae. |
Related PDB | |
Related UniProtKB | Q05871 |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11399063 |
Journal | J Mol Biol |
Year | 2001 |
Volume | 309 |
Pages | 845-53 |
Authors | Mursula AM, van Aalten DM, Hiltunen JK, Wierenga RK |
Title | The crystal structure of delta(3)-delta(2)-enoyl-CoA isomerase. |
Related PDB | 1hno 1hnu |
Related UniProtKB | Q05871 |
[4] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11781327 |
Journal | J Biol Chem |
Year | 2002 |
Volume | 277 |
Pages | 9127-32 |
Authors | Zhang D, Yu W, Geisbrecht BV, Gould SJ, Sprecher H, Schulz H |
Title | Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver. |
Related PDB | |
Related UniProtKB | |
[5] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 14741345 |
Journal | FEBS Lett |
Year | 2004 |
Volume | 557 |
Pages | 81-7 |
Authors | Mursula AM, Hiltunen JK, Wierenga RK |
Title | Structural studies on delta(3)-delta(2)-enoyl-CoA isomerase: the variable mode of assembly of the trimeric disks of the crotonase superfamily. |
Related PDB | 1pjh |
Related UniProtKB | Q05871 |
[6] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15351645 |
Journal | J Mol Biol |
Year | 2004 |
Volume | 342 |
Pages | 1197-208 |
Authors | Partanen ST, Novikov DK, Popov AN, Mursula AM, Hiltunen JK, Wierenga RK |
Title | The 1.3 A crystal structure of human mitochondrial Delta3-Delta2-enoyl-CoA isomerase shows a novel mode of binding for the fatty acyl group. |
Related PDB | |
Related UniProtKB | |
[7] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 17028011 |
Journal | Biochim Biophys Acta |
Year | 2006 |
Volume | 1763 |
Pages | 1413-26 |
Authors | Poirier Y, Antonenkov VD, Glumoff T, Hiltunen JK |
Title | Peroxisomal beta-oxidation--a metabolic pathway with multiple functions. |
Related PDB | |
Related UniProtKB | |
[8] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 18470480 |
Journal | Cell Mol Life Sci |
Year | 2008 |
Volume | 65 |
Pages | 2507-27 |
Authors | Hamed RB, Batchelar ET, Clifton IJ, Schofield CJ |
Title | Mechanisms and structures of crotonase superfamily enzymes--how nature controls enolate and oxyanion reactivity. |
Related PDB | |
Related UniProtKB |
Comments |
---|
(B1) Glu158 acts as a general acid to protonate the C4 atom, This enzyme belongs to 2-enoyl-CoA hydratase superfamily. According to the literature [3] and [8], (A) Isomerization from (3Z)-Dodec-3-enoyl-CoA to an enol intermediate: (A1) Glu158 acts as a general base to deprotonate the C2 atom, (A2) The negatively charged oxygen atom is stabilized by mainchain amide groups of Ala70 and Leu126. (B) Isomerization from the enol intermediate to (2E)-Dodec-2-enoyl-CoA: (B0) The negative charge on the thioester is stabilized by mainchain amide groups of Ala70 and Leu126. |
Created | Updated |
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2009-10-09 | 2011-11-09 |