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Information on EC 4.2.1.134 - very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase and Organism(s) Homo sapiens

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.134 very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
IUBMB Comments
This is the third component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long chain acyl CoAs. cf. EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, and EC 1.3.1.93, very-long-chain enoyl-CoA reductase.
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Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
ptpla, hacd1, 3-hydroxyacyl-coa dehydratase, hacd4, pasticcino2, hacd2, hacd3, very-long-chain (3r)-3-hydroxyacyl-coa dehydratase, ptpla dehydratase, 3 hydroxyacyl-coa dehydratase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-hydroxyacyl-CoA dehydratase
-
-
HACD1
-
isoform
HACD2
-
isoform
HACD3
-
isoform
HACD4
-
isoform
PAS2
-
-
-
-
PHS1
-
-
-
-
very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
very-long-chain (3R)-3-hydroxyacyl-CoA hydro-lyase
This is the third component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long chain acyl CoAs. cf. EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, and EC 1.3.1.93, very-long-chain enoyl-CoA reductase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-hydroxypalmitoyl-CoA
2,3-trans-hexadecenoyl-CoA + H2O
show the reaction diagram
-
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0068 - 0.1217
3-hydroxypalmitoyl-CoA
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HACD1_HUMAN
288
4
32388
Swiss-Prot
Mitochondrion (Reliability: 5)
HACD2_HUMAN
254
4
28368
Swiss-Prot
Mitochondrion (Reliability: 5)
HACD3_HUMAN
362
5
43160
Swiss-Prot
other Location (Reliability: 4)
HACD4_HUMAN
232
4
27520
Swiss-Prot
Secretory Pathway (Reliability: 5)
H3BMZ1_HUMAN
139
3
16164
TrEMBL
other Location (Reliability: 2)
H3BPZ1_HUMAN
337
5
40069
TrEMBL
other Location (Reliability: 1)
C9JWG1_HUMAN
98
2
11412
TrEMBL
Secretory Pathway (Reliability: 3)
J3KT94_HUMAN
37
1
4058
TrEMBL
Secretory Pathway (Reliability: 2)
H3BRL8_HUMAN
245
6
29206
TrEMBL
other Location (Reliability: 2)
H3BS72_HUMAN
400
5
47118
TrEMBL
other Location (Reliability: 3)
J3KS69_HUMAN
174
2
19719
TrEMBL
other Location (Reliability: 2)
H7C4K8_HUMAN
61
2
6994
TrEMBL
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54900
-
x * 54900, EGFP-tagged HACD4 isoform, estimated from amino acid sequence
55800
-
x * 55800, EGFP-tagged HACD2 isoform, estimated from amino acid sequence
59800
-
x * 59800, EGFP-tagged HACD1 isoform, estimated from amino acid sequence
70600
-
x * 70600, EGFP-tagged HACD3 isoform, estimated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae strain SAY32
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ikeda, M.; Kanao, Y.; Yamanaka, M.; Sakuraba, H.; Mizutani, Y.; Igarashi, Y.; Kihara, A.
Characterization of four mammalian 3-hydroxyacyl-CoA dehydratases involved in very long-chain fatty acid synthesis
FEBS Lett.
582
2435-2440
2008
Homo sapiens
Manually annotated by BRENDA team