Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 4.2.1.134 - very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase and Organism(s) Arabidopsis thaliana and UniProt Accession Q8VZB2

for references in articles please use BRENDA:EC4.2.1.134
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q8VZB2
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
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
-
3-hydroxyacyl-CoA dehydratase
-
Fatty acid elongase
-
3 hydroxyacyl-CoA dehydratase
-
3-hydroxyacyl-CoA dehydratase
-
Fatty acid elongase
-
fatty acyl-CoA dehydratase
-
-
PASTICCINO2
-
-
PHS1
-
-
-
-
PTPLA dehydratase
-
very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase
-
-
-
-
very-long-chain hydroxy fatty acyl-CoA 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-hydroxyacyl-CoA
enoyl-CoA + H2O
show the reaction diagram
-
-
-
?
3-hydroxyacyl-CoA
2,3-trans-enoyl-CoA + H2O
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
enzyme PTPLA is specifically expressed in root vascular tissues
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the very-long-chain 3-hydroxyacyl-CoA dehydratase PTPLA sequence is as divergent from very-long-chain 3-hydroxyacyl-CoA dehydratase PAS2 sequence as it is from yeast very-long-chain 3-hydroxyacyl-CoA dehydratase PHS1
malfunction
physiological function
comparative ectopic expression of the two very-long-chain 3-hydroxyacyl-CoA dehydratases PTPLA and PAS2 in their respective domains confirms the existence of two independent elongase complexes based on PAS2 or PTPLA dehydratase that are functionally interacting. The two dehydratases have specific expression profiles in the root with PAS2 mostly restricted to the endodermis, while PTPLA is confined in the vascular tissue and pericycle cells
evolution
the very-long-chain 3-hydroxyacyl-CoA dehydratase PTPLA sequence is as divergent from very-long-chain 3-hydroxyacyl-CoA dehydratase PAS2 sequence as it is from yeast very-long-chain 3-hydroxyacyl-CoA dehydratase PHS1
malfunction
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HACD_ARATH
221
4
25327
Swiss-Prot
Secretory Pathway (Reliability: 4)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene PAS2 or At5g10480, expression analysis, transient expression of GFP-PAS2 fusion constructs in Nicotiana benthamiana endoplasmic reticulum
expressed in Nicotiana benthamiana and Arabidopsis thaliana epidermal cells
-
gene MTH12.2 or At5g59770, expression analysis, PTPLA is fused with CYFP- or NYFP- at the N-terminal of the protein prevent potential interference with ER retention signal located at the C-terminal end, transient expression of 35S:mCherry-PTPLA constructs in Nicotiana benthamiana. The subcellular distribution of mCherry-PTPLA shows the characteristic endoplasmic reticulum network which is confirmed by its colocalization with endoplasmic reticulum-localized GFP-PAS2 fusion, in contrary to the PTPLA promoter, the KCR2 promoter is also expressed in cotyledons, leaves and in the meristem of secondary roots
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bach, L.; Gissot, L.; Marion, J.; Tellier, F.; Moreau, P.; Satiat-Jeunemaitre, B.; Palauqui, J.C.; Napier, J.A.; Faure, J.D.
Very-long-chain fatty acids are required for cell plate formation during cytokinesis in Arabidopsis thaliana
J. Cell Sci.
124
3223-3234
2011
Arabidopsis thaliana (Q8VZB2), Arabidopsis thaliana
Manually annotated by BRENDA team
Bach, L.; Michaelson, L.V.; Haslam, R.; Bellec, Y.; Gissot, L.; Marion, J.; Da Costa, M.; Boutin, J.P.; Miquel, M.; Tellier, F.; Domergue, F.; Markham, J.E.; Beaudoin, F.; Napier, J.A.; Faure, J.D.
The very-long-chain hydroxy fatty acyl-CoA dehydratase PASTICCINO2 is essential and limiting for plant development
Proc. Natl. Acad. Sci. USA
105
14727-14731
2008
Arabidopsis thaliana
Manually annotated by BRENDA team
Morineau, C.; Gissot, L.; Bellec, Y.; Hematy, K.; Tellier, F.; Renne, C.; Haslam, R.; Beaudoin, F.; Napier, J.; Faure, J.D.
Dual fatty acid elongase complex interactions in Arabidopsis
PLoS ONE
11
e0160631
2016
Arabidopsis thaliana (Q8GW27), Arabidopsis thaliana (Q8VZB2), Saccharomyces cerevisiae (P40857), Saccharomyces cerevisiae
Manually annotated by BRENDA team