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

BRENDA support

Literature summary extracted from

  • Saffert, P.; Enenkel, C.; Wendler, P.
    Structure and function of p97 and Pex1/6 type II AAA+ complexes (2017), Front. Mol. Biosci., 4, 33 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.6.4.7 Syt1 the cytoplasmic fragment of synaptotagmin Syt1 can substantially increase the basal ATPase activity by approximately 4fold Caenorhabditis elegans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.4.7 Mg2+ dependent on Saccharomyces cerevisiae
3.6.4.7 Mg2+ dependent on Caenorhabditis elegans

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.4.7 ATP + H2O Saccharomyces cerevisiae
-
 ADP + phosphate
-
 ?
3.6.4.7 ATP + H2O Caenorhabditis elegans
-
 ADP + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.6.4.7 Caenorhabditis elegans
-
-
-
3.6.4.7 Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.4.7 ATP + H2O
-
 Saccharomyces cerevisiae ADP + phosphate
-
 ?
3.6.4.7 ATP + H2O
-
 Caenorhabditis elegans ADP + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.6.4.7 heterohexamer Pex1 and Pex6 forma heterohexamer composed of a trimer of Pex1/6 dimers Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
3.6.4.7 Cdc48
-
 Caenorhabditis elegans
3.6.4.7 p97/VCP
-
 Caenorhabditis elegans
3.6.4.7 peroxin
-
 Saccharomyces cerevisiae
3.6.4.7 PEX1/6
-
 Saccharomyces cerevisiae
3.6.4.7 Pex1/6 type II AAA+ complex
-
 Saccharomyces cerevisiae
3.6.4.7 Pex1/Pex6 complex
-
 Saccharomyces cerevisiae
3.6.4.7 valosin-containing protein
-
 Caenorhabditis elegans

General Information

EC Number General Information Comment Organism
3.6.4.7 malfunction mutations in Pex1 and Pex6 cause peroxisome biogenesis disorders Saccharomyces cerevisiae
3.6.4.7 physiological function the enzyme plays a role in many processes, including endoplasmic reticulum-associated protein degradation Caenorhabditis elegans
3.6.4.7 physiological function the Pex1/Pex6 complex dislocates and recycles the transport receptor Pex5 from the peroxisomal membrane during peroxisomal protein import Saccharomyces cerevisiae