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Information on EC 3.1.3.77 - acireductone synthase and Organism(s) Homo sapiens

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.77 acireductone synthase
IUBMB Comments
This bifunctional enzyme first enolizes the substrate to form the intermediate 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate, which is then dephosphorylated to form the acireductone 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one . The acireductone represents a branch point in the methione-salvage pathway as it is used in the formation of formate, CO and 3-(methylsulfanyl)propanoate by EC 1.13.11.53 [acireductone dioxygenase (Ni2+-requiring)] and of formate and 4-(methylsulfanyl)-2-oxobutanoate either by a spontaneous reaction under aerobic conditions or by EC 1.13.11.54 {acireductone dioxygenase [iron(II)-requiring]} [1,2].
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Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
enoph1, enolase-phosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
enolase-phosphatase
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
5-(methylthio)-2,3-dioxopentyl-phosphate phosphohydrolase (isomerizing)
This bifunctional enzyme first enolizes the substrate to form the intermediate 2-hydroxy-5-(methylsulfanyl)-3-oxopent-1-enyl phosphate, which is then dephosphorylated to form the acireductone 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one [2]. The acireductone represents a branch point in the methione-salvage pathway as it is used in the formation of formate, CO and 3-(methylsulfanyl)propanoate by EC 1.13.11.53 [acireductone dioxygenase (Ni2+-requiring)] and of formate and 4-(methylsulfanyl)-2-oxobutanoate either by a spontaneous reaction under aerobic conditions or by EC 1.13.11.54 {acireductone dioxygenase [iron(II)-requiring]} [1,2].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1-oxo-heptyl)-phosphonic acid + H2O
?
show the reaction diagram
substrate analog, in complex with MASA it sits in the cleft formed by the conserved residues in the active site
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
three magnesium ions, one is buried in the active-site pocket in the interface between the two domains, where it serves as a cofactor for the enzyme activity. The other two are located on the surface of the molecule and are supposedly helpful for packing of crystals. Magnesium ions originate from the reservoir solution during crystallization and are absolutely required for the enzyme stability and activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ENOPH_HUMAN
261
0
28933
Swiss-Prot
Secretory Pathway (Reliability: 4)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by hanging drop vapour-diffusion method, to 1.7 A resolution, crystals belong to space group P212121, with unit-cell parameters a = 54.02 A, b = 57.55 A, c = 87.32 A
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crystal structure to 1.7 A resolution of MASA and its complex with a substrate analog, by hanging-drop vapor-diffusion technique
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 20 mM HEPES buffer, pH 7.5
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by Ni2+-chelating affinity column, gel filtration and anion-exchange chromatography, more than 90% pure
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
into the bacterial expression vector pET28a with a His tag on the C-terminus. Recombinant plasmid overexpressed in Escherichia coli strain BL21 (DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
compared with normal brain tissues, the level of Enoph1 is markedly increased in glioma tissues. The glioma pathological grade is positively associated with the expression level of Enoph1. Knockdown of Enoph1 expression with siRNA markedly reduces cell proliferation, and significantly decreases cell migration. Knockdown of Enoph1 promotes its downstream protein, acireductone dioxygenase 1, to shift from the nucleus to the cytoplasm of U251 glioma cells, while membrane type 1-matrix metalloproteinase expression is significantly downregulated compared with the control group
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, H.; Pang, H.; Bartlam, M.; Rao, Z.
Crystal Structure of Human E1 Enzyme and its Complex with a Substrate Analog Reveals the Mechanism of its Phosphatase/Enolase Activity
J. Mol. Biol.
348
917-926
2005
Homo sapiens (Q9UHY7)
Manually annotated by BRENDA team
Wang, H.; Pang, H.; Ding, Y.; Li, Y.; Wu, X.; Rao, Z.
Purification, crystallization and preliminary X-ray diffraction analysis of human enolase-phosphatase E1
Acta Crystallogr. Sect. F
61
521-523
2005
Homo sapiens
Manually annotated by BRENDA team
Su, L.; Yang, K.; Li, S.; Liu, C.; Han, J.; Zhang, Y.; Xu, G.
Enolase-phosphatase 1 as a novel potential malignant glioma indicator promotes cell proliferation and migration
Oncol. Rep.
40
2233-2241
2018
Homo sapiens
Manually annotated by BRENDA team