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Information on EC 3.6.1.1 - inorganic diphosphatase and Organism(s) Chlamydomonas reinhardtii and UniProt Accession Q949J1

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EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.1 inorganic diphosphatase
IUBMB Comments
Specificity varies with the source and with the activating metal ion. The enzyme from some sources may be identical with EC 3.1.3.1 (alkaline phosphatase) or EC 3.1.3.9 (glucose-6-phosphatase). cf. EC 7.1.3.1, H+-exporting diphosphatase.
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This record set is specific for:
Chlamydomonas reinhardtii
UNIPROT: Q949J1
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Word Map
The taxonomic range for the selected organisms is: Chlamydomonas reinhardtii
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
pyrophosphatase, inorganic pyrophosphatase, v-ppase, h+-ppase, vacuolar h(+)-pyrophosphatase, e-ppase, sppase, vacuolar h(+)-ppase, soluble inorganic pyrophosphatase, ippase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
soluble inorganic pyrophosphatase 2
-
H+-PPase
-
-
-
-
inorganic diphosphatase
-
-
-
-
inorganic pyrophosphatase
-
-
-
-
PPase
-
-
-
-
pyrophosphatase, inorganic
-
-
-
-
Pyrophosphate phospho-hydrolase
-
-
-
-
Pyrophosphate phosphohydrolase
-
-
-
-
Pyrophosphate-energized inorganic pyrophosphatase
-
-
-
-
soluble inorganic pyrophosphatase
-
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
diphosphate phosphohydrolase
Specificity varies with the source and with the activating metal ion. The enzyme from some sources may be identical with EC 3.1.3.1 (alkaline phosphatase) or EC 3.1.3.9 (glucose-6-phosphatase). cf. EC 7.1.3.1, H+-exporting diphosphatase.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-82-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
can partially, upt to 30%, substitute for Mg2+
Fe2+
can partially, upt to 30%, substitute for Mg2+
Mg2+
required, best divalent cation
Mn2+
can partially, upt to 30%, substitute for Mg2+
Zn2+
can partially, upt to 30%, substitute for Mg2+
Cu2+
can partially, upt to 30%, substitute for Mg2+
Fe2+
can partially, upt to 30%, substitute for Mg2+
Mg2+
required, best divalent cation
Mn2+
can partially, upt to 30%, substitute for Mg2+
Zn2+
can partially, upt to 30%, substitute for Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
22
assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ppa2; soluble inorganic pyrophosphatase isozyme II, minor isozyme
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
IPYR2_CHLRE
192
0
22175
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
1 * 24000, isozyme sPPase-II, SDS-PAGE, 1 * 24350, isozyme sPPase-II, mass spectrometry
24350
1 * 24000, isozyme sPPase-II, SDS-PAGE, 1 * 24350, isozyme sPPase-II, mass spectrometry
28000 - 32000
gel filtration and native PAGE
29850
1 * 30000, isozyme sPPase-I, SDS-PAGE, 1 * 29850, isozyme sPPase-I, mass spectrometry
30000
1 * 30000, isozyme sPPase-I, SDS-PAGE, 1 * 29850, isozyme sPPase-I, mass spectrometry
33000 - 37000
gel filtration and native PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 24000, isozyme sPPase-II, SDS-PAGE, 1 * 24350, isozyme sPPase-II, mass spectrometry
monomer
1 * 30000, isozyme sPPase-I, SDS-PAGE, 1 * 29850, isozyme sPPase-I, mass spectrometry
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
the chloroplast isozyme I contains a precursor sequence, the recombinant enzyme is processed in bacterial cells
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native isozyme sPPase-II by streptomycin and ammonium sulfate fractionation, dialysis, anion exchange and hydrophobic interaction chromatography, followed by hydroxylapatite chromatography and gel filtration
native isozyme sPPase-I by streptomycin and ammonium sulfate fractionation, dialysis, anion exchange and hydrophobic interaction chromatography, followed by hydroxylapatite chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ppa2, isozyme sPPase-II, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene ppa1, isozyme sPPase-I, DNA and amino acid sequence determination and analysis, phylogenetic analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gomez-Garcia, M.R.; Losada, M.; Serrano, A.
A novel subfamily of monomeric inorganic pyrophosphatases in photosynthetic eukaryotes
Biochem. J.
395
211-221
2006
Chlamydomonas reinhardtii (Q93Y52), Chlamydomonas reinhardtii (Q949J1), Chlamydomonas reinhardtii, Arabidopsis thaliana (Q9LXC9)
Manually annotated by BRENDA team