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Protoporphyrinogen oxidase

PPO, protoporphyrinogen oxidase, PPOX
This gene encodes the penultimate enzyme of heme biosynthesis, which catalyzes the 6-electron oxidation of protoporphyrinogen IX to form protoporphyrin IX. Mutations in this gene cause variegate porphyria, an autosomal dominant disorder of heme metabolism resulting from a deficiency in protoporphyrinogen oxidase, an enzyme located on the inner mitochondrial membrane. Alternatively spliced transcript variants encoding the same protein have been identified. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CAN, HAD, V1a, OUT
Papers on PPO
Different modes of inhibition for organic acids on polyphenoloxidase.
Zhong et al., Nanchang, China. In Food Chem, Jun 2016
It is still unclear whether the inhibitory effect of organic acid on polyphenoloxidase (PPO) is due to the reversible inhibition or decrease of pH.
A highly sensitive electrochemical biosensor for catechol using conducting polymer reduced graphene oxide-metal oxide enzyme modified electrode.
Manisankar et al., Kāraikkudi, India. In Biosens Bioelectron, Jan 2016
UNASSIGNED: The fabrication, characterization and analytical performances were investigated for a catechol biosensor, based on the PEDOT-rGO-Fe2O3-PPO composite modified glassy carbon (GC) electrode.
Selective pressure against horizontally acquired prokaryotic genes as a driving force of plastid evolution.
Rodríguez-Concepción et al., Barcelona, Spain. In Sci Rep, Dec 2015
Here we identify the ancient horizontal transfer of a bacterial polyphenol oxidase (PPO) gene to the nuclear genome of an early land plant ancestor and infer the possible mechanism behind the plastidial localization of the encoded enzyme.
Evidence for the Formation of Benzacridine Derivatives in Alkaline-Treated Sunflower Meal and Model Solutions.
Schieber et al., Bonn, Germany. In Molecules, Dec 2015
SEM and model systems consisting of amino acids and CQA were subjected to alkaline treatment and, for comparison, to oxidation of CQA by polyphenoloxidase (PPO).
[Effects of light intensity on associated enzyme activity and gene expression during callus formation of Vitis vinifera].
Qian et al., In Sheng Wu Gong Cheng Xue Bao, Aug 2015
Peroxidase (POD) and polyphenol oxidase (PPO) activities were negatively correlated with the browning rate of callus (P < 0.01).
Polyphenol oxidase in leaves: is there any significance to the chloroplastic localization?
Kingston-Smith et al., Aberystwyth, United Kingdom. In J Exp Bot, Jun 2015
Polyphenol oxidase (PPO) catalyses the oxidation of monophenols and/or o-diphenols to o-quinones with the concomitant reduction of oxygen to water which results in protein complexing and the formation of brown melanin pigments.
Hepatocellular carcinoma in variegate porphyria: a case report and literature review.
Barth et al., Harrogate, United Kingdom. In Ann Clin Biochem, May 2015
She was biochemically diagnosed with variegate porphyria, and mutational analysis confirmed the presence of a heterozygous mutation in the protoporphyrinogen oxidase gene.
Pluronics and MDR reversal: an update.
Kabanov et al., Chapel Hill, United States. In Mol Pharm, 2014
Triblock copolymers of poly(ethylene oxide) (PEO) and poly(propylene oxide) (PPO), arranged in a triblock structure PEO-PPO-PEO, Pluronics or "poloxamers", raised a considerable interest in the drug delivery field.
Forage polyphenol oxidase and ruminant livestock nutrition.
Lee, Bristol, United Kingdom. In Front Plant Sci, 2013
Polyphenol oxidase (PPO) is predominately associated with the detrimental effect of browning fruit and vegetables, however, interest within PPO containing forage crops (crops to be fed to animals) has grown since the browning reaction was associated with reduced nitrogen (N) losses in silo and the rumen.
Insect prophenoloxidase: the view beyond immunity.
Ling et al., Shanghai, China. In Front Physiol, 2013
Insect prophenoloxidase (PPO) is an important innate immunity protein due to its involvement in cellular and humoral defense.
Proteomic mapping of mitochondria in living cells via spatially restricted enzymatic tagging.
Ting et al., Cambridge, United States. In Science, 2013
Several proteins previously thought to reside in the IMS or outer membrane, including protoporphyrinogen oxidase, were reassigned to the matrix by our proteomic data and confirmed by electron microscopy.
Extended haplotype studies in South African and Dutch variegate porphyria families carrying the recurrent p.R59W mutation confirm a common ancestry.
Frank et al., Maastricht, Netherlands. In Br J Dermatol, 2012
data deliver further confirmation that the South African and Dutch variegate porphyria families carrying mutation p.R59W shared a common ancestor.
Structural insight into human variegate porphyria disease.
Shen et al., Tianjin, China. In Faseb J, 2011
Forty-seven variegate porphyria-causing mutations were purified by chromatography and kinetically characterized in vitro.
GATA-1 binding sites in exon 1 direct erythroid-specific transcription of PPOX.
van Solinge et al., Utrecht, Netherlands. In Gene, 2008
GATA-1 binding sites in exon 1 constitute key regulatory elements in differential expression of PPOX in erythroid and non-erythroid cells.
Swiss patients with variegate porphyria have unique mutations.
Minder et al., Zürich, Switzerland. In Swiss Med Wkly, 2006
Mutation in protoporphyrinogen oxidase is associated with variegate porphyria
Mitochondrial targeting of human protoporphyrinogen oxidase.
Meissner et al., Cape Town, South Africa. In Cell Biol Int, 2006
Protoporphyrinogen oxidase targeting mechanism to the mitochondrion.
King George III and porphyria: an elemental hypothesis and investigation.
Warren et al., Cambridge, United Kingdom. In Lancet, 2005
In 1969 it was proposed that the episodic madness suffered by King George III (1738-1820) resulted from an acute hereditary porphyria, variegate porphyria, caused by deficiency of protoporphyrinogen oxidase.
A R59W mutation in human protoporphyrinogen oxidase results in decreased enzyme activity and is prevalent in South Africans with variegate porphyria.
Dailey et al., Cape Town, South Africa. In Nat Genet, 1996
While earlier workers thought the distal haem biosynthetic enzyme ferrochelatase may be involved in the genesis of VP, it was shown in the early 1980's, and is now accepted, that VP is associated with decreased protoporphyrinogen oxidase activity (PPO) (E.C.
Chester porphyria: biochemical studies of a new form of acute porphyria.
Youngs et al., In Lancet, 1985
Studies of the enzymes of haem biosynthesis in peripheral blood cells showed a dual enzyme deficiency, with reduced activity of both porphobilinogen deaminase, as seen in acute intermittent porphyria, and protoporphyrinogen oxidase, as seen in variegate porphyria.
The enzymatic defect in variegate prophyria. Studies with human cultured skin fibroblasts.
Bloomer et al., In N Engl J Med, 1980
We measured the activities of protoporphyrinogen oxidase, which catalyzes the oxidation of protoporphyrinogen to protoporphyrin, and heme synthase, which catalyzes the chelation of iron to protoporphyrins, in cultured skin fibroblasts from five normal controls and five patients with variegate porphyria.
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