WordNet

an amino acid that is found in many proteins (especially collagen)
any of the enzymes that catalyze biological oxidation

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/10/23 20:09:51」(JST)

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Proline dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the PRODH gene.^[1]^[2]^[3]

The protein encoded by this gene is a mitochondrial proline dehydrogenase which catalyzes the first step in proline catabolism. Deletion of this gene has been associated with type I hyperprolinemia. The gene is located on chromosome 22q11.21, a region which has also been associated with the contiguous gene deletion syndromes: DiGeorge syndrome and CATCH22 syndrome.^[3]

References[edit]

^ Campbell HD, Webb GC, Young IG (Dec 1997). "A human homologue of the Drosophila melanogaster sluggish-A (proline oxidase) gene maps to 22q11.2, and is a candidate gene for type-I hyperprolinaemia". Hum Genet 101 (1): 69–74. doi:10.1007/s004390050589. PMID 9385373.
^ Gogos JA, Santha M, Takacs Z, Beck KD, Luine V, Lucas LR, Nadler JV, Karayiorgou M (Apr 1999). "The gene encoding proline dehydrogenase modulates sensorimotor gating in mice". Nat Genet 21 (4): 434–9. doi:10.1038/7777. PMID 10192398.
^ ^a ^b "Entrez Gene: PRODH proline dehydrogenase (oxidase) 1".

External links[edit]

Proline oxidase at the US National Library of Medicine Medical Subject Headings (MeSH)

This article on a gene on chromosome 22 is a stub. You can help Wikipedia by expanding it.

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English Journal

Activation of the NLRP3 Inflammasome in Association with Calcium Oxalate Crystal Induced Reactive Oxygen Species in Kidneys.

Joshi S1, Wang W1, Peck AB2, Khan SR3.
The Journal of urology.J Urol.2015 May;193(5):1684-91. doi: 10.1016/j.juro.2014.11.093. Epub 2014 Nov 28.
PURPOSE: We investigated the association of hyperoxaluria and calcium oxalate crystal induced production of reactive oxygen species with activation of the NLRP3 inflammasome.MATERIALS AND METHODS: Eight-week-old male rats were given hydroxy-L-proline to induce hyperoxaluria. A group of rats on the h
PMID 25437532

Induced resistance by oxidative shifts in pigeonpea (Cajanus cajan L.) following Helicoverpa armigera (Hübner) herbivory.

Kaur R1, Gupta AK, Taggar GK.
Pest management science.Pest Manag Sci.2015 May;71(5):770-82. doi: 10.1002/ps.3851. Epub 2014 Jul 25.
BACKGROUND: Oxidative responses in leaves, developing seeds and the pod wall of nine pigeonpea genotypes were investigated against Helicoverpa armigera feeding. Out of nine genotypes, four were moderately resistant, three were intermediate and two were moderately susceptible genotypes.RESULTS: A sig
PMID 24974811

Role of glycine in improving the ionic and ROS homeostasis during NaCl stress in wheat.

Badran EG1, Abogadallah GM, Nada RM, Nemat Alla MM.
Protoplasma.Protoplasma.2015 May;252(3):835-44. doi: 10.1007/s00709-014-0720-2. Epub 2014 Oct 26.
Nine-day-old wheat seedlings were treated with NaCl at 75, 150, and 225 mM for 15 days in the absence or presence of 5 mM glycine. NaCl particularly at 150 and 225 mM led to significant reductions in fresh and dry weights, chlorophylls, carotenoids, Ca(2+), K(+), and K(+)/Na(+) ratio. Contrarily
PMID 25344655

Japanese Journal

Functional Analysis of Genes Encoding Putative Oxidoreductases in Aspergillus oryzae, Which Are Similar to Fungal Fructosyl-Amino Acid Oxidase(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

Yoshida Nobuyuki,Akazawa Shin-ichi,Karino Tetsuya,Ishida Hiroki,Hata Yoji,Katsuragi Tohoru,Tani Yoshiki,Takagi Hiroshi
Journal of bioscience and bioengineering 104(5), 424-427, 2007-11-25
… rFao2 had fructosyl-amino acid oxidase activity, whereas rFao1 did not show any enzyme activity, even though the deduced amino acid sequence of Fao1 is identical to that of one of the fructosyl-amino acid oxidase isozymes from Aspergillus oryzae. … rFao7 and rFao8 showed oxidase activity toward sarcosine, L-pipecolate, and L-proline. …
NAID 110006473527

微生物酵素の生化学的及び構造生物学的研究と医療への応用

芳本忠
藥學雜誌 127(7), 1035-1045, 2007-07-01
… First, we examined proline-specific peptidases from pathogenic microorganisms. … We found several proline-specific peptidases in pathogenic bacteria. … It was also revealed that proline-specific peptidases and aminopeptidase N cooperatively degrade collagen for the uptake of amino acids as nutrition when these bacteria infect cells. …
NAID 110006318151

Presence and origin of large amounts of D-proline in the urine of mutant mice lacking D-amino acid oxidase activity

HAMASE K.
Anal Bioanal Chem 386, 705-711, 2006
NAID 30002295102

「プロリン酸化酵素」

Proline dehydrogenase (oxidase) 1
Identifiers
Symbols	PRODH; HSPOX2; PIG6; POX; PRODH1; PRODH2; TP53I6
External IDs	OMIM: 606810 MGI: 97770 HomoloGene: 40764 GeneCards: PRODH Gene
EC number	1.5.99.8
Gene Ontology
Molecular function	• proline dehydrogenase activity; • FAD binding;
Cellular component	• mitochondrial inner membrane; • mitochondrial matrix;
Biological process	• glutamate biosynthetic process; • proline metabolic process; • proline catabolic process; • intrinsic apoptotic signaling pathway in response to oxidative stress; • proline catabolic process to glutamate; • 4-hydroxyproline catabolic process; • cellular nitrogen compound metabolic process; • small molecule metabolic process;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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