Literature summary for 1.5.99.B2 extracted from

Monteoliva, M.I.; Rizzi, Y.S.; Cecchini, N.M.; Hajirezaei, M.R.; Alvarez, M.E.
Context of action of proline dehydrogenase (ProDH) in the hypersensitive response of Arabidopsis (2014), BMC Plant Biol., 14, 21 .

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Cloned(Commentary)

Cloned (Comment)	Organism
semi-quantitative, and quantitative RT-PCR enzyme expression analysis	Arabidopsis thaliana

Protein Variants

Protein Variants	Comment	Organism
additional information	mutant plants lacking DELTA1 pyrroline-5-carboxylate dehydrogenase activate ProDH during hypersensitive response like the wild-type plants. They achieve maximum oxidative burst and cell death levels producing normal hypersensitive response lesions, but evidence premature defense activation	Arabidopsis thaliana

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
mitochondrial inner membrane	-	Arabidopsis thaliana	5743	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-proline + acceptor	Arabidopsis thaliana	-	(S)-1-pyrroline-5-carboxylate + reduced acceptor	-	?

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	-	Arabidopsis thaliana	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-proline + acceptor	-	Arabidopsis thaliana	(S)-1-pyrroline-5-carboxylate + reduced acceptor	-	?

Synonyms

Synonyms	Comment	Organism
Pro dehydrogenase	-	Arabidopsis thaliana
PRODH	-	Arabidopsis thaliana

Cofactor

Cofactor	Comment	Organism	Structure
FAD	ProDH is a flavoenzyme, that can eventually transfer electrons to O2	Arabidopsis thaliana

Expression

Organism	Comment	Expression
Arabidopsis thaliana	oxidative burst causes a hypersensitive response with induction of proline dehydrogenase (ProDH), the plants do not consume Pro during maximal reactive oxygen species accumulation, and maintain almost basal DELTA1 pyrroline-5-carboxylate levels at all conditions. Mutant plants lacking DELTA1 pyrroline-5-carboxylate dehydrogenase activate ProDH like the wild-type plants. Under cold acclimation, ProDH induction is accompanied by Pro increase. ProDH activation occuring after stress release does not always be accompanied by P5CDH and can have minor effects on the Pro content	up

General Information

General Information	Comment	Organism
physiological function	proline (Pro) dehydrogenase (ProDH) catalyzes the rate limiting step in the oxidation pathway, transferring two electrons from Pro to the noncovalently bound FAD cofactor to subsequently deliver these electrons to a final acceptor. The plant enzyme sustains oxidative phosphorylation and ATP generation using endogenous electron acceptors. ProDH potentiates the oxidative burst and cell death of the plant hypersensitive response. ProDH converts Pro into DELTA1 pyrroline-5-carboxylate (P5C) and can act together with P5C dehydrogenase (P5CDH) to produce Glu, or with P5C reductase (P5CR) to regenerate Pro and thus stimulate the Pro/P5C cycle. ProDH activation has different effects on hypersensitive response. Before the oxidative burst it leads to Pro consumption involving the action of P5CDH. During the oxidative burst, ProDH becomes functionally uncoupled to P5CDH and apparently works with P5C reductase. The absence of P5CDH does not reduce reactive oxygen species, cell death, or pathogen resistance, indicating this enzyme is not accompanying ProDH in the potentiation of these defense responses. In contrast, p5cdh infected mutant plants display increased reactive oxygen species burst and earlier initiation of hypersensitive response cell death. ProDH may sustain hypersensitive response by participating in the Pro/P5C cycle. Evaluation of ProDH action at different hypersensitive response stages, overview	Arabidopsis thaliana

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Release 2023.1 (January 2023)