A group of enzymes that catalyze the reduction of 1-pyrroline carboxylate to proline in the presence of NAD(P)H. Includes both the 2-oxidoreductase (EC 1.5.1.1) and the 5-oxidoreductase (EC 1.5.1.2). The former also reduces 1-piperidine-2-carboxylate to pipecolate and the latter also reduces 1-pyrroline-3-hydroxy-5-carboxylate to hydroxyproline.
A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.
Enzymes catalyzing the dehydrogenation of secondary amines, introducing a C=N double bond as the primary reaction. In some cases this is later hydrolyzed.
Pipecolic acids are cyclic amino acids, specifically a derivative of L-lysine, that can function as an indicator of certain metabolic disorders such as lysinuric protein intolerance and maple syrup urine disease.
An NADP+ dependent enzyme that catalyzes the oxidation of L-glutamate 5-semialdehyde to L-glutamyl 5-phosphate. It plays a role in the urea cycle and metabolism of amino groups.
The first enzyme of the proline degradative pathway. It catalyzes the oxidation of proline to pyrroline-5-carboxylic acid in the presence of oxygen and water. The action is not reversible. The specific activity of proline oxidase increases with age. EC 1.5.3.-.
Heterocyclic compounds in which an oxygen is attached to a cyclic nitrogen.
A technique for detecting short-lived reactive FREE RADICALS in biological systems by providing a nitrone or nitrose compound for an addition reaction to occur which produces an ELECTRON SPIN RESONANCE SPECTROSCOPY-detectable aminoxyl radical. In spin trapping, the compound trapping the radical is called the spin trap and the addition product of the radical is identified as the spin adduct. (Free Rad Res Comm 1990;9(3-6):163)
Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)

Proline biosynthesis from L-ornithine in Clostridium sticklandii: purification of delta1-pyrroline-5-carboxylate reductase, and sequence and expression of the encoding gene, proC. (1/66)

Clostridium sticklandii utilizes combinations of amino acids for growth by Stickland reactions. Proline is an efficient electron acceptor in these reactions and is reduced to 5-aminovalerate. Proline can be partly synthesized from ornithine by the action of ornithine aminotransferase and delta1-pyrroline-5-carboxylate (PCA) reductase. Both enzymes were present in crude extracts of C. sticklandii in sufficient activity of 0.93 nkat (mg protein)(-1) and 4.3 nkat (mg protein)(-1), respectively, whereas enzymes involved in proline biosynthesis from glutamate were not detected. PCA reductase was purified to homogeneity in a three-step procedure involving ammonium sulfate precipitation, affinity chromatography with Procion Red and gel filtration on Sephadex GF200. The homogeneous enzyme was most likely an octamer of 230 kDa with a subunit size of 25 kDa as obtained by SDS-PAGE and 28.9 kDa as calculated from the sequence. Apparent Km values for PCA and NADH were 0.19 mM and 0.025 mM, respectively. The enzyme also catalysed in vitro the reverse reaction, the oxidation of proline, at alkaline pH values above 8 and higher substrate concentrations (apparent Km values: 1.55 mM for proline and 10.5 mM for NAD at pH 10.0). Studies with growing cells of C. sticklandii and [15N]proline revealed that proline is not oxidized in vivo because 15N was solely detected by HPLC-MS in 5-aminovalerate as the product of proline reduction. The proC gene encoding PCA reductase of C. sticklandii was cloned, sequenced and heterologously expressed in Escherichia coli. The enzyme exhibited high homologies to PCA reductases from different sources. Thus, C. sticklandii is able to synthesize the electron acceptor proline from ornithine (a degradation product of arginine) by action of ornithine aminotransferase and PCA reductase.  (+info)

A multisubunit complex of outer and inner mitochondrial membrane protein translocases stabilized in vivo by translocation intermediates. (2/66)

Translocation of nuclear encoded preproteins into the mitochondrial matrix requires the coordinated action of two translocases: one (Tom) located in the outer mitochondrial membrane and the other (Tim) located in the inner membrane. These translocases reversibly cooperate during protein import. We have previously constructed a chimeric precursor (pPGPrA) consisting of an authentic mitochondrial precursor at the N terminus (Delta(1)-pyrroline-5-carboxylate dehydrogenase, pPut) linked, through glutathione S-transferase, to protein A. When pPGPrA is expressed in yeast, it becomes irreversibly arrested during translocation across the outer and inner mitochondrial membranes. Consequently, the two membranes of mitochondria become progressively "zippered" together, forming long stretches in which they are in close contact (Schulke, N., Sepuri, N. B. V., and Pain, D. (1997) Proc. Natl. Acad. Sci. U. S. A. 94, 7314-7319). We now demonstrate that trapped PGPrA intermediates hold the import channels stably together and inhibit mitochondrial protein import and cell growth. Using IgG-Sepharose affinity chromatography of solubilized zippered membranes, we have isolated a multisubunit complex that contains all Tom and Tim components known to be essential for import of matrix-targeted proteins, namely Tom40, Tom22, Tim17, Tim23, Tim44, and matrix-localized Hsp70. Further characterization of this complex may shed light on structural features of the complete mitochondrial import machinery.  (+info)

A 69 bp fragment in the pyrroline-5-carboxylate reductase promoter of Arabidopsis thaliana activates minimal CaMV 35S promoter in a tissue-specific manner. (3/66)

The Arabidopsis thaliana gene that encodes pyrroline-5-carboxylate reductase (At-P5R), the last enzyme in proline biosynthesis in A. thaliana, is developmentally regulated and is highly expressed in cells that divide rapidly or undergo changes in osmotic potential. A 69 bp region (P69; -120 to -51) has previously been identified in a 5' deletion analysis of the At-P5R promoter to be necessary for the basal expression. Here, the essential role of P69 for tissue-specific expression of At-P5R is demonstrated by loss- and gain-of-function experiments.  (+info)

Fits, pyridoxine, and hyperprolinaemia type II. (4/66)

The rare inherited disorder hyperprolinaemia type II presents with fits in childhood, usually precipitated by infection. A diagnosis of hyperprolinaemia type II and vitamin B(6) deficiency was made in a well nourished child with fits. It is thought that pyridoxine deficiency was implicated in her fits and was the result of inactivation of the vitamin by the proline metabolite, pyrroline-5-carboxylate.  (+info)

Extraordinarily high density of unrelated genes showing overlapping and intraintronic transcription units. (5/66)

The cloning of pyrroline 5-carboxylate reductase from Drosophila melanogaster was accomplished by cDNA complementation of an Escherichia coli proline auxotroph. The corresponding P5cr gene is tightly clustered with three other expressed coding regions. A bidirectional promoter, an overlapping 3'UTR and an intraintronic sequence may all be found in only 4.3 kb, making this the most densely clustered region of unrelated genes in any eukaryote.  (+info)

The Bradyrhizobium japonicum proline biosynthesis gene proC is essential for symbiosis. (6/66)

Plant host-derived proline is proposed to serve as an energy source for rhizobia in the rhizosphere and in symbiotic root nodules. The Bradyrhizobium japonicum proC gene was isolated, and a proC mutant strain that behaved as a strict proline auxotroph in culture was constructed. The proC strain elicited undeveloped nodules on soybeans that lacked nitrogen fixation activity and plant hemoglobin. We conclude that the proC gene is essential for symbiosis and suggest that the mutant does not obtain an exogenous supply of proline in association with soybeans sufficient to satisfy its auxotrophy.  (+info)

Biosynthesis of proline in Pseudomonas aeruginosa. Properties of gamma-glutamyl phosphate reductase and 1-pyrroline-5-carboxylate reductase. (7/66)

gamma-Glutamyl phosphate reductase, the second enzyme of proline biosynthesis, catalyses the formation of l-glutamic acid 5-semialdehyde from gamma-glutamyl phosphate with NAD(P)H as cofactor. It was purified 150-fold from crude extracts of Pseudomonas aeruginosa PAO 1 by DEAE-cellulose chromatography and hydroxyapatite adsorption chromatography. The partially purified preparation, when assayed in the reverse of the biosynthetic direction, utilized l-1-pyrroline-5-carboxylic acid as substrate and reduced NAD(P)(+). The apparent K(m) values were: NAD(+), 0.36mm; NADP(+), 0.31mm; l-1-pyrroline-5-carboxylic acid, 4mm with NADP(+) and 8mm with NAD(+); P(i), 28mm. 3-(Phosphonoacetylamido)-l-alanine, a structural analogue of gamma-glutamyl phosphate, inhibited this enzyme competitively (K(i)=7mm). 1-Pyrroline-5-carboxylate reductase (EC 1.5.1.2), the third enzyme of proline biosynthesis, was purified 56-fold by (NH(4))(2)SO(4) fractionation, Sephadex G-150 gel filtration and DEAE-cellulose chromatography. It reduced l-1-pyrroline-5-carboxylate with NAD(P)H as a cofactor to l-proline. NADH (K(m)=0.05mm) was a better substrate than NADPH (K(m)=0.02mm). The apparent K(m) values for l-1-pyrroline-5-carboxylate were 0.12mm with NADPH and 0.09mm with NADH. The 3-acetylpyridine analogue of NAD(+) at 2mm caused 95% inhibition of the enzyme, which was also inhibited by thio-NAD(P)(+), heavy-metal ions and thiol-blocking reagents. In cells of strain PAO 1 grown on a proline-medium the activity of gamma-glutamyl kinase and gamma-glutamyl phosphate reductase was about 40% lower than in cells grown on a glutamate medium. No repressive effect of proline on 1-pyrroline-5-carboxylate reductase was observed.  (+info)

Multiple genes for the last step of proline biosynthesis in Bacillus subtilis. (8/66)

The complete Bacillus subtilis genome contains four genes (proG, proH, proI, and comER) with the potential to encode Delta(1)-pyrroline-5-carboxylate reductase, a proline biosynthetic enzyme. Simultaneous defects in three of these genes (proG, proH, and proI) were required to confer proline auxotrophy, indicating that the products of these genes are mostly interchangeable with respect to the last step in proline biosynthesis.  (+info)

Pyrroline-5-carboxylate reductase (PCR) is an enzyme that belongs to the family of oxidoreductases. Specifically, it is a part of the subclass of aldo-keto reductases. This enzyme catalyzes the chemical reaction that converts pyrroline-5-carboxylate to proline, which is an essential step in the biosynthesis of proline, an important proteinogenic amino acid.

The reaction catalyzed by PCR involves the reduction of a keto group to a hydroxyl group, and it requires the cofactor NADPH as a reducing agent. The systematic name for this enzyme is pyrroline-5-carboxylate:NADP+ oxidoreductase (proline-forming).

Deficiencies in PCR have been associated with several human diseases, including hyperprolinemia type II, a rare inherited disorder characterized by an accumulation of pyrroline-5-carboxylate and proline in body fluids.

Proline is an organic compound that is classified as a non-essential amino acid, meaning it can be produced by the human body and does not need to be obtained through the diet. It is encoded in the genetic code as the codon CCU, CCC, CCA, or CCG. Proline is a cyclic amino acid, containing an unusual secondary amine group, which forms a ring structure with its carboxyl group.

In proteins, proline acts as a structural helix breaker, disrupting the alpha-helix structure and leading to the formation of turns and bends in the protein chain. This property is important for the proper folding and function of many proteins. Proline also plays a role in the stability of collagen, a major structural protein found in connective tissues such as tendons, ligaments, and skin.

In addition to its role in protein structure, proline has been implicated in various cellular processes, including signal transduction, apoptosis, and oxidative stress response. It is also a precursor for the synthesis of other biologically important compounds such as hydroxyproline, which is found in collagen and elastin, and glutamate, an excitatory neurotransmitter in the brain.

Oxidoreductases acting on CH-NH group donors are a class of enzymes within the larger group of oxidoreductases, which are responsible for catalyzing oxidation-reduction reactions. Specifically, this subclass of enzymes acts on CH-NH group donors, where the CH-NH group is a chemical functional group consisting of a carbon atom (C) bonded to a nitrogen atom (N) via a single covalent bond.

These enzymes play a crucial role in various biological processes by transferring electrons from the CH-NH group donor to an acceptor molecule, which results in the oxidation of the donor and reduction of the acceptor. This process can lead to the formation or breakdown of chemical bonds, and plays a key role in metabolic pathways such as amino acid degradation and nitrogen fixation.

Examples of enzymes that fall within this class include:

* Amino oxidases, which catalyze the oxidative deamination of amino acids to produce alpha-keto acids, ammonia, and hydrogen peroxide.
* Transaminases, which transfer an amino group from one molecule to another, often in the process of amino acid biosynthesis or degradation.
* Amine oxidoreductases, which catalyze the oxidation of primary amines to aldehydes and secondary amines to ketones, with the concomitant reduction of molecular oxygen to hydrogen peroxide.

Pipicolic acid is not a term that refers to a specific medical condition or disease. Instead, it is a metabolite that is involved in the body's metabolic processes.

Pipicolic acid is a type of organic compound called a cyclic amino acid, which is derived from the amino acid lysine. It is produced in the liver and is excreted in urine. Pipicolic acid has been found to have various functions in the body, including regulating the metabolism of lipids and bile acids.

Abnormal levels of pipicolic acid in the body may be associated with certain medical conditions, such as liver disease or genetic disorders that affect amino acid metabolism. However, pipicolic acid is not typically used as a diagnostic marker for these conditions.

In summary, pipicolic acid is a cyclic amino acid produced in the liver and involved in various metabolic processes in the body. Abnormal levels of pipicolic acid may be associated with certain medical conditions but are not typically used as diagnostic markers.

Glutamate-5-semialdehyde dehydrogenase (G5SDH) is an enzyme that plays a crucial role in the metabolism of amino acids, specifically in the catabolic pathway of the amino acid tryptophan. G5SDH catalyzes the conversion of glutamate-5-semialdehyde to 5-aminolevulinate, which is a precursor for the synthesis of porphyrins, including heme, a component of hemoglobin.

The reaction catalyzed by G5SDH involves the oxidation of glutamate-5-semialdehyde to 5-aminolevulinate, with the concomitant reduction of NAD+ to NADH. Deficiencies in G5SDH activity can lead to neurological disorders and impaired heme synthesis, as observed in certain genetic diseases such as 2,4-dienoyl-CoA reductase deficiency and pyridoxine-dependent epilepsy.

Proline oxidase is an enzyme that catalyzes the chemical reaction of oxidizing proline to Δ^1^-pyrroline-5-carboxylate (P5C) and hydrogen peroxide (H2O2). The reaction is a part of the catabolic pathway for proline utilization in some organisms.

The systematic name for this enzyme is L-proline:oxygen oxidoreductase (deaminating, decarboxylating). It belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as an acceptor. This enzyme participates in arginine and proline metabolism.

Cyclic N-oxides are a class of organic compounds that contain a cyclic structure with a nitrogen atom bonded to an oxygen atom as an N-oxide. An N-oxide is a compound in which the nitrogen atom has a positive charge and the oxygen atom has a negative charge, forming a polar covalent bond. In cyclic N-oxides, this N-O group is part of a ring structure, which can be composed of various combinations of carbon, nitrogen, and other atoms. These compounds have been studied for their potential use in pharmaceuticals, agrochemicals, and materials science.

Spin trapping is a technique used in free radical research to detect and study short-lived, reactive free radicals. It involves the use of spin trap compounds, which react with the radicals to form more stable, longer-lived radical adducts. These adducts can then be detected and analyzed using various techniques such as electron paramagnetic resonance (EPR) spectroscopy.

The spin trap compound is typically a nitrone or nitroso compound, which reacts with the free radical to form a nitroxide radical. The nitroxide radical has a characteristic EPR spectrum that can be used to identify and quantify the original free radical. This technique allows for the direct detection and measurement of free radicals in biological systems, providing valuable insights into their role in various physiological and pathological processes.

NADP (Nicotinamide Adenine Dinucleotide Phosphate) is a coenzyme that plays a crucial role as an electron carrier in various redox reactions in the human body. It exists in two forms: NADP+, which functions as an oxidizing agent and accepts electrons, and NADPH, which serves as a reducing agent and donates electrons.

NADPH is particularly important in anabolic processes, such as lipid and nucleotide synthesis, where it provides the necessary reducing equivalents to drive these reactions forward. It also plays a critical role in maintaining the cellular redox balance by participating in antioxidant defense mechanisms that neutralize harmful reactive oxygen species (ROS).

In addition, NADP is involved in various metabolic pathways, including the pentose phosphate pathway and the Calvin cycle in photosynthesis. Overall, NADP and its reduced form, NADPH, are essential molecules for maintaining proper cellular function and energy homeostasis.

1-pyrroline-5-carboxylate reductase, NADPH-L-Delta1-pyrroline carboxylic acid reductase, and L-proline-NAD(P)+ 5-oxidoreductase ... In enzymology, a pyrroline-5-carboxylate reductase (EC 1.5.1.2) is an enzyme that catalyzes the chemical reaction L-proline + ... Yura T; Vogel HJ (1959). "Pyrroline-5-carboxylate reductase of Neurospora crassa: partial purification and some properties". ... Smith ME; Greenberg DM (1956). "Characterization of an enzyme reducing pyrroline-5-carboxylate to proline". Nature. 177 (4520 ...
In enzymology, a pyrroline-2-carboxylate reductase (EC 1.5.1.1) is an enzyme that catalyzes the chemical reaction L-proline + ... This enzyme is also called Delta1-pyrroline-2-carboxylate reductase. This enzyme participates in lysine degradation and ... 1-pyrroline-2-carboxylate + NAD(P)H + H+ The 3 substrates of this enzyme are L-proline, NAD+, and NADP+, whereas its 4 products ... are 1-pyrroline-2-carboxylate, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those ...
Pyrroline-5-carboxylate reductase 1, mitochondrial is an enzyme that in humans is encoded by the PYCR1 gene. This gene encodes ... "Entrez Gene: PYCR1 pyrroline-5-carboxylate reductase 1". Reversade B, Escande-Beillard N, Dimopoulou A, Fischer B, Chng SC, Li ... Meng Z, Lou Z, Liu Z, Li M, Zhao X, Bartlam M, Rao Z (June 2006). "Crystal structure of human pyrroline-5-carboxylate reductase ... PDBe-KB provides an overview of all the structure information available in the PDB for Human Pyrroline-5-carboxylate reductase ...
Pyrroline-5-carboxylate reductase family, member 2 is a protein that in humans is encoded by the PYCR2 gene. This gene belongs ... "Entrez Gene: Pyrroline-5-carboxylate reductase family, member 2". Nakayama, T; Al-Maawali, A; El-Quessny, M; Rajab, A; Khalil, ... to the pyrroline-5-carboxylate reductase family. The encoded mitochondrial protein catalyzes the conversion of pyrroline-5- ... Encoding Pyrroline-5-Carboxylate Reductase 2, Cause Microcephaly and Hypomyelination". American Journal of Human Genetics. 96 ( ...
Pyrroline-5-Carboxylate Reductase 1; PYCR1 - 179035 Online Mendelian Inheritance in Man (OMIM): Aldehyde Dehydrogenase 18 ...
Pyrroline-5-carboxylate reductase 1 (PYCR1), pyrroline-5-carboxylate reductase 2 (PYCR2), and pyrroline-5-carboxylate reductase ... Delta-1-pyrroline-5-carboxylate synthase catalyzes the conversion of glutamate to delta-1-pyrroline-5-carboxylate synthase. ... "PYCR1 pyrroline-5-carboxylate reductase 1 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2022-10-22. " ... "PYCR2 pyrroline-5-carboxylate reductase 2 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2022-10-22. " ...
Pyrroline-5-carboxylate is further reduced by the enzyme pyrroline-5-carboxylate reductase (P5CR) to yield a proline amino acid ... The next reaction is catalyzed by the enzyme pyrroline-5-carboxylate synthase (P5CS), which catalyzes the reduction of the ϒ- ... Pérez-Arellano, I; Carmona-Alvarez, F; Martínez, AI; Rodríguez-Díaz, J; Cervera, J (March 2010). "Pyrroline-5-carboxylate ... This results in the formation of glutamate semialdehyde, which spontaneously cyclizes to pyrroline-5-carboxylate. ...
The enzyme pyrroline-5-carboxylate reductase converts P5C into proline In proline degradation, the enzyme proline dehydrogenase ... "Δ1-Pyrroline-5-carboxylate and Δ1-pyrroline-3-hydroxy-5-carboxylate: Chromatography on the amino acid analyzer". Analytical ... Liu G, Maunoury C, Kamoun P, Aral B (Oct 1996). "Assignment of the human gene encoding the delta 1-pyrroline-5-carboxylate ... Its conjugate base and anion is 1-pyrroline-5-carboxylate (P5C). In solution, P5C is in spontaneous equilibrium with glutamate- ...
Delta-1-pyrroline-5-carboxylate synthetase (P5CS) is an enzyme that in humans is encoded by the ALDH18A1 gene. This gene is a ... P5CS consists of two domains: gamma-glutamyl kinase and gamma-glutamyl phosphate reductase, each of which are used to complete ... Hu CA, Khalil S, Zhaorigetu S, Liu Z, Tyler M, Wan G, Valle D (November 2008). "Human Delta1-pyrroline-5-carboxylate synthase: ... Liu G, Maunoury C, Kamoun P, Aral B (October 1996). "Assignment of the human gene encoding the delta 1-pyrroline-5-carboxylate ...
... which is reduced to proline by pyrroline-5-carboxylate reductase (using NADH or NADPH), or turned into ornithine by ornithine ... "An Ancestral Allele of Pyrroline-5-carboxylate synthase1 Promotes Proline Accumulation and Drought Adaptation in Cultivated ... This can then either spontaneously cyclize to form 1-pyrroline-5-carboxylic acid, ...
1-pyrroline-5-carboxylate dehydrogenase MeSH D08.811.682.662.695 - pyrroline carboxylate reductases MeSH D08.811.682.662.750 - ... gmp reductase MeSH D08.811.682.655.500 - nitrate reductases MeSH D08.811.682.655.500.124 - nitrate reductase MeSH D08.811. ... nitrite reductases MeSH D08.811.682.655.750.249 - ferredoxin-nitrite reductase MeSH D08.811.682.655.750.500 - nitrite reductase ... testosterone 5-alpha-Reductase MeSH D08.811.682.662.162 - dihydropteridine reductase MeSH D08.811.682.662.171 - FMN reductase ...
December 2005). "Crystal structures of Delta1-piperideine-2-carboxylate/Delta1-pyrroline-2-carboxylate reductase belonging to a ...
... which is reduced to proline by pyrroline-5-carboxylate reductase (using NADH or NADPH), or turned into ornithine by ornithine ... For example, Birch reduction of pyrrole esters and amides produced pyrrolines, with the regioselectivity depending on the ... Structural analogs of pyrrole include: Pyrroline, a partially saturated analog with one double bond Pyrrolidine, the saturated ... This can then either spontaneously cyclize to form 1-pyrroline-5-carboxylic acid, ...
... which is reduced to proline by pyrroline-5-carboxylate reductase (using NADH or NADPH), or turned into ornithine by ornithine ... This can then either spontaneously cyclize to form 1-pyrroline-5-carboxylic acid, ...
"Crystal structures of Delta1-piperideine-2-carboxylate/Delta1-pyrroline-2-carboxylate reductase belonging to a new family of ... However, there are a few exceptions to this general rule, and enzymes such as aldose reductase, glucose-6-phosphate ... Argyrou A, Vetting MW, Aladegbami B, Blanchard JS (2006). "Mycobacterium tuberculosis dihydrofolate reductase is a target for ... and dihydrofolate reductase. Since many oxidoreductases use NAD+ and NADH as substrates, and bind them using a highly conserved ...
Deletion 6q16 q21 Delirium Delirium tremens Delusional disorder Delleman-Oorthuys syndrome Delta-1-pyrroline-5-carboxylate ... lung disease DiGeorge syndrome Digestive duplication Digitorenocerebral syndrome Digoxin toxicity Dihydropteridine reductase ...
1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase [NAD(P)H EC 1.5.1.2: pyrroline-5-carboxylate reductase EC 1.5. ... 2-methyl-1-pyrroline reductase * EC 1.5.1.49: 1-pyrroline-2-carboxylate reductase [NAD(P)H] * EC 1.5.1.50: dihydromonapterin ... methylenetetrahydrofolate reductase (NAD(P)H) EC 1.5.1.21: 1-piperideine-2-carboxylate/1-pyrroline-2-carboxylate reductase ( ... flavin reductase (NADH) EC 1.5.1.37: FAD reductase (NADH) EC 1.5.1.38: FMN reductase (NADPH) EC 1.5.1.39: FMN reductase (NAD(P) ...
1-pyrroline-4-hydroxy-2-carboxylate deaminase EC 3.5.4.23: blasticidin-S deaminase EC 3.5.4.24: sepiapterin deaminase EC 3.5. ... dinitrogen reductase] hydrolase EC 3.2.2.25: N-methyl nucleosidase EC 3.2.2.26: futalosine hydrolase EC 3.2.2.27: uracil-DNA ... hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase EC 3.1.3.48: protein-tyrosine-phosphatase EC 3.1.3.49: [pyruvate ... 1-aminocyclopropane-1-carboxylate deaminase EC 3.5.99.8: 5-nitroanthranilic acid aminohydrolase EC 3.5.99.9: 2-nitroimidazole ...
1-pyrroline-5-carboxylate reductase, NADPH-L-Delta1-pyrroline carboxylic acid reductase, and L-proline-NAD(P)+ 5-oxidoreductase ... In enzymology, a pyrroline-5-carboxylate reductase (EC 1.5.1.2) is an enzyme that catalyzes the chemical reaction L-proline + ... Yura T; Vogel HJ (1959). "Pyrroline-5-carboxylate reductase of Neurospora crassa: partial purification and some properties". ... Smith ME; Greenberg DM (1956). "Characterization of an enzyme reducing pyrroline-5-carboxylate to proline". Nature. 177 (4520 ...
Functional Impact of a Cancer-Related Variant in Human Δ-Pyrroline-5-Carboxylate Reductase 1.. Publication Type:. Journal ... p,Pyrroline-5-carboxylate reductase (PYCR) is a proline biosynthetic enzyme that catalyzes the NAD(P)H-dependent reduction of Δ ... Home » Functional Impact of a Cancer-Related Variant in Human Δ-Pyrroline-5-Carboxylate Reductase 1. ... pyrroline-5-carboxylate (P5C) to proline. Humans have three PYCR isoforms, with PYCR1 often upregulated in different types of ...
Mutation in pyrroline-5-carboxylate reductase 1 gene in families with cutis laxa type 2. Am J Hum Genet. 2009 Jul;85(1):120-9. ... The PYCR1 protein carries out the last step in this process by turning pyrroline-5-carboxylate into proline. The conversion ...
pyrroline-5-carboxylate reductase [EC:1.5.1.2]. All links Ontology (1) KEGG BRITE (1) Pathway (4) KEGG PATHWAY (4) Chemical ... R03293 Hydroxyproline + NADP+ ,=, L-1-Pyrroline-3-hydroxy-5-carboxylate + NADPH + H+. ...
Human pyrroline-5-carboxylate reductase (PYCR1) acts on Delta(1)-piperideine-6-carboxylate generating L-pipecolic acid. J ... Pyrroline-5-carboxylate reductase 1 promotes proliferation and inhibits apoptosis in non-small cell lung cancer. Oncol Lett. ... Mutations in PYCR2, Encoding Pyrroline-5-Carboxylate Reductase 2, Cause Microcephaly and Hypomyelination. Am J Hum Genet. 2015; ... Human mitochondrial pyrroline-5-carboxylate reductase 1 promotes invasiveness and impacts survival in breast cancers. ...
A second, simpler, redox neutral system was then constructed by combining the pyrroline-5-carboxylate reductase with a lysine-6 ... Firstly, a transaminase capable of lysine ε-deamination was coupled with a novel pyrroline-5-carboxylate reductase, yielding 60 ...
Pyrroline-5-carboxylate reductase. Model: iNRG857_1313. Reaction:. 1pyr5c_c + 2.0 h_c + nadph_c → nadp_c + pro__L_c ...
Pyrroline-5-carboxylate reductase. Model: iAM_Pf480. Reaction:. 1pyr5c_c + 2.0 h_c + nadph_c ⇌ nadp_c + pro__L_c ...
... pyrroline-5-carboxylate reductase (P ≤ 7.99 × 10-5), and RC.35692: Δ1-pyrroline-5-carboxylate synthetase (P , 10-200) ( ...
Pyrroline Carboxylate Reductases - Preferred Concept UI. M0018282. Scope note. A group of enzymes that catalyze the reduction ... Pyrroline Carboxylate Reductases Entry term(s). Carboxylate Reductases, Pyrroline Reductases, Pyrroline Carboxylate ... Pyrroline carboxylate reductases Entry term(s):. Carboxylate Reductases, Pyrroline. Reductases, Pyrroline Carboxylate. ... A group of enzymes that catalyze the reduction of 1-pyrroline carboxylate to proline in the presence of NAD(P)H. Includes both ...
Pyrroline Carboxylate Reductases. A group of enzymes that catalyze the reduction of 1-pyrroline carboxylate to proline in the ... Thin LayerPyrroline Carboxylate ReductasesLycopersicon esculentumD-Amino-Acid OxidasePlant RootsEnoxacinPyrrolesCaproates ... Carbon RadioisotopesCyclohexanecarboxylic AcidsAlkenesLucanthoneCarboxylic Ester HydrolasesPyrroline Carboxylate ReductasesD- ... former also reduces 1-piperidine-2-carboxylate to pipecolate and the latter also reduces 1-pyrroline-3-hydroxy-5-carboxylate to ...
Pyrroline-5-carboxylate reductase. 95.08%. PM0083594. 9. A0A6S6I601. Glucose-1-phosphate thymidylyltransferase. 95.10%. ... Peptide methionine sulfoxide reductase MsrA. 97.53%. PM0083584. 118. A0A6M2Y3Z4. Orotidine 5-phosphate decarboxylase. 97.56%. ...
Pyrroline Carboxylate Reductases 9% * Metabolome 9% * Lipids 9% * Biomarkers 9% * Thiazolidines 9% ...
pyrroline-5-carboxylate reductase 64, 318. DVU2336. carboxyl-terminal protease 234, 341. ...
pyrroline-5-carboxylate reductase (RefSeq). 66, 409. BSU23950. yqjA. hypothetical protein (RefSeq). 67, 319. ... 2-succinyl-5-enolpyruvyl-6-hydroxy-3- cyclohexene-1-carboxylate synthase (RefSeq). 132, 319. ...
pyrroline-5-carboxylate reductase 2.... QARS. 2058. EPRS1. glutamyl-prolyl-tRNA synthetase 1 [.... ...
pyrroline-5-carboxylate reductase 1 HGNC id 9721 *FLASH GENE. *DNA. *RNA ...
... γ-glutamyl phosphate reductase), and Pro3p (Δ1-pyrroline-5-carboxylate (P5C) reductase) [6][7]. Proline is also synthesized ... 1-pyrroline-5-carboxylate reductase. J Bacteriol 174(11): 3782-3788. doi: 10.1128/jb.174.15.5176b.1992 ... Four permeases import proline and the toxic proline analogue azetidine-2-carboxylate into yeast. Yeast 21(3): 193-199. doi: ... maintains yeast replicative lifespan by regulating ribonucleotide reductase 1 (RNR1) gene transcription. Biochem Biophys Res ...
pyrroline-5-carboxylate reductase complex GO:1902792 * procollagen-proline 4-dioxygenase complex ...
GO:0004735; Molecular function: pyrroline-5-carboxylate reductase activity. GO:0006561; Biological process: proline ... RHEA:14109: L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADPH EC 1.5.1.2 ... RHEA:14105: L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) + NADH EC 1.5.1.2 ... Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.. ...
Disease variants of human ?-pyrroline-5-carboxylate reductase 2 (PYCR2). Archives of biochemistry and biophysics 2021 3 703 ...
pyrroline-5-carboxylate reductase 1 [S.... RAP1GAP. 5909. RAP1GAP. RAP1 GTPase activating protein [Source.... ...
Funciton: Gamma-glutamyl phosphate reductase (EC 1.2.1.41) Locus tag: LAR_0333. Name: proI. Funciton: Pyrroline-5-carboxylate ...
pyrroline-5-carboxylate reductase family, member 2. Gene symbol. PYCR2. Other names/aliases. P5CR2. ...
... γ-glutamyl phosphate reductase (ProA), and Δ1-pyrroline-5-carboxylate reductase (ProI) increased significantly upon butanol ... and through catabolic route of proline by Δ1-pyrroline-5-carboxylate dehydrogenase (PutC or RocA) [30] (Fig. 3A). Glutamate ... the analysis prominently revealed the significant upregulation of Δ1-pyrroline-5-carboxylate dehydrogenase (RocA or PutC; EC ... γ-glutamyl kinase/γ-glutamyl phosphate reductase, for improved osmotic tolerance of Escherichia coli transformants. FEMS ...
Pyrroline-5-carboxylate reductase dimerisation [Interproscan].","protein_coding" "KNA49511","VCV51_030312","Vibrio cholerae "," ... ","3-oxoacyl-[acyl-carrier-protein] reductase FabG [Ensembl]. Enoyl-(Acyl carrier protein) reductase [Interproscan].","protein_ ... ","UDP-N-acetylenolpyruvoylglucosamine reductase [Ensembl]. FAD binding domain, UDP-N-acetylenolpyruvoylglucosamine reductase [ ... ","4-hydroxyphenylacetate 3-monooxygenase reductase component [Ensembl]. Flavin reductase like domain [Interproscan].","protein ...
Human Pyrroline-5-carboxylate reductase 2 (PYCR2) ELISA Kit $339.00. - $24,569.00. Tips for Abbkine antibodies. 1.The species ...
One such gene, proC, codes for pyrroline-5-carboxylate reductase [33] and was reported as essential in E. coli, Mycobacterium ...
Expression of P5C reductase (P5CR) was indispensable for embryo development but surprisingly not needed for pollen or egg cell ... In contrast to previous reports, we found that pyrroline-5-carboxylate (P5C) synthetase 2 (P5CS2) is not essential for sexual ... Szoke A, Miao GH, Hong Z, Verma DP: Subcellular location of δ1-pyrroline-5-carboxylate reductase in root/nodule and leaf of ... Hua XJ, Van de Cotte B, Van Montagu M, Verbruggen N: Developmental regulation of pyrroline-5-carboxylate reductase gene ...
  • In the budding yeast Saccharomyces cerevisiae , the synthesis of proline from glutamate in the cytoplasm is catalyzed by three enzymes: Pro1p (γ-glutamyl kinase), Pro2p (γ-glutamyl phosphate reductase), and Pro3p (Δ 1 -pyrroline-5-carboxylate (P5C) reductase) [6] [7] . (microbialcell.com)
  • This gene is a member of the aldehyde dehydrogenase family and encodes a bifunctional ATP- and NADPH-dependent mitochondrial enzyme with both gamma-glutamyl kinase and gamma-glutamyl phosphate reductase activities. (anticorps-enligne.fr)
  • In enzymology, a pyrroline-5-carboxylate reductase (EC 1.5.1.2) is an enzyme that catalyzes the chemical reaction L-proline + NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } 1-pyrroline-5-carboxylate + NAD(P)H + H+ The 3 substrates of this enzyme are L-proline, NAD+, and NADP+, whereas its 4 products are 1-pyrroline-5-carboxylate, NADH, NADPH, and H+. (wikipedia.org)
  • Other names in common use include proline oxidase, L-proline oxidase, 1-pyrroline-5-carboxylate reductase, NADPH-L-Delta1-pyrroline carboxylic acid reductase, and L-proline-NAD(P)+ 5-oxidoreductase. (wikipedia.org)
  • PYCR catalyzes an NADPH dependent reaction of pyrroline-5-carboxylate (P5C) into proline. (jcancer.org)
  • A second, simpler, redox neutral system was then constructed by combining the pyrroline-5-carboxylate reductase with a lysine-6-dehydrogenase. (rsc.org)
  • dehydrogenase/reductase 1 [Source:HGNC. (gsea-msigdb.org)
  • Expression of P5C reductase (P5CR) was indispensable for embryo development but surprisingly not needed for pollen or egg cell fertility. (biomedcentral.com)
  • In plants, glutamate is converted to proline in the cytosol and potentially in plastids by the sequential reactions of pyrroline-5-carboxylate (P5C) synthetase (P5CS) and P5C reductase (P5CR) [ 1 ]. (biomedcentral.com)
  • Delta 1-pyrroline-5-carboxylate reductase, catalyzes the final step in proline biosynthesis from glutamate and ornithine.In situ hybridization indicated that under normal growth conditions, the highest concentration of P5CR transcripts occurs in the cortical parenchyma, phloem, vascular cambium and pith parenchyma in the vicinity of the protoxylem. (gifu-u.ac.jp)
  • The P5CS gene codes for a delta¹-pyrroline-5-carboxylate. (embrapa.br)
  • Pyrroline-5-carboxylate reductase (PYCR) is a proline biosynthetic enzyme that catalyzes the NAD(P)H-dependent reduction of Δ-pyrroline-5-carboxylate (P5C) to proline. (anl.gov)
  • Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. (expasy.org)
  • The encoded protein catalyzes the reduction of glutamate to delta1-pyrroline-5-carboxylate, a critical step in the de novo biosynthesis of proline, ornithine and arginine. (anticorps-enligne.fr)
  • The PYCR1 protein carries out the last step in this process by turning pyrroline-5-carboxylate into proline. (medlineplus.gov)
  • Pyrroline-5-carboxylate reductase 1 (PYCR1) plays an important role in tumor development. (jcancer.org)
  • The former also reduces 1-piperidine-2-carboxylate to pipecolate and the latter also reduces 1-pyrroline-3-hydroxy-5-carboxylate to hydroxyproline. (bvsalud.org)
  • In contrast to previous reports, we found that pyrroline-5-carboxylate (P5C) synthetase 2 (P5CS2) is not essential for sexual reproduction although p5cs2 mutant plants were retarded in vegetative development and displayed reduced fertility under long-day conditions. (biomedcentral.com)
  • Mutation in pyrroline-5-carboxylate reductase 1 gene in families with cutis laxa type 2. (medlineplus.gov)
  • pyrroline-5-carboxylate reductase 2 (PYCR2). (cdc.gov)
  • A group of enzymes that catalyze the reduction of 1-pyrroline carboxylate to proline in the presence of NAD(P)H. Includes both the 2-oxidoreductase (EC 1.5.1.1) and the 5-oxidoreductase (EC 1.5.1.2). (bvsalud.org)
  • Belongs to the pyrroline-5-carboxylate reductase family. (expasy.org)
  • Dynamic adaptation of cytosolic thioredoxin reductase levels during metabolic changes results in improved H2 O2 handling and explains previously observed differences between cell types. (biomed.news)
  • Pyrroline-5-carboxylate reductase (PYCR) is mainly located in the mitochondria and plays an important role in the biosynthesis of proline [ 10 , 11 ]. (jcancer.org)
  • Firstly, a transaminase capable of lysine ε-deamination was coupled with a novel pyrroline-5-carboxylate reductase, yielding 60% conversion at the 50 mM scale with free enzymes and in situ recycling of the cofactor. (rsc.org)
  • Functional Impact of a Cancer-Related Variant in Human Δ-Pyrroline-5-Carboxylate Reductase 1. (anl.gov)
  • Molecular function: pyrroline-5-carboxylate reductase activity. (expasy.org)
  • A second, simpler, redox neutral system was then constructed by combining the pyrroline-5-carboxylate reductase with a lysine-6-dehydrogenase. (rsc.org)
  • Four mitochondrial enzymes are responsible for 4-hydroxproline (4-Hyp) breakdown: hydroxyproline oxidase (HPOX), Δ1-pyrroline-5-carboxylate dehydrogenase (1P5CDH), aspartate aminotransferase (AspAT), and 4-hydroxy-2-oxoglutarate aldolase (HOGA). (blogspot.com)
  • Hyperprolinemia type II is caused by variants in the ALDH4A1 gene, which provides instructions for producing the enzyme pyrroline-5-carboxylate dehydrogenase. (nih.gov)
  • Variants in either the PRODH or ALDH4A1 gene can cause a reduction in proline dehydrogenase or pyrroline-5-carboxylate dehydrogenase function and a decrease in the breakdown of proline. (nih.gov)
  • Characterization of a novel class of glyoxylate reductase belonging to the β-hydroxyacid dehydrogenase family in Acetobacter aceti. (ritsumei.ac.jp)
  • This gene is a member of the aldehyde dehydrogenase family and encodes a bifunctional ATP- and NADPH-dependent mitochondrial enzyme with both gamma-glutamyl kinase and gamma-glutamyl phosphate reductase activities. (nih.gov)
  • A pro3 ure2 strain expressing a PGK1 promoter-driven PUT2 allele encoding Delta(1)-pyrroline-5-carboxylate dehydrogenase lacking a mitochondrial targeting sequence produced significant cytoplasmic activity, accumulated twice as much intracellular glutamate, and produced twice as much cell mass as the parent when grown anaerobically on limiting arginine as sole nitrogen source. (oregonstate.edu)
  • Delta 1-pyrroline-5-carboxylate reductase, catalyzes the final step in proline biosynthesis from glutamate and ornithine.In situ hybridization indicated that under normal growth conditions, the highest concentration of P5CR transcripts occurs in the cortical parenchyma, phloem, vascular cambium and pith parenchyma in the vicinity of the protoxylem. (gifu-u.ac.jp)
  • We show that in hypoxic conditions, mitochondrial pyrroline 5-carboxylate reductase 1 (PYCR1) activity is increased, oxidizing NADH with the synthesis of proline as a by-product. (birmingham.ac.uk)
  • This enzyme helps to break down the pyrroline-5-carboxylate produced in the previous reaction, converting it to the amino acid glutamate. (nih.gov)
  • The encoded protein catalyzes the reduction of glutamate to delta1-pyrroline-5-carboxylate, a critical step in the de novo biosynthesis of proline, ornithine and arginine. (nih.gov)
  • Properties of gamma-glutamyl phosphate reductase and 1-pyrroline-5-carboxylate reductase. (nih.gov)
  • A group of enzymes that catalyze the reduction of 1-pyrroline carboxylate to proline in the presence of NAD (P)H. Includes both the 2-oxidoreductase (EC 1.5.1.1) and the 5-oxidoreductase (EC 1.5.1.2). (bvsalud.org)
  • 1. Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1. (nih.gov)
  • 10. Structure, biochemistry, and gene expression patterns of the proline biosynthetic enzyme pyrroline-5-carboxylate reductase (PYCR), an emerging cancer therapy target. (nih.gov)
  • This enzyme begins the process of breaking down proline by starting the reaction that converts proline to pyrroline-5-carboxylate. (nih.gov)
  • Glyoxylate is metabolized either to glycolate by glyoxylate reductase (GR) in the mitochondria and cytoplasm or to glycine by peroxisomal alanine-glyoxylate aminotransferase (AGT). (blogspot.com)
  • 14478 3-oxoacyl-[acyl-carrier protein] reductase fabG BBZA01000001 CDS ARMA_0014 complement(14430. (go.jp)
  • 19. Purification, characterization, and crystallization of human pyrroline-5-carboxylate reductase. (nih.gov)
  • 9. Kinetics of human pyrroline-5-carboxylate reductase in L-thioproline metabolism. (nih.gov)
  • Hyperprolinemia type II results in proline levels in the blood between 10 and 15 times higher than normal, and high levels of a related compound called pyrroline-5-carboxylate. (nih.gov)
  • 20. Partial purification and some properties of delta1-pyrroline-5-carboxylate reductase from Escherichia coli. (nih.gov)