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beta-glutamylphosphate reductase
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dehydrogenase, glutamate semialdehyde
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gamma glutamyl semialdehyde dehydrogenase
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gamma-glutamyl phosphate reductase
glutamate 5-semialdehyde dehydrogenase
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glutamate semialdehyde dehydrogenase
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Glutamate-5-semialdehyde dehydrogenase
glutamate-gamma-semialdehyde dehydrogenase
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glutamic gamma-semialdehyde dehydrogenase
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glutamic-gamma-semialdehyde dehydrogenase
Glutamyl-gamma-semialdehyde dehydrogenase
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GSA dehydrogenase
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pyrroline 5-carboxylate dehydrogenase
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pyrroline-5-carboxylate synthase
pyrroline-5-carboxylate synthetase
reductase, gamma-glutamyl phosphate
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Aldh18a1
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gamma-glutamyl phosphate reductase
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gamma-glutamyl phosphate reductase
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gamma-glutamyl phosphate reductase
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gamma-glutamyl phosphate reductase
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gamma-glutamyl phosphate reductase
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gamma-glutamyl phosphate reductase
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gamma-glutamyl phosphate reductase
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gamma-GPR
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Glutamate-5-semialdehyde dehydrogenase
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Glutamate-5-semialdehyde dehydrogenase
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Glutamate-5-semialdehyde dehydrogenase
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glutamic-gamma-semialdehyde dehydrogenase
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glutamic-gamma-semialdehyde dehydrogenase
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glutamic-gamma-semialdehyde dehydrogenase
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glutamic-gamma-semialdehyde dehydrogenase
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P5CS
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
P5CS
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
P5CS
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
P5CS
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
pyrroline-5-carboxylate synthase
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
pyrroline-5-carboxylate synthase
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
pyrroline-5-carboxylate synthase
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
pyrroline-5-carboxylate synthase
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
pyrroline-5-carboxylate synthetase
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
pyrroline-5-carboxylate synthetase
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
pyrroline-5-carboxylate synthetase
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
pyrroline-5-carboxylate synthetase
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
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acetaldehyde + NAD+ + H2O
acetate + NADH + H+
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?
glutamate gamma-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
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?
L-5-glutamyl phosphate + NADPH
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L-glutamate 5-semialdehyde + phosphate + NAD+
L-glutamyl 5-phosphate + NADH + H+
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?
L-glutamate 5-semialdehyde + phosphate + NADP+
gamma-glutamyl phosphate + NADPH + H+
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH + H+
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?
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
additional information
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ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
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L-5-glutamyl phosphate + NADPH
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second enzyme in pathway of proline biosynthesis
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?
L-5-glutamyl phosphate + NADPH
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gamma-glutamyl kinase (the first enzyme of proline biosynthetic pathway) and gamma-glutamyl phosphate reductase (second enzyme) form a complex which stabilizes the labile intermediate i.e. gamma-glutamyl phosphate
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?
L-glutamate 5-semialdehyde + phosphate + NADP+
gamma-glutamyl phosphate + NADPH + H+
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r
L-glutamate 5-semialdehyde + phosphate + NADP+
gamma-glutamyl phosphate + NADPH + H+
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L-glutamate 5-semialdehyde spontaneously cyclizes to pyrroline 5-carboxylate. The product gamma-glutamyl phosphate decomposes to pyrrolidone 5-carboxylate.
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r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH
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?
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH
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r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH
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arsenate can replace phosphate
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r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH
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divalent anions can substitute for phosphate
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r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH
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L-glutamate 5-semialdehyde is in equilibrium with delta'-pyrroline-5-carboxylate
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r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH
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arsenate can replace phosphate
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r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH
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?
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH
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L-glutamate 5-semialdehyde spontaneously cyclizes to delta-1-pyrroline-5-carboxylic acid
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?
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH
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?
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
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?
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
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r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
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r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
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r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
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?
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
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r
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Agenesis of Corpus Callosum
Clinical and biochemical features guiding the diagnostics in neurometabolic cutis laxa.
Agenesis of Corpus Callosum
Extending the ALDH18A1 clinical spectrum to severe autosomal recessive fetal cutis laxa with corpus callosum agenesis.
Alopecia
Unique presentation of cutis laxa with Leigh-like syndrome due to ECHS1 deficiency.
Alzheimer Disease
Association of variants within APOE, SORL1, RUNX1, BACE1 and ALDH18A1 with dementia in Alzheimer's disease in subjects with Down syndrome.
Cataract
?1 -Pyrroline-5-carboxylate synthetase deficiency: An emergent multifaceted urea cycle-related disorder.
Cataract
A missense mutation in ALDH18A1, encoding Delta1-pyrroline-5-carboxylate synthase (P5CS), causes an autosomal recessive neurocutaneous syndrome.
Cerebellar Ataxia
Novel mutations in the ALDH18A1 gene in complicated hereditary spastic paraplegia with cerebellar ataxia and cognitive impairment.
Congenital Disorders of Glycosylation
Unique presentation of cutis laxa with Leigh-like syndrome due to ECHS1 deficiency.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Unique presentation of cutis laxa with Leigh-like syndrome due to ECHS1 deficiency.
Cryptorchidism
Cutis laxa, fat pads and retinopathy due to ALDH18A1 mutation and review of the literature.
Cutis Laxa
?1 -Pyrroline-5-carboxylate synthetase deficiency: An emergent multifaceted urea cycle-related disorder.
Cutis Laxa
Autosomal dominant cutis laxa with progeroid features due to a novel, de novo mutation in ALDH18A1.
Cutis Laxa
Compound heterozygous mutations in two different domains of ALDH18A1 do not affect the amino acid levels in a patient with hereditary spastic paraplegia.
Cutis Laxa
Cutis laxa, fat pads and retinopathy due to ALDH18A1 mutation and review of the literature.
Cutis Laxa
Expanding the Spectrum of Neurological Manifestations in Cutis Laxa, Autosomal Recessive, Type IIIA.
Cutis Laxa
Extending the ALDH18A1 clinical spectrum to severe autosomal recessive fetal cutis laxa with corpus callosum agenesis.
Cutis Laxa
Further expansion of the phenotypic spectrum associated with mutations in ALDH18A1, encoding ?(1) -pyrroline-5-carboxylate synthase (P5CS).
Cutis Laxa
Genetic analysis of Pycr1 and Pycr2 in mice.
Cutis Laxa
Imaging in cutis laxa syndrome caused by a dominant negative ALDH18A1 mutation, with hypotheses for intracranial vascular tortuosity and wide perivascular spaces.
Cutis Laxa
Loss of ALDH18A1 function is associated with a cellular lipid droplet phenotype suggesting a link between autosomal recessive cutis laxa type 3A and Warburg Micro syndrome.
Cutis Laxa
Predominant Motor Delay as a Major Presenting Clinical Sign in Cutis Laxa- Report of a Case with Review of Literature.
Cutis Laxa
Recurrent De Novo Mutations Affecting Residue Arg138 of Pyrroline-5-Carboxylate Synthase Cause a Progeroid Form of Autosomal-Dominant Cutis Laxa.
Cutis Laxa
Severe congenital cutis laxa with cardiovascular manifestations due to homozygous deletions in ALDH18A1.
Cutis Laxa
SPG9A with the new occurrence of an ALDH18A1 mutation in a CMT1A family with PMP22 duplication: case report.
Cutis Laxa
Unique presentation of cutis laxa with Leigh-like syndrome due to ECHS1 deficiency.
Dementia
Association of variants within APOE, SORL1, RUNX1, BACE1 and ALDH18A1 with dementia in Alzheimer's disease in subjects with Down syndrome.
Down Syndrome
Association of variants within APOE, SORL1, RUNX1, BACE1 and ALDH18A1 with dementia in Alzheimer's disease in subjects with Down syndrome.
glutamate-5-semialdehyde dehydrogenase deficiency
Understanding pyrroline-5-carboxylate synthetase deficiency: clinical, molecular, functional, and expression studies, structure-based analysis, and novel therapy with arginine.
glutamate-5-semialdehyde dehydrogenase deficiency
Unique presentation of cutis laxa with Leigh-like syndrome due to ECHS1 deficiency.
Hearing Loss
Glutamate-related gene expression changes with age in the mouse auditory midbrain.
HIV Infections
Reconnaissance of the candidate genes involved in the pathogenesis of human immunodeficiency virus and targeted by antiretroviral therapy.
Hyperargininemia
Neurophysiological characteristics in argininemia: a case report.
Infections
Identification of ALDH4 as a p53-inducible gene and its protective role in cellular stresses.
Joint Dislocations
A missense mutation in ALDH18A1, encoding Delta1-pyrroline-5-carboxylate synthase (P5CS), causes an autosomal recessive neurocutaneous syndrome.
Joint Instability
?1 -Pyrroline-5-carboxylate synthetase deficiency: An emergent multifaceted urea cycle-related disorder.
Liver Neoplasms
Metabolic pathway analyses identify proline biosynthesis pathway as a promoter of liver tumorigenesis.
Megalencephaly
Unique presentation of cutis laxa with Leigh-like syndrome due to ECHS1 deficiency.
Melanoma
Disruption of Proline Synthesis in Melanoma Inhibits Protein Production Mediated by the GCN2 Pathway.
Melanoma
Salubrinal in Combination With 4E1RCat Synergistically Impairs Melanoma Development by Disrupting the Protein Synthetic Machinery.
Menkes Kinky Hair Syndrome
Unique presentation of cutis laxa with Leigh-like syndrome due to ECHS1 deficiency.
Metabolic Diseases
Pyrroline-5-carboxylate synthase and proline biosynthesis: from osmotolerance to rare metabolic disease.
Microcephaly
Cutis laxa, fat pads and retinopathy due to ALDH18A1 mutation and review of the literature.
Myopia
Novel Myopia Genes and Pathways Identified From Syndromic Forms of Myopia.
Neoplasms
Disruption of Proline Synthesis in Melanoma Inhibits Protein Production Mediated by the GCN2 Pathway.
Neoplasms
Inhibition of the ALDH18A1-MYCN positive feedback loop attenuates MYCN-amplified neuroblastoma growth.
Neoplasms
Proline metabolism in cancer.
Neurocutaneous Syndromes
?1 -Pyrroline-5-carboxylate synthetase deficiency: An emergent multifaceted urea cycle-related disorder.
Neurocutaneous Syndromes
A missense mutation in ALDH18A1, encoding Delta1-pyrroline-5-carboxylate synthase (P5CS), causes an autosomal recessive neurocutaneous syndrome.
Neurocutaneous Syndromes
Alteration of ornithine metabolism leads to dominant and recessive hereditary spastic paraplegia.
Paraplegia
ALDH18A1 gene mutations cause dominant spastic paraplegia SPG9: loss of function effect and plausibility of a dominant negative mechanism.
Paraplegia
Autosomal dominant SPG9: intrafamilial variability and onset during pregnancy.
Paraplegia
Compound heterozygous mutations in two different domains of ALDH18A1 do not affect the amino acid levels in a patient with hereditary spastic paraplegia.
Paraplegia
Novel Compound Missense and Intronic Splicing Mutation in ALDH18A1 Causes Autosomal Recessive Spastic Paraplegia.
Paraplegia
P5CS expression study in a new family with ALDH18A1-associated hereditary spastic paraplegia SPG9.
Paraplegia
Reply: ALDH18A1 gene mutations cause dominant spastic paraplegia SPG9: loss of function effect and plausibility of a dominant negative mechanism.
Progeria
Cutis laxa, fat pads and retinopathy due to ALDH18A1 mutation and review of the literature.
Retinitis Pigmentosa
Cutis laxa, fat pads and retinopathy due to ALDH18A1 mutation and review of the literature.
Scoliosis
Unique presentation of cutis laxa with Leigh-like syndrome due to ECHS1 deficiency.
Spastic Paraplegia, Hereditary
Alteration of ornithine metabolism leads to dominant and recessive hereditary spastic paraplegia.
Spastic Paraplegia, Hereditary
Compound heterozygous mutations in two different domains of ALDH18A1 do not affect the amino acid levels in a patient with hereditary spastic paraplegia.
Spastic Paraplegia, Hereditary
Novel Compound Missense and Intronic Splicing Mutation in ALDH18A1 Causes Autosomal Recessive Spastic Paraplegia.
Spastic Paraplegia, Hereditary
Novel mutations in the ALDH18A1 gene in complicated hereditary spastic paraplegia with cerebellar ataxia and cognitive impairment.
Spastic Paraplegia, Hereditary
Tremor as an early sign of hereditary spastic paraplegia due to mutations in ALDH18A1.
transaldolase deficiency
Unique presentation of cutis laxa with Leigh-like syndrome due to ECHS1 deficiency.
Tremor
Tremor as an early sign of hereditary spastic paraplegia due to mutations in ALDH18A1.
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Kramer, J.J.; Gooding, R.C.; Jones, M.E.
A radiochemical assay for a NADP+-specific gamma-glutamate semialdehyde dehydrogenase extracted from mitochondrial membrane of rat intestinal epithelial cells
Anal. Biochem.
168
380-386
1988
Rattus norvegicus
brenda
Kramer, J.J.; Henslee, J.G.; Wakabayashi, Y.; Jones, M.E.
Glutamate semialdehyde dehydrogenase
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
3
200-210
1983
Rattus norvegicus
-
brenda
Deutch, A.H.; Smith, C.J.; Rushlow, K.E.
Overproduction and purification of the three enzymes constituting the Escherichia coli proline biosynthetic pathway
Dev. Ind. Microbiol.
26
437-444
1985
Escherichia coli
-
brenda
Deutch, A.H.; Rushlow, K.E.; Smith, C.J.
Analysis of the Escherichia coli proBA locus by DNA and protein sequencing
Nucleic Acids Res.
12
6337-6355
1984
Escherichia coli
brenda
Mahan, M.J.; Csonka, L.N.
Genetic analysis of the proBA genes of Salmonella typhimurium: physical and genetic analyses of the cloned proB+ A+ genes of Escherichia coli and of a mutant allele that confers proline overproduction and enhanced osmotolerance
J. Bacteriol.
156
1249-1262
1983
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Hayzer, D.J.; Leisinger, T.
Proline biosynthesis in Escherichia coli. Kinetic and mechanistic properties of glutamate semialdehyde dehydrogenase
Biochim. Biophys. Acta
742
391-398
1983
Escherichia coli
brenda
Hayzer, D.J.; Leisinger, T.
Proline biosynthesis in Escherichia coli. Purification and characterisation of glutamate-semialdehyde dehydrogenase
Eur. J. Biochem.
121
561-565
1982
Escherichia coli, Pseudomonas aeruginosa
brenda
Hayzer, D.J.; Leisinger, T.
Proline biosynthesis in Escherichia coli. Stoichiometry and end-product identification of the reaction catalysed by glutamate semialdehyde dehydrogenase
Biochem. J.
197
269-274
1981
Escherichia coli
brenda
Hayzer, D.J.; Moses, V.
The enzymes of proline biosynthesis in Escherichia coli. Their molecular weights and the problem of enzyme aggregation
Biochem. J.
173
219-228
1978
Escherichia coli
brenda
Gamper, H.; Moses, V.
Enzyme organization in the proline biosynthetic pathway of Escherichia coli
Biochim. Biophys. Acta
354
75-87
1974
Escherichia coli
brenda
Baich, A.
The biosynthesis of proline in Escherichia coli: phosphate-dependent glutamate-semialdehyde dehydrogenase (NADP), the second enzyme in the pathway
Biochim. Biophys. Acta
244
129-134
1971
Escherichia coli, Escherichia coli 55-I
brenda
Garcia-Rios, M; Fujita, T.; Larosa, P.C.; Locy, R.D.; Clitero, J.M.; Bressan, R.A.; Csonka, L.N.
Cloning of a polycistronic cDNA from tomato encoding gamma-glutamyl kinase and gamma-glutamyl phosphate reductase
Proc. Natl. Acad. Sci. USA
94
8249-8254
1997
Solanum lycopersicum
brenda
Yaklichkin, S.Y.; Zimina, M.S.; Neumyvakin, L.V.
Proline biosynthesis gene proB of thermophilic Bacterium Thermus ruber: cloning, sequencing, and properties of encoded gamma-glutamylphosphate kinase
Mol. Biol.
33
628-635
1999
Meiothermus ruber
-
brenda
Louie, H.; Chan.V.L.
Cloning and characterization of the gamma-glutamylphosphate reductase gene of Campylobacter jejuni
Mol. Gen. Genet.
240
29-35
1993
Campylobacter jejuni, Campylobacter jejuni TGH9011
brenda
Meijer, P.J.; Lilius, G.; Holmberg, N.; Bulow, L
An artificial bifunctional enzyme, gamma-glutamyl kinase/gamma-glutamyl phosphate reductase, improves NaCl tolerance when expressed in Escherichia Coli
Biotechnol. Lett.
18
1133-1138
1996
Escherichia coli
-
brenda
Page, R.; Nelson, M.S.; von Delft, F.; Elsliger, M.a.; Canaves, J.M.; Brinen, L.S.; Dai, X.; Deacon, A.M.; Floyd, R.; Godzik, A.; Grittini, C.; Grzechnik, S.K.; Jaroszewski, L.; Klock, H.E.; Koesema, E.; Kovarik, J.S.; Kreusch, A.; Kuhn, P.; Lesley, S.A.; McMullan, D.; McPhillips, T.M.; Miller, M.D.; Morse, A.; Moy, K.; Ouyang, J.; Robb, A.; Rodrigues, K.; Schwarzenbacher, R.; Spraggon, G.; Stevens, R.C.; van den Bedem, H.; Velasquez, J.; Vincent, J.; Wang, X.; West, B.; Wolf, G.; Hodgson, K.O.; Wooley, J.; Wilson, I.A.
Crystal structure of gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.0 A resolution
Proteins
54
157-161
2003
Thermotoga maritima (Q9WYC9), Thermotoga maritima
brenda
Takagi, H.; Takaoka, M.; Kawaguchi, A.; Kubo, Y.
Effect of L-proline on sake brewing and ethanol stress in Saccharomyces cerevisiae
Appl. Environ. Microbiol.
71
8656-8662
2005
Saccharomyces cerevisiae
brenda
Chen, M.; Cao, J.; Zheng, C.; Liu, Q.
Directed evolution of an artificial bifunctional enzyme, gamma-glutamyl kinase/gamma-glutamyl phosphate reductase, for improved osmotic tolerance of Escherichia coli transformants
FEMS Microbiol. Lett.
263
41-47
2006
Bacillus subtilis
brenda
Marchitti, S.A.; Deitrich, R.A.; Vasiliou, V.
Neurotoxicity and metabolism of the catecholamine-derived 3,4-dihydroxyphenylacetaldehyde and 3,4-dihydroxyphenylglycolaldehyde: the role of aldehyde dehydrogenase
Pharmacol. Rev.
59
125-150
2007
Homo sapiens
brenda
Alnouti, Y.; Klaassen, C.D.
Tissue distribution, ontogeny, and regulation of aldehyde dehydrogenase (Aldh) enzymes mRNA by prototypical microsomal enzyme inducers in mice
Toxicol. Sci.
101
51-64
2008
Mus musculus (Q9Z110)
brenda
Saum, S.H.; Mueller, V.
Salinity-dependent switching of osmolyte strategies in a moderately halophilic bacterium: glutamate induces proline biosynthesis in Halobacillus halophilus
J. Bacteriol.
189
6968-6975
2007
Halobacillus halophilus (A7Y114), Halobacillus halophilus
brenda
Hempel, J.; Kraut, A.; Wymore, T.
Gamma glutamyl semialdehyde dehydrogenase: Simulations on native and mutant forms support the importance of outer shell lysines
Chem. Biol. Interact.
178
75-78
2009
Thermus thermophilus
brenda
Gao, C.; Han, B.
Evolutionary and expression study of the aldehyde dehydrogenase (ALDH) gene superfamily in rice (Oryza sativa)
Gene
431
86-94
2009
Oryza sativa (Q941T1)
brenda
Turchetto-Zolet, A.C.; Margis-Pinheiro, M.; Margis, R.
The evolution of pyrroline-5-carboxylate synthase in plants: a key enzyme in proline synthesis
Mol. Genet. Genomics
281
87-97
2009
Pachira quinata (B1P5P3), Cedrela odorata (B1P5P4), Ceiba pentandra (B1P5P5), Ceiba pentandra (B1P5P6), Schizolobium parahyba (B1P5P7), Schizolobium parahyba (B1P5P8)
brenda