Results 151 to 160 of about 1,126 (165)
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Pyrroline-5-Carboxylate Reductase and Proline Oxidase Activity in the Neonatal Pig
The Journal of Nutrition, 1989Recent evidence suggests that proline is an indispensible amino acid in the diet of the young pig. A dietary requirement may relate to the activity and developmental changes of the enzymes that synthesize and degrade proline. The activity of pyrroline-5-carboxylate (P5C) reductase (EC 1.5.1.2), which catalyzes the final step in proline synthesis, and ...
S E, Samuels, K S, Acton, R O, Ball
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[128] Pyrroline-5-carboxylate reductase
1962Publisher Summary Pyrroline-5-carboxylate reductase has a wide distribution. It occurs in many mammalian tissues, particularly in liver, brain and testis, in the hepatopancreas of the terrestial slug, Ariolimax Californicus brachyphallus , and in the microorganisms Neurospora crassa, Escherichia coli, and Aerobacter aerogenes. The chapter presents
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Protein Expression and Purification, 2006
Pyrroline-5-carboxylate reductase (P5CR) plays an important role in the survival of Mycobacterium tuberculosis and is related to virulence of this pathogen. RT-PCR analysis indicated that proC, encoding P5CR, was expressed at the transcriptional level cultured in vitro.
Yanping, Yang +6 more
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Pyrroline-5-carboxylate reductase (P5CR) plays an important role in the survival of Mycobacterium tuberculosis and is related to virulence of this pathogen. RT-PCR analysis indicated that proC, encoding P5CR, was expressed at the transcriptional level cultured in vitro.
Yanping, Yang +6 more
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Journal of Inherited Metabolic Disease, 2014
AbstractWe have conducted biochemical studies with commercial available pyrroline‐5‐carboxylate (P5C) reductase (PYCR1) to investigate whether this enzyme plays a role in L‐lysine degradation. Our recent studies with antiquitin/ALDH7A1 deficient fibroblasts revealed an alternative genesis of L‐pipecolic acid, and we then hypothesized that PYCR1 was ...
Struys, E.A. +2 more
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AbstractWe have conducted biochemical studies with commercial available pyrroline‐5‐carboxylate (P5C) reductase (PYCR1) to investigate whether this enzyme plays a role in L‐lysine degradation. Our recent studies with antiquitin/ALDH7A1 deficient fibroblasts revealed an alternative genesis of L‐pipecolic acid, and we then hypothesized that PYCR1 was ...
Struys, E.A. +2 more
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Synthesis and Evaluation of Effective Inhibitors of Plant δ1-Pyrroline-5-carboxylate Reductase
Journal of Agricultural and Food Chemistry, 2013Analogues of previously studied phenyl-substituted aminomethylene-bisphosphonic acids were synthesized and evaluated as inhibitors of Arabidopsis thaliana δ(1)-pyrroline-5-carboxylate reductase. With the aim of improving their effectiveness, two main modifications were introduced into the inhibitory scaffold: the aminomethylenebisphosphonic moiety was ...
FORLANI, Giuseppe +6 more
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Purification and characterization of pyrroline-5-carboxylate reductase from bovine retina
Biochimica et Biophysica Acta (BBA) - General Subjects, 1982Bovine retinal pyrroline-5-carboxylate reductase (L-proline: NAD(P)+ 5-oxidoreductase, EC 1.5.1.2) was purified 180-fold from crude extract, using affinity chromatography with 2',5'-ADP Sepharose 4B. The purified enzyme utilized either NADH or NADPH as the coenzyme.
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Biochemical Genetics, 2001
The first insect cDNA and genomic sequences encoding pyrroline 5-carboxylate reductase (EC 1.5.1.2) have been isolated from Drosophila melanogaster. The cDNA sequence was identified by interspecies complementation of an E. coli proline auxotroph and encodes a protein 280 amino acids in length with 25-41% identity to pyrroline 5-carboxylate reductases ...
S R, Misener, V K, Walker
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The first insect cDNA and genomic sequences encoding pyrroline 5-carboxylate reductase (EC 1.5.1.2) have been isolated from Drosophila melanogaster. The cDNA sequence was identified by interspecies complementation of an E. coli proline auxotroph and encodes a protein 280 amino acids in length with 25-41% identity to pyrroline 5-carboxylate reductases ...
S R, Misener, V K, Walker
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Stimulation of the hexose monophosphate pathway by pyrroline-5-carboxylate reductase in the lens
Experimental Eye Research, 1985Addition of pyrroline-5-carboxylate (P5C) or its precursors to rat lenses cultured for 24 hr in TC-199 medium containing 14C-glucose results in an apparent concentration-dependent increase in hexose monophosphate-pentose (HMP) pathway activity. Addition of proline, the reduction product of P5C, did not result in an increase, suggesting that stimulation
T, Shiono, P F, Kador, J H, Kinoshita
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Archives of Biochemistry and Biophysics, 1991
Electrophoretic evidence was obtained for two forms of pyrroline-5-carboxylate reductase (P5CR) in soybean nodules. One form was purified over 2300-fold. The apparent sizes of the polypeptides comprising the pyrroline-5-carboxylate reductases from soybean cytosol (29,700) and Escherichia coli (28,000) were consistent with those predicted from the ...
O P, Chilson +2 more
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Electrophoretic evidence was obtained for two forms of pyrroline-5-carboxylate reductase (P5CR) in soybean nodules. One form was purified over 2300-fold. The apparent sizes of the polypeptides comprising the pyrroline-5-carboxylate reductases from soybean cytosol (29,700) and Escherichia coli (28,000) were consistent with those predicted from the ...
O P, Chilson +2 more
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1971
Publisher Summary This chapter focuses on Δ-Pyrroline-5-carboxylate Reductase (Calf Liver) (Reduction of Al-Pyrroline-5-carboxylate to Proline). Enzyme activity is measured in soluble preparations by the decrease in absorbancy at 340 mμ. In conformity with the proposed international unit, enzyme activity may be defined as that amount which reduces 1 ...
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Publisher Summary This chapter focuses on Δ-Pyrroline-5-carboxylate Reductase (Calf Liver) (Reduction of Al-Pyrroline-5-carboxylate to Proline). Enzyme activity is measured in soluble preparations by the decrease in absorbancy at 340 mμ. In conformity with the proposed international unit, enzyme activity may be defined as that amount which reduces 1 ...
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