Results 191 to 200 of about 46,423 (228)
Recent advances in nonprotein amino acids: insights from function to biosynthesis. [PDF]
J Anim Sci BiotechnolZou Y +9 more
europepmc +1 more source
The role of abnormal amino acid metabolism in the occurrence and development of tumors. [PDF]
Front OncolZhang Y, Chen H.
europepmc +1 more source
Biochemical characterization of proline dehydrogenase in Arabidopsis mitochondria [PDF]
FEBS Journal, 2014 Proline has multiple functions in plants. Besides being a building block for protein biosynthesis proline plays a central role in the plant stress response and in further cellular processes. Here, we report an analysis on the integration of proline dehydrogenase (ProDH) into mitochondrial metabolism in Arabidopsis thaliana.
Hans-Peter Braun, Arnould Savouré
exaly +3 more sources
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Mechanism-based inhibition of proline dehydrogenase by proline analogues
BBA - Proteins and Proteomics, 1993The inactivation of proline dehydrogenase by several L-Pro analogues was investigated with the aim to block the essential metabolic pathway of tsetse flies allowing the degradation of L-Pro to L-Glu. In vitro studies on rat liver mitochondria showed that only 4-methylene-L-proline was able to inactivate proline dehydrogenase.
Jean-François Biellmann +2 more
exaly +3 more sources
Applied Biochemistry and Biotechnology, 2022
D-proline and N-boc-5-hydroxy-L-proline are key chiral intermediates in the production of eletriptan and saxagliptin, respectively. An efficient proline racemase-proline dehydrogenase cascade was developed for the enantioselective production of D-proline.
Hui Lin, Shiwen Xia
exaly +3 more sources
D-proline and N-boc-5-hydroxy-L-proline are key chiral intermediates in the production of eletriptan and saxagliptin, respectively. An efficient proline racemase-proline dehydrogenase cascade was developed for the enantioselective production of D-proline.
Hui Lin, Shiwen Xia
exaly +3 more sources
British Journal of Haematology, 2023
SummaryAmino acids in the bone marrow microenvironment (BMME) are a critical factor for multiple myeloma (MM) progression. Here, we have determined that proline is elevated in BMME of MM patients and links to poor prognosis in MM. Moreover, exogenous proline regulates MM cell proliferation and drug resistance.
Jingyu Zhang +12 more
openaire +2 more sources
SummaryAmino acids in the bone marrow microenvironment (BMME) are a critical factor for multiple myeloma (MM) progression. Here, we have determined that proline is elevated in BMME of MM patients and links to poor prognosis in MM. Moreover, exogenous proline regulates MM cell proliferation and drug resistance.
Jingyu Zhang +12 more
openaire +2 more sources
Proline Dehydrogenase — A New Enzyme for Pollen
Biochemie Und Physiologie Der Pflanzen, 1976Summary Using quantitative biochemical procedures, the distribution of proline dehydrogenase in pollengrains and pollen tubes of Crotalaria juncea L. is demonstrated for the first time. Increased accumulation of proline in the dormant pollen and its subsequent decrease in the germinating phase along with the increased activity of proline ...
C P Malik, M B Singh
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Studies on the inner mitochondrial membrane localization of proline dehydrogenase
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 19771. The site of proline dehydrogenase (EC 1.5.99.-) activity in blowfly (Phormia regina) flight muscle mitochondria has been investigated employing the inner membrane-impermeable Fe(CN)63-as electron acceptor. Antimycin had no inhibitory effect on ferricyanide reduction due to proline dehydrogenase activity. Ferricyanide reductase activity due to inside
E, Balboni, R I, Hecht
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BioFactors, 2016
AbstractProlidase is a cytosolic imidodipeptidase that specifically splits imidodipeptides with C‐terminal proline or hydroxyproline. The enzyme plays an important role in the recycling of proline from imidodipeptides for resynthesis of collagen and other proline‐containing proteins.
Ilona, Zareba, Jerzy, Palka
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AbstractProlidase is a cytosolic imidodipeptidase that specifically splits imidodipeptides with C‐terminal proline or hydroxyproline. The enzyme plays an important role in the recycling of proline from imidodipeptides for resynthesis of collagen and other proline‐containing proteins.
Ilona, Zareba, Jerzy, Palka
openaire +2 more sources
Allohydroxy-d-proline dehydrogenase
Archives of Microbiology, 1977Growth of Pseudomonas aeruginosa PA01 on isomers of hydroxyproline induced the synthesis of an allohydroxy-D-proline dehydrogenase. The enzyme resembled the D-alanine dehydrogenase of this organism in its association with the particulate fraction and its linkage to oxygen through a cytochrome-containing respiratory chain, but differed from this and ...
A J, Bater, W A, Venables, S, Thomas
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