Cited by 269Amino Acid Enzymes and MetabolismBiochemical and Molecular ResearchFolate and B Vitamins Research

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Enzymes of serine metabolism in normal, developing and neoplastic rat tissues

Snell, Keith·1984·Advances in Enzyme Regulation

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Abstract

1.|The cellular pattern of serine metabolism was conceptualized into four main areas of metabolic sequences: the biosynthesis of serine from intermediates of the glycolytic pathway (the so-called “phosphorylated pathway”); and alternative pathways of serine utilization initiated by serine dehydratase, serine aminotransferase and serine hydroxymethyltransferase. 2.|The known regulatory and adaptive properties of the enzymes involved in these pathways were reviewed in detail and key enzymes associated with each pathway (phosphoserine aminotransferase, serine dehydratase, serine aminotransferase, and serine hydroxymethyltransferase, respectively) were selected for further investigation. 3.|Tissue distribution studies in the rat revealed that whereas serine dehydratase and serine aminotransferase activities were largely confined to the liver, phosphoserine aminotransferase and serine hydroxymethyltransferase activities were more broadly distributed. In particular in tissues with a high rate of cell turnover, phosphoserine aminotransferase and serine hydroxymethyltransferase activities were coordinately increased. An increase in serine hydroxymethyltransferase activity coincided temporally with the incorporation of [3-14C]serine and thymidine into DNA in normal human lymphocytes during proliferation after mitogenic stimulation by phytohemagglutinin. The evidence suggested a primarily gluconeogenic role for serine dehydratase and serine aminotransferase. Serine hydroxymethyl-transferase has a role in providing glycine and one-carbon folate co-factors as precursors for nucleotide biosynthesis and in some situations serves to metabolically couple the pathway of serine biosynthesis to utilization for de novo purine and pyrimidine synthesis. 4.|Multiple enzymic forms were distinguished for serine dehydratase, serine aminotransferase and serine hydroxymethyltransferase. For serine dehydratase the two cytosolic multiple forms had no apparent functional significance; the multiple forms were catalytically unmodified by conditions promoting phosphorylation-dephosphorylation in vitro. The mitochondrial form of serine aminotransferase showed adaptive responses in gluconcogenic situations, and the hypothesis was proposed that the mitochondrial isoenzyme of serine hydroxymethyltransferase is associated together with serine aminotransferase in a pathway for gluconeogenesis from protein-derived amino acids such as glycine and hydroxyproline. 5.|The adaptive behaviour of the enzymes during the neonatal development of rat liver revealed that serine aminotransferase reached a peak in the mid-suckling period at a time when gluconcogenesis is known to be increased. Use of phosphoenolypyruvate carboxykinase inhibitors (mercaptopicolinate or quinolinate) supported a pathway via serine aminotransferase for gluconeogenesis from serine and hydroxyproline at this developmental stage. The concept of the involvement in a carbon salvage pathway to deal with increased body collagen turnover at this time was advanced. The developmental adaptation of serine aminotransferase at birth was shown to involve glucagon, acting via cyclic AMP, and to be dependent on transcriptional gene regulation. 6.|Serine dehydratase showed a biphasic developmental pattern, similar to other enzymes involved in amino acid catabolism. The peaks of activity at the early neonatal and weaning developmental stages were shown to involve the joint action of glucagon, acting via cyclic AMP, and corticosteroid hormones. The inductions were dependent, at least initially, on transcriptional gene regulation but the precise mechanistic role of the two classes of hormone has yet to be defined. At both developmental peaks the distribution of serine dehydratase multiple forms was identical, and differential developmental regulation of the forms was not involved in determining the overall pattern of serine dehydratase development. 7.|Phosphoserine aminotransferase and cytosolic serine hydroxymethyl-transferase showed similar developmental patterns with a peak of activity in the perinatal period. This coincides with an active period of hepatocyte proliferation and of nucleotide biosynthesis. A further rise of serine hydroxymethyltransferase coinciding with a second postnatal surge of proliferative hepatocellular growth was independent of de novo serine biosynthesis and reflected increased provision of serine from dietary sources. 8.|A survey of the key enzymes of serine metabolism in transplantable rat neoplasms revealed that, in general, serine dehydratase and serine aminotransferase were deleted from the cellular repertoire of metabolic capacities. In contrast, phosphoserine aminotransferase and serine hydroxymethyltransferase were selectively retained to varying degrees in neoplastic tissues. 9.|The pattern of serine metabolism displayed in normal, developing and neoplastic tissues revealed an integrated, genetically-programmed, response of enzymes of serine biosynthesis and of alt

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Background
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Background
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Background
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Background
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“3G), a rate-limiting enzyme for de novo serine biosynthesis from glucose (10, 36), was also lower in rats that were allowed to wheel run.”
Background
Reduced number of satellite oligodendrocytes of pyramidal neurons in layer 5 of the prefrontal cortex in schizophrenia
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“l-serine is the substrate for protein and different biomolecule synthesis, including glycine, l-cysteine, phosphatidylserine and d-serine [40, 41].”
Background
Amino acid metabolism in the kidney.
Kuhlmann, M. K., & Kopple, J. D. (1990) · PubMed · Cited by 17
Mouse 3-phosphoglycerate dehydrogenase gene: genomic organization, chromosomal localization, and promoter analysis
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Rat Liver Serine Dehydratase
Ogawa, H., Takusagawa, F., Wakaki, K., Kishi, H., Eskandarian, M. R., Kobayashi, M., Date, T., Huh, N., & Pitot, H. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.18.12855 · Cited by 17
Developmental regulation of rat serine dehydratase gene expression: evidence for the presence of a repressor in fetal hepatocytes
Noda, C., Fukushima, C., Fujiwara, T., Matsuda, K., Kobune, Y., & Ichihara, A. (1994) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(94)90030-2 · Cited by 17
Serine isotopomer analysis by 13C-NMR defines glycine-serine interconversion in situ in the renal proximal tubule
Cowin, G., Willgoss, D. A., Bartley, J. P., & Endre, Z. H. (1996) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(95)00142-5 · Cited by 16
A Quantum Mechanical/Molecular Mechanical Study on the Catalysis of the Pyridoxal 5′-Phosphate-Dependent Enzyme l -Serine Dehydratase
Zhao, Z., & Liu, H. (2008) · The Journal of Physical Chemistry B · doi:10.1021/jp802262m · Cited by 15
Asp-89: a critical residue in maintaining the oligomeric structure of sheep liver cytosolic serine hydroxymethyltransferase
RAO, J. V. K., Junutula, J. R., Sharma, B., Rao, N. A., & Savithri, H. S. (1999) · Biochemical Journal · doi:10.1042/bj3430257 · Cited by 15
Glucose contribution to nucleic acid base synthesis in proliferating hepatoma cells: a glycine-biosynthesis-mediated pathway
Bismut, H., Caron, M., Coudray‐Lucas, C., & Capeau, J. (1995) · Biochemical Journal · doi:10.1042/bj3080761 · Cited by 15
Neuroleptic effects on serine and glycine metabolism
Baruah, S., Waziri, R., & Sherman, A. D. (1993) · Biological Psychiatry · doi:10.1016/0006-3223(93)90197-l · Cited by 15
Hormonal Regulation of Serine Dehydratase Gene Expression in Liver and Kidney of the Adrenalectomized Rat
Kanamoto, R., Su, Y., & Pitot, H. C. (1991) · Molecular Endocrinology · doi:10.1210/mend-5-11-1661 · Cited by 15
“The expression of the serine dehydratase (SDH) gene, whose product, SDH, catalyzes the formation of pyruvate from serine for gluconeogenesis, is essentially restricted to the gluconeogenic tissues of the liver and kidney (1,2).”
Background
Downregulation in the expression of the serine dehydratase in the rat liver during chronic metabolic acidosis
López‐Flores, I., Peragón, J., Valderrama, R., Esteban, F. J., Luque, F., Peinado, M. Á., Aranda, F., Lupiáñez, J. A., & Barroso, J. B. (2006) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00095.2006 · Cited by 14
“In this sense, it is noteworthy that the release of glucocorticoids during metabolic acidosis has been well established (5, 46), although in the liver, glucocorticoid itself does not induce SerDH in vivo but rather has a permissive effect on transcription by stimulating the action of glucagon via cAMP (47).”
BackgroundResult
A catalytic mechanism that explains a low catalytic activity of serine dehydratase like-1 from human cancer cells: Crystal structure and site-directed mutagenesis studies
Yamada, T., Komoto, J., Kasuya, T., Takata, Y., Ogawa, H., Mori, H., & Takusagawa, F. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.01.020 · Cited by 14
Serine utilization in mouse liver: Influence of caloric restriction and aging
Hagopian, K., Ramsey, J. J., & Weindruch, R. H. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.02.062 · Cited by 14
“In rat liver, changes of activity with age have been reported [6,22,23],”
BackgroundResultInfluential
Synthesis of photodeprotectable serine derivatives. “Caged serine”
Pirrung, M. C., & Nunn, D. S. (1992) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(00)80414-x · Cited by 14
Multi-omics Analysis of the Role of PHGDH in Colon Cancer
Dai, Z., Chen, L., Pan, K., Zhao, X., Xu, W., Du, J., & Xing, C. (2023) · Technology in Cancer Research & Treatment · doi:10.1177/15330338221145994 · Cited by 13
Some biochemical and histochemical properties of human liver serine dehydratase
Kashii, T., Gomi, T., Oya, T., Ishii, Y., Oda, H., Maruyama, M., Kobayashi, M., Masuda, T., Yamazaki, M., Nagata, T., et al. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.08.004 · Cited by 13
l-Serine-O-phosphate in the central nervous system
Antflick, J. E., Vetiska, S., Baizer, J. S., Yao, Y., Baker, G. B., & Hampson, D. R. (2009) · Brain Research · doi:10.1016/j.brainres.2009.08.087 · Cited by 13
Proteomic profiling reveals oxidative phosphorylation pathway is suppressed in longissimus dorsi muscle of weaned piglets fed low-protein diet supplemented with limiting amino acids
Yan, G., Li, X., Cheng, X., Peng, Y., Long, B., Fan, Q., Wang, Z., Zheng, Z., Shi, M. Y., & Yan, X. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.08.024 · Cited by 13
“PHGDH and PSAT1 are the first two enzymes involved in the serine synthesis pathway which converts the glycolytic intermediate 3-phosphoglycerat into serine (Snell, 1984).”
BackgroundInfluential
Discovering Essential Multiple Gene Effects Through Large Scale Optimization: An Application to Human Cancer Metabolism
Occhipinti, A., Hamadi, Y., Kugler, H., Wintersteiger, C. M., Yordanov, B., & Angione, C. (2020) · IEEE Transactions on Computational Biology and Bioinformatics · doi:10.1109/tcbb.2020.2973386 · Cited by 13
“Increased PHGDH ﬂux, and in general serine synthesis pathway activity, was initially measured in mouse cancer when compared to normal tissues [26].”
Background
Role of serine biosynthesis and its utilization in the alternative pathway from glucose to glycogen during the response to insulin in cultured foetal-rat hepatocytes
Bismut, H., & Plas, C. (1991) · Biochemical Journal · doi:10.1042/bj2760577 · Cited by 13
A novel intermediate in the interaction of thiosemicarbazide with sheep liver serine hydroxymethyltransferase.
Acharya, J., & Rao, N. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)41741-3 · Cited by 13
The genetic organization and protein crystallographic structure of human serine hydroxymethyltransferase
Snell, K., Baumann, U., Byrne, P. C., Chave, K. J., RENWICK, S. B., Sanders, P. G., & Whitehouse, S. K. (2000) · Advances in Enzyme Regulation · doi:10.1016/s0065-2571(99)00035-7 · Cited by 13
Self-citation
Functional analysis of mouse 3‐phosphoglycerate dehydrogenase (Phgdh) gene promoter in developing brain
Shimizu, M., Furuya, S., Shinoda, Y., Mitoma, J., Okamura, T., Miyoshi, I., Kasai, N., Hirabayashi, Y., & Suzuki, Y. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20102 · Cited by 13
“The Phgdh gene encodes a cytosolic enzyme initiating the phosphorylated pathway of de novo L-Ser biosynthesis (Snell, 1984).”
Background
The Association between Serum Serine and Glycine and Related-Metabolites with Pancreatic Cancer in a Prospective Cohort Study
Luu, H. N., Paragomi, P., Wang, R., Huang, J. Y., Adams‐Haduch, J. M., Midttun, Ø., Ulvik, A., Nguyen, T., Brand, R. E., Gao, Y., et al. (2022) · Cancers · doi:10.3390/cancers14092199 · Cited by 12
“The carbon donation of serine is linked to the conversion of tetrahydrofolate (THF) to methylene-tetrahydrofolate (Methylene-THF) [12,13].”
Background
Enzymatic and biochemical properties of a novel human serine dehydratase isoform
Ogawa, H., Gomi, T., Nishizawa, M., Hayakawa, Y., Endo, S., Hayashi, K., Ochiai, H., Takusagawa, F., Pitot, H. C., Mori, H., et al. (2006) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2006.02.010 · Cited by 12
Selective upregulation of 3-phosphoglycerate dehydrogenase (Phgdh) expression in adult subventricular zone neurogenic niche
Kinoshita, M. O., Shinoda, Y., Sakai, K., Hashikawa, T., Watanabe, M., Machida, T., Hirabayashi, Y., & Furuya, S. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.02.001 · Cited by 12
Allosteric regulation of metabolism in cancer: endogenous mechanisms and considerations for drug design
Macpherson, J. A., & Anastasiou, D. (2017) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2017.03.022 · Cited by 12
The role and research progress of serine metabolism in tumor cells
Lyu, H., Bao, S., Cai, L., Wang, M., Liu, Y., Sun, Y., & Hu, X. S. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1509662 · Cited by 13
“Studies have shown that both endogenous serine produced from glucose and functionally acquired exogenous serine are associated with the growth of cancer cells in vitro and in vivo and functionally promote cancer progression (6 – 10).”
Activities of serine hydroxymethyltransferase in murine tissues and tumours
Tendler, S. J. B., Threadgill, M. D., & Tisdale, M. J. (1987) · Cancer Letters · doi:10.1016/0304-3835(87)90103-0 · Cited by 11
Evidence for a dimeric structure of rat liver serine dehydratase
Ogawa, H. (2002) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00146-7 · Cited by 11
Serine dehydratase expression decreases in rat livers injured by chronic thioacetamide ingestion
López‐Flores, I., Barroso, J. B., Valderrama, R., Esteban, F. J., Martínez‐Lara, E., Luque, F., Peinado, M. Á., Ogawa, H., Lupi��ez, J. A., & Peragón, J. (2005) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-005-2995-2 · Cited by 11
“It also bears noting, concerning our findings on chronic liver injury, that SerDH activity decreases or even disappears in conjunction with several types of liver cancer, in particular with transplantable Morris hepatomas, Novikoff hepatoma and with a primary hepatoma arising during azodye-induced carcinogenesis [4].”
BackgroundResultInfluential
Serine synthesis by an isolated perfused rat kidney preparation
Scaduto, R. C., & Davis, E. J. (1985) · Biochemical Journal · doi:10.1042/bj2300303 · Cited by 11
Kinetic Evidence of a Noncatalytic Substrate Binding Site That Regulates Activity in Legionella pneumophila l -Serine Dehydratase
Grant, G. A. (2012) · Biochemistry · doi:10.1021/bi3008774 · Cited by 10
Molecular and functional characterization of d-3-phosphoglycerate dehydrogenase in the serine biosynthetic pathway of the hyperthermophilic archaeon Sulfolobus tokodaii
Shimizu, Y., Sakuraba, H., Doi, K., & Ohshima, T. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.11.010 · Cited by 10
Untargeted Metabolomics Studies of H9c2 Cardiac Cells Submitted to Oxidative Stress, β-Adrenergic Stimulation and Doxorubicin Treatment: Investigation of Cardiac Biomarkers
Lima, M. F., Amaral, A. G., Moretto, I. A., Paiva-Silva, F. J. T. N., Pereira, F. O. B., Barbas, C., dos Santos, A. M., Simionato, A. V. C., & Rupérez, F. J. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.898742 · Cited by 9
“However, Snell explains that enzymes from the serine biosynthetic pathway are present displaying high activity in the kidneys, testicles, spleen and brain, while presenting low activities in the skeletal and cardiac muscle (Snell, 1984).”
Background
The Response to Postnatal Stress: Amino Acids Transporters and PKC Activity
Odeón, M. M., Salatino, A., Rodríguez, C. B., Scolari, M. J., & Acosta, G. B. (2010) · Neurochemical Research · doi:10.1007/s11064-010-0153-z · Cited by 9
“This small neutral amino acid is synthesized from the glycolytic intermediate 3-phosphoglycerate [14, 15].”
Background
Optimized two‐dimensional gel electrophoresis in an alkaline pH range improves the identification of intracellular CFDA‐cisplatin‐protein adducts in ovarian cancer cells
Kotz, S., Kullmann, M., Kalayda, G. V., Dyballa‐Rukes, N., Jaehde, U., & Metzger, S. U. (2018) · Electrophoresis · doi:10.1002/elps.201700377 · Cited by 9
Proteogenomic Study of the Effect of an Improved Mixed Diet of Live Preys on the Aquaculture of Octopus vulgaris Paralarvae
Varó, I., Prado-Álvarez, M., Ortea, I., Morales, A. E., García-Fernández, P., Domíngues, P., Tur, R., Dios, S., & Gestal, C. (2022) · Frontiers in Marine Science · doi:10.3389/fmars.2021.817701 · Cited by 9
“In addition, Ser is considered the largest source of intermediates for purine and thymidine synthesis (Snell, 1984; Barret, 1994).”
Background
SLC17A2 Expression Correlates with Prognosis and Immune Infiltrates in Hepatocellular Carcinoma
Jiang, Z., Chen, X., & Jiang, Z. (2022) · Combinatorial Chemistry & High Throughput Screening · doi:10.2174/1386207325666220126104358 · Cited by 9
3-Phosphoglycerate dehydrogenase expression is regulated by HOXA10 in murine endometrium and human endometrial cells
Du, H., Vitiello, D., Sarno, J. L., & Taylor, H. S. (2009) · Reproduction · doi:10.1530/rep-08-0376 · Cited by 9
“It is expressed at high levels in diverse tissue including: prostate, testis, ovary, brain, liver, kidney and pancreas (Snell 1984).”
Background
Vitamin B12deficiency results in the abnormal regulation of serine dehydratase and tyrosine aminotransferase activities correlated with impairment of the adenylyl cyclase system in rat liver
Ebara, S., Nakao, M., Tomoda, M., Yamaji, R., Watanabe, F., Inui, H., & Nakano, Y. (2007) · British Journal Of Nutrition · doi:10.1017/s0007114507812025 · Cited by 9
Aspects of one-carbon folate cycling related to fluoropyrimidine and antifolate therapy
Spears, C. P., Carlsson, G. U., Muggia, F. M., Jaresko, G. S., & Gustavsson, B. G. (1995) · Cancer treatment and research · doi:10.1007/978-1-4615-2007-8_6 · Cited by 9
Phosphoserine Aminotransferase has Conserved Active Site from Microbes to Higher Eukaryotes with Minor Deviations
Singh, R. K., Kumar, D., & Gourinath, S. (2021) · Protein and Peptide Letters · doi:10.2174/0929866528666210215140231 · Cited by 8
2 Serine, Glycine, and Threonine
de Koning, T. J., Fuchs, S. A., & Klomp, L. W. J. (2007) · Springer eBooks · doi:10.1007/978-0-387-30373-4_2 · Cited by 8
Modulation of glycine-serine interconversion by TCA and glycolytic intermediates in normoxic and hypoxic proximal tubules
Cowin, G., Willgoss, D. A., & Endre, Z. H. (1996) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(95)00141-7 · Cited by 8
Periportal expression of the serine dehydratase gene in rat liver
Ogawa, H., & Kawamata, S. (1995) · The Histochemical Journal · doi:10.1007/bf02389024 · Cited by 8
Pathways of glycogen synthesis from glucose during the glycogenic response to insulin in cultured foetal hepatocytes
Bismut, H., & Plas, C. (1989) · Biochemical Journal · doi:10.1042/bj2630889 · Cited by 8

Authors: Snell, K.
Venue: Advances in Enzyme Regulation
Publisher: Elsevier BV
Published: 1984-01
Volume: 22
Pages: 325-400
ISSN: 0065-2571 (ISSN-L)
DOI: 10.1016/0065-2571(84)90021-9
OpenAlex: W1979511656
Cited by: 267
References: 202
Citations by year: 2026: 2 · 2025: 6 · 2024: 5 · 2023: 9 · 2022: 7 · 2021: 11 · 2020: 9 · 2019: 10 · 2018: 14 · 2017: 8 · 2016: 7 · 2015: 9 · 2014: 12 · 2013: 6 · 2012: 9
FWCI: 2.37
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Advances in Enzyme Regulation (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Health Sciences › Nursing › Nutrition and Dietetics › Folate and B Vitamins Research
Keywords: serine metabolism, serine dehydratase, serine hydroxymethyltransferase, phosphoserine aminotransferase, gluconeogenesis, nucleotide synthesis, isozymes, tissue distribution, cell proliferation, lymphocytes, phytohemagglutinin
MeSH terms: Transaminases, Animals, Carbohydrate Dehydrogenases, Cell Division, Cell Line, DNA, Female, Fetus, Growth, Isoenzymes, Liver, Male, Neoplasms, Phosphoric Monoester Hydrolases, Rats, Inbred Strains, Serine, L-Serine Dehydratase, Glycine Hydroxymethyltransferase, Subcellular Fractions, Tissue Distribution, Phosphoglycerate Dehydrogenase, Rats

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Enzymes of serine metabolism in normal, developing and neoplastic rat tissues

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