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Enzymes of serine metabolism in normal, developing and neoplastic rat tissues
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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“Increased activity of de novo serine synthesis enzymes in cancer has been observed for more than 30 years (Snell, 1984; Snell et al., 1988).”
From Targeting Metabolism for Cancer Therapy (2017) · cites this paper as Snell, 1984
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“Increased serine biosynthesis is one of many metabolic changes that have been reported in cancer cells (Davis et al., 1970; Snell, 1984), and serine is a central node for the biosynthesis of many molecules (Fig.”
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“L-Serine biosynthesis from a glycolytic intermediate 3-phosphoglycerate (i.e., phosphorylated pathway) involves three sequential reactions initiated by 3-phosphoglycerate dehydrogenase (3PGDH) (Ichihara and Greenberg, 1957; Snell, 1984).”
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“Also in stark contrast with cancer cells (Locasale et al., 2011; Snell, 1984), glucose does not generate fatty acids and cholesterol, amino acids including glycine and serine or purine nucleobases.”
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“By contrast, glycine is converted from l-serine that is synthesized from 3-phosphoglycerate, an intermediate of the glycolytic pathway (Ichihara & Greenberg, 1957; Snell, 1984).”
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“Lserine serves as a precursor in the synthesis of L-cysteine, sphingolipids, and the neuromodulators D-serine and glycine, which modulate excitatory NMDA receptors and inhibitory glycine receptors in the brain (Snell, 1984).”
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“The serine synthesis pathway converts the glycolytic intermediate 3-phosphoglycerate into serine via a three-step reaction involving three metabolic enzymes: phosphoglycerate dehydrogenase (PHGDH),(3) phosphoserine aminotransferase 1 (PSAT1), and phosphate ester hydrolysis (12).”
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“In mammals, SD is involved in the regulation of 427 liver gluconeogenesis from serine in different dietary, hormonal and developmental states by 428 providing pyruvate (47), but in the case of rainbow trout pyruvate originating from SD 429 activity might be directed to lipid synthesis and thus contribute to enhanced l…”
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“It is noteworthy that Snell and coworkers had previously identified enhanced activity of the PHGDH pathway in homogenates of neoplastic tissues relative to normal tissues (Snell, 1984, 1986).”
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“…amounts, the preferential reorientation of serine utilization for nucleotide precursor formation in the corresponding tumour is achieved by a deletion of these competing enzymes whilst retaining a proportion of serine hydroxymethyltransferase activity (Snell, 1984, 1985; Snell & Weber, 1986 ).”
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“In mammals, SD is involved in the regulation of liver gluconeogenesis from serine in different dietary, hormonal and developmental states by providing pyruvate ( Snell 1984 ).”
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“In prokaryotes and mammals, Ser is synthesized predominantly via the PS pathway using 3-PGA (Pizer, 1963; McKitrick and Pizer, 1980; Snell, 1984; Achouri et al., 1997; Dey et al., 2005), whereas in yeast (Saccharomyces cerevisiae), Ser can be produced either by the PS or the gluconeogenic pathway,…”
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“In mammals, SD is involved in the regulation of liver gluconeogenesis from serine in different dietary, hormonal, and developmental states by providing pyruvate (41).”
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“Glycine, which interconverts with L-serine by means of serine hydroxymethyltransferase [56], is also decreased in Phgdh null embryos but to a lesser extent than L-serine.”
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“…of the de novo serine synthesis module was initially reported to correlate with increased liver cell proliferation and tumorigenesis in rats (Snell, 1984; Snell et al., 1987; Snell and Weber, 1986), and despite the known protumorigenic effects of folate species in child leukemias, the…”
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“biosynthesis, PHGDH, has been reported in recent cancer biology studies [9].”
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“Because L-Ser serves as a building block for proteins and indispensable precursors for membrane lipids (phosphatidyl-L-Ser and sphingolipids) and nucleotides (Snell, 1984; Stryer, 1995), a higher demand for the amino acid should be associated with developing brains, where neural cells proliferate and differentiate by…”
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“The enzymes of the phosphorylated pathway are widely distributed in humans and high mRNA expression and activity of these enzymes are found in a variety of organs (Snell, 1984; Klomp et al., 2000; Baek et al., 2003).”
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“Subsequent studies showed that PHGDH activity was most consistently increased and correlated with tumor growth in many other tumors [31].”
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“The enzyme defect affects the conversion of 3-phosphoglycerate to 3-phosphohydroxypyruvate, the ¢rst step in the L-serine biosynthetic pathway (Snell 1984).”
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“Subsequent work (Snell, 1984) showed that this was true in many other tumors as well, and that among the pathway enzymes, tumor growth was most consistently correlated with an increase in PGDH activity.”
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“Increased serine biosynthesis is one of many metabolic changes that have been reported in cancer cells [43,44], and serine is a central node for the biosynthesis of many molecules such as glycine and cysteine [45].”
BackgroundTreatment with amino acids in serine deficiency disorders
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“L-Serine has for several years been recognized as having a role in cellular proliferation, being a precursor for nucleotide synthesis (Snell 1984) However, after the first report of patients with serine deficiency disorders it became clear that”
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“Tumor cells require excessive nutrients to support their growth and survival, and genes within the L -serine synthesis and FOCM pathways are commonly expressed at higher levels in cancer cells (103).”
BackgroundMethodGlycine homeostasis requires reverse SHMT flux
McBride, M. J., Hunter, C. J., Zhang, Z., TeSlaa, T. A., Xu, X., Ducker, G. S., & Rabinowitz, J. D. (2024) · Cell Metabolism · doi:10.1016/j.cmet.2023.12.001 · Cited by 71
Schwechheimer, S. K., Becker, J., Peyriga, L., Portais, J., Sauer, D., Müller, R., Hoff, B., Haefner, S., Schröder, H., Zelder, O., et al. (2018) · Metabolic Engineering · doi:10.1016/j.ymben.2018.04.005 · Cited by 67
Contrasting catalytic and allosteric mechanisms for phosphoglycerate dehydrogenases
Grant, G. A. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.10.005 · Cited by 66
The PHGDH enigma: Do cancer cells only need serine or also a redox modulator?
Li, A. M., & Ye, J. (2020) · Cancer Letters · doi:10.1016/j.canlet.2020.01.036 · Cited by 65
Novel neuroglial and glioglial relationships mediated by L-serine metabolism
Furuya, S., & Watanabe, M. (2003) · Archivum histologicum japonicum · doi:10.1679/aohc.66.109 · Cited by 63
Control of Oxalate Formation from L-Hydroxyproline in Liver Mitochondria
Takayama, T., Fujita, K., Suzuki, K. T., Sakaguchi, M., Fujie, M., Nagai, E., Watanabe, S., Ichiyama, A., & Ogawa, Y. (2003) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000059310.67812.4f · Cited by 63
“Glycine thus formed may be oxidized to CO2 and ammonia by the mitochondrial glycine cleavage enzyme system, and in conjugation with this oxidation another molecule of glycine is converted to L-serine by mitochondrial serine hydroxymethyltransferase (5).”
BackgroundThe intrinsic disorder alphabet. III. Dual personality of serine
Uversky, V. N. (2015) · Intrinsically Disordered Proteins · doi:10.1080/21690707.2015.1027032 · Cited by 59
Flux of the l-Serine Metabolism in Rabbit, Human, and Dog Livers
Xue, H., Sakaguchi, T., Fujie, M., Ogawa, H., & Ichiyama, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.23.16028 · Cited by 56
1H MR spectroscopic imaging with short and long echo time to discriminate glycine in glial tumours
Hattingen, E., Lanfermann, H., Quick, J., Franz, K., Zanella, F. E., & Pilatus, U. (2008) · Magnetic Resonance Materials in Physics Biology and Medicine · doi:10.1007/s10334-008-0145-z · Cited by 55
“Serine biosynthesis from 3-phosphoglycerate, an intermediate of the glycolytic pathway [41] seems to be enhanced in proliferating cells [37,42,43].”
BackgroundA retrospective overview of PHGDH and its inhibitors for regulating cancer metabolism
Zhao, J.-Y., Feng, K., Wang, F., Zhang, J., Cheng, J. F., Lin, G., Gao, D., & Tian, P. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113379 · Cited by 56
Metabolic control analysis of mammalian serine metabolism
Snell, K., & Fell, D. A. (1990) · Advances in Enzyme Regulation · doi:10.1016/0065-2571(90)90006-n · Cited by 55
Self-citationThreonine metabolism in isolated rat hepatocytes
House, J. D., Hall, B., & Brosnan, J. T. (2001) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2001.281.6.e1300 · Cited by 55
“In addition, the enzyme threonine dehydratase does not appear to be regulated by either allosteric mechanisms or covalent modification (29).”
BackgroundThe phosphorylated pathway of serine biosynthesis links plant growth with nitrogen metabolism
Zimmermann, S. E., Benstein, R. M., Flores‐Tornero, M., Blau, S., Anoman, A. D., Rosa‐Téllez, S., Gerlich, S. C., Salem, M. A., Alseekh, S., Kopřiva, S., et al. (2021) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiab167 · Cited by 55
Enzymes of serine metabolism in normal and neoplastic rat tissues
Snell, K. (1985) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(85)90149-7 · Cited by 54
Self-citation3-Phosphoglycerate dehydrogenase: a potential target for cancer treatment
Li, M., Wu, C., Yang, Y., Zheng, M., Yu, S., Wang, J., Chen, L., & Li, H. (2021) · Cellular Oncology · doi:10.1007/s13402-021-00599-9 · Cited by 51
SLC1A5 provides glutamine and asparagine necessary for bone development in mice
Sharma, D., Yu, Y., Shen, L., Zhang, G., & Karner, C. M. (2021) · eLife · doi:10.7554/elife.71595 · Cited by 51
Hashimoto, A., & Chiba, Y. (2004) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2004.05.036 · Cited by 51
Jaeken, J., Detheux, M., Maldergem, L. V., Frijns, J., Alliet, P. L., Foulon, M., Carchon, H. A., & SCHAFTINGEN, E. V. (1996) · Journal of Inherited Metabolic Disease · doi:10.1007/bf01799435 · Cited by 50
“This suggested a defect in the serine de novo biosynthetic pathway (Snell 1983), which was confirmed by finding, in fibroblasts of the two patients, a markedly decreased activity of phosphoglycerate dehydrogenase, the first step in this pathway (Figure t).”
Yamamoto, T., Nishizaki, I., Furuya, S., Hirabayashi, Y., Takahashi, K., Okuyama, S., & Yamamoto, H. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00742-7 · Cited by 49
Linking Serine/Glycine Metabolism to Radiotherapy Resistance
Sánchez‐Castillo, A., Vooijs, M., & Kampen, K. R. (2021) · Cancers · doi:10.3390/cancers13061191 · Cited by 47
“The reversible interconversion of serine and glycine is catalyzed by either the cytosolic or mitochondrial serine hydroxymethyltransferase (SHMT), SHMT1 or SHMT2, respectively [12,23].”
BackgroundAmino Acids in Cancer and Cachexia: An Integrated View
Ragni, M., Fornelli, C., Nisoli, E., & Penna, F. (2022) · Cancers · doi:10.3390/cancers14225691 · Cited by 48
Ali, V., Hashimoto, T., Shigeta, Y., & Nozaki, T. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04195.x · Cited by 47
“In addition to its role in the synthesis of L-cysteine and L-glycine and also in the formation of L-methionine by the interconversion of L-cysteine via L-cystathionine, L-serine is a major precursor of phosphatidyl-L-serine, sphingolipids, taurine, porphyrins, purines, thymidine and neuromodulators D-serine and D-glyc…”
BackgroundTwo new cases of serine deficiency disorders treated with l-serine
Brassier, A., Valayannopoulos, V., Bahi‐Buisson, N., Wiame, E., Hubert, L., Boddaert, N., Kamińska, A., Habarou, F., Desguerre, I., SCHAFTINGEN, E. V., et al. (2015) · European Journal of Paediatric Neurology · doi:10.1016/j.ejpn.2015.10.007 · Cited by 47
Nutritional regulation and tissue-specific expression of the serine dehydratase gene in rat.
Ogawa, H., Fujioka, M., Su, Y., Kanamoto, R., & Pitot, H. C. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54938-3 · Cited by 47
Yu, J., Xiao, F., Guo, Y., Deng, J., Liu, B., Zhang, Q., Li, K., Wang, C., Chen, S., & Guo, F. (2014) · Diabetes · doi:10.2337/db14-1368 · Cited by 46
“Three steps are involved in serine synthesis (11), and PSAT1 is involved in the second step catalyzing the 3-phosphohydroxypyruvate to form L-phosphoserine (11,12).”
BackgroundAssociations between multiple system atrophy and polymorphisms of SLC1A4, SQSTM1, and EIF4EBP1 Genes
Soma, H., Yabe, I., Takei, A., Fujiki, N., Yanagihara, T., & Sasaki, H. (2008) · Movement Disorders · doi:10.1002/mds.22046 · Cited by 45
“L-Ser is biosynthesized from 3-phosphoglycerate through phoshorylated serine pathway.(18) Astrocytes”
BackgroundIdentification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase
Maliekal, P., Vertommen, D., Delpierre, G., & SCHAFTINGEN, E. V. (2005) · Glycobiology · doi:10.1093/glycob/cwj050 · Cited by 45
“A), Dowex 1-X8 (200 mesh; Cl- form) was from Acros Organics (Geel, Belgium).”
BackgroundFlux of the l-Serine Metabolism in Rat Liver
Xue, H., Fujie, M., Sakaguchi, T., Oda, T., Ogawa, H., Kneer, N. M., Lardy, H. A., & Ichiyama, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.23.16020 · Cited by 44
Serine Metabolic Reprogramming in Tumorigenesis, Tumor Immunity, and Clinical Treatment
Wang, S., Xiaoxue, Y., Guanbin, S., Yang, L., Junyu, J., & Liu, W. (2023) · Advances in Nutrition · doi:10.1016/j.advnut.2023.05.007 · Cited by 47
The Fate of Glutamine in Human Metabolism. The Interplay with Glucose in Proliferating Cells
Mazat, J., & Ransac, S. (2019) · Metabolites · doi:10.3390/metabo9050081 · Cited by 44
“It is the pr cursor of glycine (see [39] for a mini-re i In his pioneering work, Snell demonstrated the importance of serin biosynthesis in rat carcinoma [40].”
BackgroundPind, S., Slominski, E., Mauthe, J., Pearlman, K., Swoboda, K. J., Wilkins, J. A., Sauder, P. J., & Natowicz, M. R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111419200 · Cited by 43
Nishiu, M., Yanagawa, R., Nakatsuka, S., Yao, M., Tsunoda, T., Nakamura, Y., & Aozasa, K. (2002) · Japanese Journal of Cancer Research · doi:10.1111/j.1349-7006.2002.tb01335.x · Cited by 43
Unterlass, J. E., Baslé, A., Blackburn, T. J., Tucker, J. A., Cano, C., Noble, M. E. M., & Curtin, N. J. (2016) · Oncotarget · doi:10.18632/oncotarget.11487 · Cited by 42
Crystal structure of the pyridoxal‐5′‐phosphate‐dependent serine dehydratase from human liver
Sun, L., Bartlam, M. G., Liu, Y., Pang, H., & Rao, Z. (2005) · Protein Science · doi:10.1110/ps.041179105 · Cited by 40
“Extensive studies have been carried out on SDH from rat and the enzyme has been found to play an important role in gluconeogenesis since its activity is remarkably induced by the consumption of high-protein diets, starvation, and other conditions (Snell 1984; Ebara et al. 2001).”
BackgroundSerine metabolism in human pregnancy
Kalhan, S. C., Gruca, L. L., Parimi, P. S., O’Brien, A., Dierker, L. J., & Burkett, E. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00167.2002 · Cited by 39
“development is underscored by its role as precursor for nucleotide biosynthesis during the rapid growth phase in neonatal rats (38, 39) and as a source for the one carbon pool for nucleotide synthesis and during cell proliferation (40).”
Background
Metadata
- Authors
- Snell, K.
- Venue
- Advances in Enzyme Regulation
- Publisher
- Elsevier BV
- Published
- 1984-01
- Volume
- 22
- Pages
- 325-400
- ISSN
- 0065-2571 (ISSN-L)
- 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
- 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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