Disease relevance of Sds

• SDH (L-serine dehydratase, EC 4.3.1.17) catalyzes the pyridoxal 5'-phosphate (PLP)-dependent dehydration of L-serine to yield pyruvate and ammonia [1].
• The peptide sequences near the bound pyridoxal phosphate are conserved in serine dehydratase from rat liver, and threonine dehydratases from yeast and Escherichia coli [2].
• Effect of pyridoxine availability on the activity of serine dehydratase of normal liver, host liver, and three Morris hepatomas [3].
• These results suggest that nutritional control and tissue-specific expression of the serine dehydratase gene is closely associated with the alteration of DNase I hypersensitivity at specific sites of the 5'-flanking region of the gene [4].
• The circadian cycle for ornithine aminotransferase synthesis was in phase with the cycles for body weight and relative liver weight (maxima at 9 a.m., minima at 9 p.m.) but was approximately 12 hours out of phase with the cycle for serine dehydratase synthesis [5].

Psychiatry related information on Sds

• The effect of o,p'-DDT feeding and food deprivation on plasma and liver amino acids and liver serine dehydratase in rats [6].

High impact information on Sds

• The effect(s) of dietary pyridoxine availability on serine dehydratase (SD) specific activity levels of normal liver [3].
• Serine dehydratase activity depends greatly on dietary vitamin B6 and hence I propose that activity levels in vivo are regulated by its presence or absence [3].
• Isolation and nucleotide sequence of the cDNA for rat liver serine dehydratase mRNA and structures of the 5' and 3' flanking regions of the serine dehydratase gene [7].
• Rat serine dehydratase cDNA clones were isolated from a lambda gt11 cDNA library on the basis of their reactivity with monospecific immunoglobulin to the purified enzyme [7].
• The deduced amino acid sequence contained sequences of several portions of the serine dehydratase protein, as determined by Edman degradation [7].

Chemical compound and disease context of Sds

• Serine hydroxymethyltransferase activity was present in hepatomas, whereas other enzymes of serine utilization (serine dehydratase and serine aminotransferase) were absent [8].
• PEPCK, which is localized to the proximal tubules under the normal condition, spreads throughout the entire cortex to the outer medullary rays by acidosis, whereas SDH does not change regardless of treatment with dexamethasone or NH(4)Cl [9].
• We conclude that the enhanced regulatory effect of epinephrine counteracting insulin on SDH gene transcription in liver of newborn dogs may be one of the mechanisms responsible for the neonatal insulin resistance which contributes to neonatal hyperglycemia [10].

Biological context of Sds

• Rat liver serine dehydratase (SDH) is known to be involved in gluconeogenesis [11].
• Organization and structure of the 5' flanking region of the rat serine dehydratase gene [12].
• The possibility to producing two species of serine dehydratase mRNAs from a single gene by transcription from different sites and alternative splicing is discussed [12].
• For study of the mechanisms regulating the induction of serine dehydratase by various hormones in rat liver [Noda et al. (1988) J. Biol. Chem. 263, 14764-14768], we cloned the gene for this enzyme from a rat genomic library [12].
• Southern blot analysis of rat genomic DNA suggested the presence of one copy of serine dehydratase gene per haploid genome [12].

Anatomical context of Sds

• This unique hormone requirement was studied further with a cDNA probe complementary to SDH mRNA in primary cultured hepatocytes of adult rats [13].
• Evidence is presented to show that, following the administration of amino acids in vivo, the relative synthetic capabilities of free and membrane-bound polyribosomes synthesizing serine dehydratase vary with time [14].
• Dominant numbers of T cells in acute HP included CD8+ RT6- (TCYT) and CD8+ CD45R- (TCYT) subsets, with putative cytotoxic T-cell activity, in addition to CD4+ RT6- (TDH) cells [15].
• Diurnal rhythms of rat liver serine dehydratase, D-site binding protein, and 3-hydroxy-3-methylglutaryl coenzyme A reductase mRNA levels are altered by destruction of the suprachiasmatic nucleus of the hypothalamus [16].
• The serine dehydratase activity in crude homogenates of rat liver, intestine, adipose tissue, kidney, brain, leg striated muscle, skin and stomach, both in fed and 24-hour fasted rats have been estimated [17].

Associations of Sds with chemical compounds

• The 5' end of serine dehydratase mRNA is located 148 nucleotides upstream of the initiator methionine codon [12].
• The blocked amino-terminal residue of rat liver serine dehydratase was shown to be acetylalanine by analysis of an isolated amino-terminal peptide after digestion with acylamino acid-releasing enzyme [2].
• SD activity was highly affected by pyridoxine [3].
• Hyperplastic area showed a marked deficiency of beta-glucuronidase and serine dehydratase during their developing phase, the 6th through the 9th experimental weeks, and were fairly specifically labeled by injections of tritiated thymidine after partial hepatectomy performed at the 9th week [18].
• These results suggested that SDH is the major metabolic exit of L-serine in rat liver [19].

Regulatory relationships of Sds

• Rat GATA-1 expressed as a GST-fusion protein in E. coli bound to the GAT(A/T) motif in the serine dehydratase gene [20].
• We have previously demonstrated that glucagon but not dexamethasone could induce serine dehydratase (SDH: EC.4.2.1.13) in liver, and either glucagon or dexamethasone could induce the enzyme in kidney of normal rats [21].

Other interactions of Sds

• In contrast, functions related to hepatocyte-specific characters, such as the inductions of tyrosine aminotransferase, serine dehydratase, and malic enzyme and synthesis of triglycerides, are stimulated by high cell density [22].
• While the basal levels of the enzymes serine dehydratase and tyrosine aminotransferase were the same as those found in control rats, their response to glucagon was reduced in experimental animals with or without tumors [23].
• Other enzymes, namely alanine and aspartate aminotransferase, ornithine aminotransferase, ornithine carbamoyltransferase, serine dehydratase, and histidine ammonialyase, were not affected by treatment of rats with alphaMeTrp [24].
• After 20 hours starvation, activity of alanine aminotransferase and serine dehydratase still reflected the induction of these enzymes in fed rats [25].
• Similarly, the activities of alanine aminotransferase, arginase and serine dehydratase were significantly higher in the liver of P50 rats compared with P14 rats [26].

Analytical, diagnostic and therapeutic context of Sds

• Rat liver serine dehydratase mRNA virtually disappeared from livers of rats fed a protein-free diet for 5 days [7].
• The native M(r) of rat SDH was only determined by the ultracentrifugation method more than three decades ago, and that of sheep SDH was done by the method of gel chromatography [11].
• Kidney contained serine dehydratase mRNA at a level of 5% of liver as determined by Northern blotting [4].
• Liver serine dehydratase activities in the groups fed MCT or LCT were similar, although they were significantly lower than in the control group [27].
• In situ hybridization and immunohistochemistry revealed that SDH was localized to the proximal straight tubule of the nephron [9].

References