Control of expression of one-carbon metabolism genes of Saccharomyces cerevisiae is mediated by a tetrahydrofolate-responsive protein binding to a glycine regulatory region including a core 5'-CTTCTT-3' motif. (1/33)
Expression of yeast genes involved in one-carbon metabolism is controlled by glycine, by L-methionine, and by nitrogen sources. Here we report a novel control element containing a core CTTCTT motif mediating the glycine response, demonstrating that a protein binds this element, that binding is modulated by tetrahydrofolate, and that folate is required for the in vivo glycine response. In an heterologous CYC1 promoter the region needed for the glycine response of GCV2 (encoding the P-subunit of glycine decarboxylase) mediated repression that was relieved by glycine. It was also responsible for L-methionine control but not nitrogen repression. GCV1 and GCV3 have an homologous region in their promoters. The GCV1 region conferred a glycine response on an heterologous promoter acting as a repressor or activator depending on promoter context. A protein was identified that bound to the glycine regulatory regions of GCV1 and GCV2 only if the CTTCTT motif was intact. This protein protected a 17-base pair CATCN7CTTCTT region of GCV2 that is conserved between GCV1 and GCV2. Protein binding was increased by tetrahydrofolate, and use of a fol1 deletion mutant indicated the involvement of a folate in the in vivo glycine response. Tetrahydrofolate or a derivative may act as a ligand for the transcription factor controlling expression of one-carbon metabolism genes. (+info)Role for the leucine-responsive regulatory protein (Lrp) as a structural protein in regulating the Escherichia coli gcvTHP operon. (2/33)
The Escherichia coli glycine-cleavage enzyme system (gcvTHP and lpd gene products) provides C1 units for cellular methylation reactions. Both the GcvA and leucine-responsive regulatory (Lrp) proteins are required for regulation of the gcv operon. One model proposed for gcv regulation is that Lrp plays a structural role, bending the DNA to allow GcvA to function as either an activator or a repressor in response to environmental signals. This hypothesis was tested by replacing all but the upstream 22 bp of the Lrp-binding region in a gcvT::lacZ fusion with the I1A site from phage lambda. Integration host factor (IHF) binds the I1A site and bends the DNA about 140 degrees. Shifting the I1A site by increments of 1 base around the DNA helix resulted in IHF-dependent activation and repression of gcvT::lacZ expression that were face-of-the-helix dependent. Activation was also dependent on the GcvA protein, and repression was dependent on both the GcvA and GcvR proteins, demonstrating that the roles for these proteins were not altered. The results are consistent with Lrp playing primarily a structural role in gcv regulation, although they do not completely rule out the possibility that Lrp also interacts with another gcv-regulatory protein or with RNA polymerase. (+info)Identification of the folate binding sites on the Escherichia coli T-protein of the glycine cleavage system. (3/33)
T-protein is a component of the glycine cleavage system and catalyzes the tetrahydrofolate-dependent reaction. To determine the folate-binding site on the enzyme, 14C-labeled methylenetetrahydropteroyltetraglutamate (5,10-CH2-H4PteGlu4) was enzymatically synthesized from methylenetetrahydrofolate (5, 10-CH2-H4folate) and [U-14C]glutamic acid and subjected to cross-linking with the recombinant Escherichia coli T-protein using 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide, a zero-length cross-linker between amino and carboxyl groups. The cross-linked product was digested with lysylendopeptidase, and the resulting peptides were separated by reversed-phase high performance liquid chromatography. Amino acid sequencing of the labeled peptides revealed that three lysine residues at positions 78, 81, and 352 were involved in the cross-linking with polyglutamate moiety of 5, 10-CH2-H4PteGlu4. The comparable experiment with 5,10-CH2-H4folate revealed that Lys-81 and Lys-352 were also involved in cross-linking with the monoglutamate form. Mutants with single or multiple replacement(s) of these lysine residues to glutamic acid were constructed by site-directed mutagenesis and subjected to kinetic analysis. The single mutation of Lys-352 caused similar increase (2-fold) in Km values for both folate substrates, but that of Lys-81 affected greatly the Km value for 5,10-CH2-H4PteGlu4 rather than for 5,10-CH2-H4folate. It is postulated that Lys-352 may serve as the primary binding site to alpha-carboxyl group of the first glutamate residue nearest the p-aminobenzoic acid ring of 5,10-CH2-H4folate and 5,10-CH2-H4PteGlu4, whereas Lys-81 may play a key role to hold the second glutamate residue through binding to alpha-carboxyl group of the second glutamate residue. (+info)The amino-terminal region of the Escherichia coli T-protein of the glycine cleavage system is essential for proper association with H-protein. (4/33)
T-protein is a component of the glycine cleavage system and catalyzes the tetrahydrofolate-dependent reaction. Our previous work on Escherichia coli T-protein (ET) showed that the lack of the N-terminal 16 residues caused a loss of catalytic activity [Okamura-Ikeda, K., Ohmura, Y., Fujiwara, K. and Motokawa, Y. (1993) Eur. J. Biochem. 216, 539-548]. To define the role of the N-terminal region of ET, a series of deletion mutants were constructed by site-directed mutagenesis and expressed in E. coli. Deletions of the N-terminal 4, 7 and 11 residues led to reduction in the activity to 42, 9 and 4%, respectively, relative to the wild-type enzyme (wtET). The mutant with 7-residue deletion (ETDelta7) was purified and analyzed. ETDelta7 exhibited a marked increase in Km (25-fold) for E. coli H-protein (EH) accompanied by a 10-fold decrease in kcat compared with wtET, indicating the importance of the N-terminal region in the interaction with EH. The role of this region in the ET-EH interaction was investigated by cross-linking of wtET-EH or ETDelta7-EH complex with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide, a zero-length cross-linker, in the presence of folate substrates. The resulting tripartite cross-linked products were cleaved with lysylendopeptidase and V8 protease. After purification by reversed-phase HPLC, the cross-linked peptides were subjected to Edman sequencing. An intramolecular cross-linking between Asp34 and Lys216 of wtET which was not observed in wtET alone and an intermolecular cross-linking between Lys288 of wtET and Asp-43 of EH were identified. In contrast, no such cross-linking was detected from the cross-linked product of ETDelta7. These results suggest that EH, when it interacts with ET, causes a change in conformation of ET and that the N-terminal region of ET is essential for the conformational change leading to the proper interaction with EH. (+info)Regulation of the balance of one-carbon metabolism in Saccharomyces cerevisiae. (5/33)
One-carbon metabolism in yeast is an essential process that relies on at least one of three one-carbon donor molecules: serine, glycine, or formate. By a combination of genetics and biochemistry we have shown how cells regulate the balance of one-carbon flow between the donors by regulating cytoplasmic serine hydroxymethyltransferase activity in a side reaction occurring in the presence of excess glycine. This control governs the level of 5,10-methylene tetrahydrofolate (5,10-CH(2)-H(4)folate) in the cytoplasm, which has a direct role in signaling transcriptional control of the expression of key genes, particularly those encoding the unique components of the glycine decarboxylase complex (GCV1, GCV2, and GCV3). Based on these and other observations, we propose a model for how cells balance the need to supplement their one-carbon pools when charged folates are limiting or when glycine is in excess. We also propose that under normal conditions, cytoplasmic 5,10-CH(2)-H(4)folate is mainly directed to generating methyl groups via methionine, whereas one-carbon units generated from glycine in mitochondria are more directed to purine biosynthesis. When glycine is in excess, 5, 10-CH(2)-H(4)folate is decreased, and the regulation loop shifts the balance of generation of one-carbon units into the mitochondrion. (+info)Nitrite reductase gene enrichment improves assimilation of NO(2) in Arabidopsis. (6/33)
Transgenic plants of Arabidopsis bearing the spinach (Spinacia oleracea) nitrite reductase (NiR, EC 1.7.7.1) gene that catalyzes the six-electron reduction of nitrite to ammonium in the second step of the nitrate assimilation pathway were produced by use of the cauliflower mosaic virus 35S promoter and nopaline synthase terminator. Integration of the gene was confirmed by a genomic polymerase chain reaction (PCR) and Southern-blot analysis; its expression by a reverse transcriptase-PCR and two-dimensional polyacrylamide gel electrophoresis western-blot analysis; total (spinach + Arabidopsis) NiR mRNA content by a competitive reverse transcriptase-PCR; localization of NiR activity (NiRA) in the chloroplast by fractionation analysis; and NO(2) assimilation by analysis of the reduced nitrogen derived from NO(2) (NO(2)-RN). Twelve independent transgenic plant lines were characterized in depth. Three positive correlations were found for NiR gene expression; between the total NiR mRNA and total NiR protein contents (r = 0.74), between the total NiR protein and NiRA (r = 0.71), and between NiRA and NO(2)-RN (r = 0.65). Of these twelve lines, four had significantly higher NiRA than the wild-type control (P < 0.01), and three had significantly higher NO(2)-RN (P < 0.01). Each of the latter three had one to two copies of spinach NiR cDNA per haploid genome. The NiR flux control coefficient for NO(2) assimilation was estimated to be about 0.4. A similar value was obtained for an NiR antisense tobacco (Nicotiana tabacum cv Xanthi XHFD8). The flux control coefficients of nitrate reductase and glutamine synthetase were much smaller than this value. Together, these findings indicate that NiR is a controlling enzyme in NO(2) assimilation by plants. (+info)Effects of breed, parity, and folic Acid supplement on the expression of folate metabolism genes in endometrial and embryonic tissues from sows in early pregnancy. (7/33)
Folic acid and glycine are factors of great importance in early gestation. In sows, folic acid supplement can increase litter size through a decrease in embryonic mortality, while glycine, the most abundant amino acid in the sow oviduct, uterine, and allantoic fluids, is reported to act as an organic osmoregulator. In this study, we report the characterization of cytoplasmic serine hydroxymethyltransferase (cSHMT), T-protein, and vT-protein (variant T-protein) mRNA expression levels in endometrial and embryonic tissues in gestating sows on Day 25 of gestation according to the breed, parity, and folic acid + glycine supplementation. Expression levels of cSHMT, T-protein, and vT-protein mRNA in endometrial and embryonic tissues were performed using semiquantitative reverse transcription-polymerase chain reaction. We also report, for the first time, an alternative splicing event in the porcine T-protein gene. Results showed that a T-protein splice variant, vT-protein, is present in all the tested sow populations. Further characterizations revealed that this T-protein splice variant contains a coding intron that can adopt a secondary structure. Results demonstrated that cSHMT mRNA expression levels were significantly higher in sows receiving the folic acid + glycine supplementation, independently of the breed or parity and in both endometrial and embryonic tissues. Upon receiving the same treatment, the vT-protein and T-protein mRNA expression levels were significantly reduced in the endometrial tissue of Yorkshire-Landrace sows only. These results indicate that modulation of specific gene expression levels in endometrial and embryonic tissues of sows in early gestation could be one of the mechanism involved with the role of folic acid on improving swine reproduction traits. (+info)Probing the H-protein-induced conformational change and the function of the N-terminal region of Escherichia coli T-protein of the glycine cleavage system by limited proteolysis. (8/33)
T-protein, a component of the glycine cleavage system, catalyzes a tetrahydrofolate-dependent reaction. Previously, we reported a conformational change of Escherichia coli T-protein upon interacting with E. coli H-protein (EH), showing an important role for the N-terminal region of the T-protein in the interaction. To further investigate the T-protein catalysis, the wild type (ET) and mutants were subjected to limited proteolysis. ET was favorably cleaved at Lys(81), Lys(154), Lys(288), and Lys(360) by lysylendopeptidase and the cleavages at Lys(81) and Lys(288) were strongly prevented by EH. Although ET was highly resistant to trypsinolysis, the mutant with an N-terminal 7-residue deletion (ETDelta7) was quite susceptible and instantly cleaved at Arg(16) accompanied by the rapid degradation of the resulting C-terminal fragment, indicating that the cleavage at Arg(16) is the trigger for the C-terminal fragmentation. EH showed no protection from the N-terminal cleavage, although substantial protection from the C-terminal fragmentation was observed. The replacement of Leu(6) of ET with alanine resulted in a similar sensitivity to trypsin as ETDelta7. These results suggest that the N-terminal region of ET functions as a molecular "hasp" to hold ET in the compact form required for the proper association with EH. Leu(6) seems to play a central role in the hasp function. Interestingly, Lys(360) of ET was susceptible to proteolysis even after the stabilization of the entire molecule of ET by EH, indicating its location at the surface of the ET-EH complex. Together with the buried position of Lys(81) in the complex and previous results on folate binding sites, these results suggest the formation of a folate-binding cavity via the interaction of ET with EH. The polyglutamyl tail of the folate substrate may be inserted into the bosom of the cavity leaving the pteridine ring near the entrance of the cavity in the context of the catalytic reaction. (+info)
OriGene - AMT (NM 000481) cDNA Clone
Anti-Aminomethyltransferase antibody (ab76387) | Abcam
Crystal structure of DMGO provides a prototype for a new tetrahydrofolate-binding fold | Biochemical Society Transactions
Q72LB1 | SWISS-MODEL Repository
Glycine cleavage system - Wikipedia
Variant non ketotic hyperglycinemia is caused by mutations in |i|LIAS|/i|, |i|BOLA3|/i| and the novel gene |i|GLRX5|/i| -...
Nonketotic hyperglycinemia: spectrum of imaging findings with emphasis on diffusion-weighted imaging | SpringerLink
Promoter Characterization and Constitutive Expression of the Escherichia coli gcvR Gene | Journal of Bacteriology
A0QYG3 | SWISS-MODEL Repository
Ketotic hyperglycinemia definition | Drugs.com
DMOZ - Health: Conditions and Diseases: Nutritional and Metabolic Disorders: Inherited: Nonketotic Hyperglycinemia
Light-dependent and tissue-specific expression of the H-protein of the glycine decarboxylase complex | [email protected]
One carbon enzyme systems Serine hydroxymethyltransferase (SHMT) and Glycine cleavage complex (GCV) | LAMP
The Razor high-throughput peptide cleavage system from CEM | Laboratory Talk
Drosophila pumpless protein
Summary Report | CureHunter
HYPERGLYCINEMIA, LACTIC ACIDOSIS, AND SEIZURES; HGCLAS | MENDELIAN.CO
ECMDB: Glycine (ECMDB00123) (M2MDB000046)
Leukoencephalopathy with cysts and hyperglycinemia may result from NFU1 deficiency. - PubMed - NCBI
Diana Hotel: 2018 Room Prices, Deals & Reviews | Expedia
Hyperglycinemia - Wikipedia
Neurobiology of a Mutation in Glycine Metabolism in Psychotic Disorders - Tabular View - ClinicalTrials.gov
GDCSPA - Glycine dehydrogenase (decarboxylating) A, mitochondrial precursor - Flaveria pringlei - GDCSPA gene & protein
ENZYME entry 6.3.1.20
Hyperosmolar Hyperglycemic Nonketotic Syndrome and Diabetes | HowStuffWorks
CEM Corporation
Miami Childrens Health System renamed to honor Nicklaus family - Miamis Community News
EMB3003 protein (Arabidopsis thaliana) - STRING network view
New Saccharomyces Sequences 01/24/04
New Saccharomyces Sequences 11/16/96
Nonketotic Hyperosmolar ComaInterActive Health
Glycine decarboxylase in Rhodopseudomonas spheroides and in rat liver mitochondria | Biochemical Journal
Glycine decarboxylase is a transcriptional target of MYCN required for neuroblastoma cell proliferation and tumorigenicity<...
Article - Nonketotic hyperglycemia-induced hemichorea-hemiballism
Hospitals in Deming, NM (NM) - Hospital Ratings, Cost, Length of Stay, Affiliated Physicians, More...
Medical Xpress - diabetes prevalence
A biochemical analysis of the interaction of victorin and oats
Prairie Pest Monitoring Network Blog: Weekly Update (June 1, 2016; Wk 05) - Pea leaf weevil
KEGG BRITE: KEGG Orthology (KO) - Hydrogenovibrio crunogenus
Prairie Pest Monitoring Network Blog: Weekly Update (May 18, 2016; Wk 03) - Pea leaf weevil
knodel.pea leaf weevil - Crop & Pest Report
ECO401 Economics Assignment 01 spring 2021 Solution / Discussion Due Date: 11-05-2021 - Virtual University of Pakistan
Aminomethyltransferase
... is an enzyme that catabolizes the creation of methylenetetrahydrofolate. It is part of the glycine ...
GCSH
... a tetrahydrofolate-requiring aminomethyltransferase enzyme), and L protein (a lipoamide dehydrogenase). The H protein shuttles ...
GCST
... can stand for: New standard tuning "Glycine cleavage system T protein", another name for aminomethyltransferase This ...
AMT
... a synthetic psychedelic of the tryptamine family Aminomethyltransferase, gene for an enzyme that breaks down glycine Air Motion ...
Rickettsiella
... glycine cleavage system aminomethyltransferase GcvT, M3 family metallopeptidase, lysm peptidoglycan-binding domain-containing ...
List of EC numbers (EC 2)
... aminomethyltransferase EC 2.1.2.11: 3-methyl-2-oxobutanoate hydroxymethyltransferase EC 2.1.2.12: now EC 2.1.1.74 EC 2.1.2.13: ...
List of MeSH codes (D08)
... aminomethyltransferase MeSH D08.811.913.555.400.300 - glutamate formimidoyltransferase MeSH D08.811.913.555.400.500 - glycine ... aminomethyltransferase MeSH D08.811.600.391.150 - dihydrolipoamide dehydrogenase MeSH D08.811.600.391.175 - glycine ...
Diplorickettsia massiliensis
... glycine cleavage system aminomethyltransferase GcvT, M3 family metallopeptidase, lysm peptidoglycan-binding domain-containing ...
List of MeSH codes (D05)
... aminomethyltransferase MeSH D05.500.562.452.150 - dihydrolipoamide dehydrogenase MeSH D05.500.562.452.175 - glycine ...
Aminomethyltransferase | Profiles RNS
"Aminomethyltransferase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... This graph shows the total number of publications written about "Aminomethyltransferase" by people in this website by year, and ... Below are the most recent publications written about "Aminomethyltransferase" by people in Profiles. ... whether "Aminomethyltransferase" was a major or minor topic of these publications. ...
MedlinePlus: Genes
PDPR pyruvate dehydrogenase phosphatase regulatory subunit [Homo sapiens (human)] - Gene - NCBI
GCV_T; Aminomethyltransferase folate-binding domain. pfam08669. Location:786 → 852. GCV_T_C; Glycine cleavage T-protein C- ... GCV_T; Aminomethyltransferase folate-binding domain. pfam08669. Location:648 → 752. GCV_T_C; Glycine cleavage T-protein C- ... GCV_T; Aminomethyltransferase folate-binding domain. pfam08669. Location:346 → 450. GCV_T_C; Glycine cleavage T-protein C- ... GCV_T; Aminomethyltransferase folate-binding domain. pfam08669. Location:786 → 852. GCV_T_C; Glycine cleavage T-protein C- ...
KEGG REACTION: R01221
SCOPe 2.08: Domain d1vloa3: 1vlo A:365-367
Browse ORF cDNA clones by gene type protein-coding, letter g, page 1
HOMD :: SEQF1671
BiGG Reaction FOMETRi in iEKO11 1354
Nitrogen metabolism - Yeast Metabolome Database
GSE34156 NOD2 LIGAND VS NOD2 AND TLR1 TLR2 LIGAND 6H TREATED MONOCYTE UP
Code System Concept
The AMT gene homepage - Malaysian Node of the Human Variome Project Database
Words in 22 letters without X
List of EC numbers (EC 2)
Glycine and Serine metabolism
EC 2.1.2.10
Accepted name: aminomethyltransferase. Reaction: [protein]-S8-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]- ... Other name(s): S-aminomethyldihydrolipoylprotein:(6S)-tetrahydrofolate aminomethyltransferase (ammonia-forming); T-protein; ... Systematic name: [protein]-S8-aminomethyldihydrolipoyllysine:tetrahydrofolate aminomethyltransferase (ammonia-forming). ...
Aligments for a candidate for gcvT in Bacteroides thetaiotaomicron VPI-5482
Align Aminomethyltransferase; EC 2.1.2.10; Glycine cleavage system T protein (uncharacterized) to candidate 354110 BT4584 ... Align candidate 354110 BT4584 (putative aminomethyltransferase (NCBI ptt file)) to HMM TIGR00528 (gcvT: glycine cleavage system ... Query= curated2:B2RI74 (362 letters) >lcl,FitnessBrowser__Btheta:354110 BT4584 putative aminomethyltransferase (NCBI ptt file) ... 354110 BT4584 putative aminomethyltransferase (NCBI ptt file) # score bias c-Evalue i-Evalue hmmfrom hmm to alifrom ali to ...
Cannabis Compound Database: Showing Compound Card for Tetrahydrofolic acid (CDB005115)
Model Search | BioModels
Pre GI: CDS description
Network Portal - Gene VNG0459G
"sequence id","alias","species","description",...
The Donner Party (2009 film) - Onion Wiki
Search: protein class:Congenital disorders of amino acid metabolism AND with antibodies:Yes - The Human Protein Atlas
YJR139C 267.488705 INESSENTIAL HOM6 "Homoserine dehydrogenase (L-homoserine:NADP oxidoreductase),5-amino-6-(5...
DeCS 2018 - July 31, 2018 version
View source for Guidelines for new Molecular Functions - GO Wiki
2.101
- A component, with EC 2.1.2.10, aminomethyltransferase and EC 1.8.1.4, dihydrolipoyl dehydrogenanse, of the glycine cleavage system, previously known as glycine synthase. (unipr.it)
Enzyme1
- Aminomethyltransferase is an enzyme that catabolizes the creation of methylenetetrahydrofolate. (onionsearchengine.com)
Glycine cleavage1
- Mutation analysis of glycine decarboxylase, aminomethyltransferase and glycine cleavage system protein-H genes in 13 unrelated families with glycine encephalopathy. (moh.gov.my)