Feedback Inhibition of l-Glutamine d-Fructose 6-Phosphate Amidotransferase by Uridine Diphosphate N-Acetylglucosamine in Neurospora crassa
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| Published in | Journal of Bacteriology Vol. 103; no. 3; pp. 588 - 594 |
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| Main Authors | , , |
| Format | Journal Article |
| Language | English |
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United States
American Society for Microbiology
01.09.1970
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| AbstractList | The enzyme,
l
-glutamine
d
-fructose 6-phosphate amidotransferase (EC 2.6.1.16) of
Neurospora crassa
, which catalyzes the formation of glucosamine 6-phosphate was shown to be subject to feedback inhibition by uridine diphosphate
N
-acetyl-
d
-glucosamine (UDP-GlcNAc). The conclusion is based on the following observations. UDP-GlcNAc, the direct precursor of chitin, did not accumulate in the cell even when its utilization for the synthesis of cell wall chitin was interrupted by the antibiotic polyoxin D, a competitive inhibitor of the chitin synthetase (EC 2.4.1.16). Furthermore, the cellular level of UDP-GlcNAc rose in a short period of time when the amidotransferase was bypassed in vivo by the addition of glucosamine to the growing medium of the fungus. The amidotransferase was purified from
N. crassa
approximately 85-fold. Kinetic studies showed that UDP-GlcNAc was a potent and specific inhibitor of the amidotransferase, and that it did not alter the Michaelis constant for either
l
-glutamine or
d
-fructose 6-phosphate, suggesting that the inhibitor binds at a site on the enzyme distinct from the active site. The enzyme, l-glutamine d-fructose 6-phosphate amidotransferase (EC 2.6.1.16) of Neurospora crassa, which catalyzes the formation of glucosamine 6-phosphate was shown to be subject to feedback inhibition by uridine diphosphate N-acetyl-d-glucosamine (UDP-GlcNAc). The conclusion is based on the following observations. UDP-GlcNAc, the direct precursor of chitin, did not accumulate in the cell even when its utilization for the synthesis of cell wall chitin was interrupted by the antibiotic polyoxin D, a competitive inhibitor of the chitin synthetase (EC 2.4.1.16). Furthermore, the cellular level of UDP-GlcNAc rose in a short period of time when the amidotransferase was bypassed in vivo by the addition of glucosamine to the growing medium of the fungus. The amidotransferase was purified from N. crassa approximately 85-fold. Kinetic studies showed that UDP-GlcNAc was a potent and specific inhibitor of the amidotransferase, and that it did not alter the Michaelis constant for either l-glutamine or d-fructose 6-phosphate, suggesting that the inhibitor binds at a site on the enzyme distinct from the active site. The enzyme, l-glutamine d-fructose 6-phosphate amidotransferase (EC 2.6.1.16) of Neurospora crassa, which catalyzes the formation of glucosamine 6-phosphate was shown to be subject to feedback inhibition by uridine diphosphate N-acetyl-d-glucosamine (UDP-GlcNAc). The conclusion is based on the following observations. UDP-GlcNAc, the direct precursor of chitin, did not accumulate in the cell even when its utilization for the synthesis of cell wall chitin was interrupted by the antibiotic polyoxin D, a competitive inhibitor of the chitin synthetase (EC 2.4.1.16). Furthermore, the cellular level of UDP-GlcNAc rose in a short period of time when the amidotransferase was bypassed in vivo by the addition of glucosamine to the growing medium of the fungus. The amidotransferase was purified from N. crassa approximately 85-fold. Kinetic studies showed that UDP-GlcNAc was a potent and specific inhibitor of the amidotransferase, and that it did not alter the Michaelis constant for either l-glutamine or d-fructose 6-phosphate, suggesting that the inhibitor binds at a site on the enzyme distinct from the active site.The enzyme, l-glutamine d-fructose 6-phosphate amidotransferase (EC 2.6.1.16) of Neurospora crassa, which catalyzes the formation of glucosamine 6-phosphate was shown to be subject to feedback inhibition by uridine diphosphate N-acetyl-d-glucosamine (UDP-GlcNAc). The conclusion is based on the following observations. UDP-GlcNAc, the direct precursor of chitin, did not accumulate in the cell even when its utilization for the synthesis of cell wall chitin was interrupted by the antibiotic polyoxin D, a competitive inhibitor of the chitin synthetase (EC 2.4.1.16). Furthermore, the cellular level of UDP-GlcNAc rose in a short period of time when the amidotransferase was bypassed in vivo by the addition of glucosamine to the growing medium of the fungus. The amidotransferase was purified from N. crassa approximately 85-fold. Kinetic studies showed that UDP-GlcNAc was a potent and specific inhibitor of the amidotransferase, and that it did not alter the Michaelis constant for either l-glutamine or d-fructose 6-phosphate, suggesting that the inhibitor binds at a site on the enzyme distinct from the active site. Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2014 by the American Society for Microbiology. For an alternate route to JB .asm.org, visit: JB |
| Author | Kazuo Kakiki Tomomasa Misato Akira Endo |
| AuthorAffiliation | Institute for Physical and Chemical Research, Saitama, Japan Fermentation Research Laboratories, Sankyo Company Ltd., Shinagawa-ku, Tokyo, Japan |
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| Cites_doi | 10.1146/annurev.mi.20.100166.001345 10.1016/S0021-9258(18)97661-1 10.1016/S0021-9258(19)52451-6 10.1016/S0021-9258(18)70655-8 10.1146/annurev.bi.35.070166.000505 10.1016/S0021-9258(18)97662-3 10.1016/S0021-9258(18)70653-4 10.1016/S0021-9258(18)69933-8 10.1016/0006-291X(69)90870-5 10.1073/pnas.52.2.371 10.1016/S0021-9258(18)95943-0 10.1016/S0021-9258(18)97402-8 10.1038/188741a0 10.1016/0304-4165(66)90154-1 |
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| References | Pogell B. M. (p_16) 1959; 228 Horecker B. L. (p_8) 1966; 20 Strange R. E. (p_17) 1960; 138 Endo A. (p_4) 1969; 37 Ghosh S. G. (p_5) 1960; 235 Mayer R. M. (p_14) 1965; 240 Atkinson D. H. (p_1) 1966; 35 Strominger J. L. (p_18) 1959; 234 Lovett J. S. (p_12) 1960; 47 Kornfeld S. (p_11) 1964; 52 Vogel H. J. (p_19) 1956; 13 Lowry 0. (p_13) 1951; 193 Kornfeld R. (p_9) 1967; 242 Bernstein R. L. (p_2) 1966; 240 Clarke J. S. (p_3) 1961; 81 Glaser L. (p_6) 1965; 101 Kornfeld R. H. (p_10) 1966; 117 Melo A. (p_15) 1965; 240 Glaser L. (p_7) 1957; 228 5330665 - Biochim Biophys Acta. 1966 Mar 28;117(1):79-87 14329291 - Biochim Biophys Acta. 1965 Mar 1;101:6-15 14482181 - Biochem J. 1961 Oct;81:1-8 14206604 - Proc Natl Acad Sci U S A. 1964 Aug;52:371-9 13827775 - J Biol Chem. 1960 May;235:1265-73 13475353 - J Biol Chem. 1957 Oct;228(2):701-12 14253442 - J Biol Chem. 1965 Jan;240:398-405 13475355 - J Biol Chem. 1957 Oct;228(2):729-42 4961641 - J Biol Chem. 1967 Jul 10;242(13):3135-41 13672971 - J Biol Chem. 1959 Jul;234(7):1822-7 5353899 - Biochem Biophys Res Commun. 1969 Nov 6;37(4):718-22 14907713 - J Biol Chem. 1951 Nov;193(1):265-75 14299608 - J Biol Chem. 1965 May;240:1900-4 14253441 - J Biol Chem. 1965 Jan;240:391-7 5330234 - Annu Rev Microbiol. 1966;20:253-90 |
| References_xml | – volume: 20 start-page: 253 year: 1966 ident: p_8 article-title: The biosynthesis of bacterial polysaccharides. Annu publication-title: Rev. Microbiol. doi: 10.1146/annurev.mi.20.100166.001345 – volume: 240 start-page: 391 year: 1966 ident: p_2 article-title: Control aspects of uridine 5'-diphosphate glucose and thymidine 5'-diphosphate glucose synthesis by microbial enzymes publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)97661-1 – volume: 101 start-page: 6 year: 1965 ident: p_6 article-title: The synthesis of teichoic acid. IV. On the regulation of cytidine 5'-diphosphateglycerol concentration publication-title: Biochim. Biophys. Acta – volume: 13 start-page: 42 year: 1956 ident: p_19 article-title: A convenient growth medium for Newuospora (medium N) publication-title: Microbial Genet. Bull. – volume: 193 start-page: 265 year: 1951 ident: p_13 article-title: Protein measurement with the Folin phenol reagent publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)52451-6 – volume: 228 start-page: 729 year: 1957 ident: p_7 article-title: The synthesis of chitin in cell-free extracts of Neurospora crassa publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)70655-8 – volume: 35 start-page: 85 year: 1966 ident: p_1 article-title: Regulation of enzyme activity. Annu publication-title: Rev. Biochem. doi: 10.1146/annurev.bi.35.070166.000505 – volume: 240 start-page: 398 year: 1965 ident: p_15 article-title: The nucleotide specificity and feedback control of thymidine diphosphate D-glucose pyrophosphorylase publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)97662-3 – volume: 228 start-page: 701 year: 1959 ident: p_16 article-title: Enzymatic synthesis of glucosamine 6-phosphate in rat liver publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)70653-4 – volume: 234 start-page: 1822 year: 1959 ident: p_18 article-title: Uridine diphosphoacetylglucosamine pyrophosphorylase publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)69933-8 – volume: 37 start-page: 718 year: 1969 ident: p_4 article-title: Polyoxin D, a competitive inhibitor of UDP-N-acetylglucosamine: chitin N-acetylglucosaminyltransferase in Neurospora crassa publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/0006-291X(69)90870-5 – volume: 52 start-page: 371 year: 1964 ident: p_11 article-title: The feedback control of sugar nucleotide biosynthesis in liver publication-title: Proc. Nat. Acad. Sci. U.S.A. doi: 10.1073/pnas.52.2.371 – volume: 242 start-page: 3135 year: 1967 ident: p_9 article-title: Studies on L-glutamine D-fructose 6-phosphate amidotransferase. I. Feedback inhibition by uridine diphosphate N-acetylglucosamine publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)95943-0 – volume: 81 start-page: 1P year: 1961 ident: p_3 article-title: The regulation of amino sugar metabolism in Bacillus subtilis publication-title: Biochem. J. – volume: 47 start-page: 499 year: 1960 ident: p_12 article-title: The relation between biochemical and morphological differentiation in Blastocladiella emersonii. I. Enzymatic synthesis of glucosamine 6-phosphate publication-title: Phytopathology. – volume: 240 start-page: 1900 year: 1965 ident: p_14 article-title: Purification and properties of cytidine diphosphate D-glucose pyrophosphorylase from Salmonella paratyphi A publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)97402-8 – volume: 138 start-page: 741 year: 1960 ident: p_17 article-title: Hexosamine synthesis by cell-free extracts of various bacteria publication-title: Nature doi: 10.1038/188741a0 – volume: 235 start-page: 1265 year: 1960 ident: p_5 article-title: Glucosamine metabolism. V. Enzymatic synthesis of glucosamine 6-phosphate publication-title: J. Biol. Chem. – volume: 117 start-page: 79 year: 1966 ident: p_10 article-title: Control of synthesis of guanosine 5'-diphosphate D-mannose and guanosine 5'-diphosphate L-fucose in bacteria publication-title: Biochim. Biophys. Acta doi: 10.1016/0304-4165(66)90154-1 – reference: 5330234 - Annu Rev Microbiol. 1966;20:253-90 – reference: 14907713 - J Biol Chem. 1951 Nov;193(1):265-75 – reference: 14253442 - J Biol Chem. 1965 Jan;240:398-405 – reference: 14253441 - J Biol Chem. 1965 Jan;240:391-7 – reference: 5330665 - Biochim Biophys Acta. 1966 Mar 28;117(1):79-87 – reference: 14299608 - J Biol Chem. 1965 May;240:1900-4 – reference: 13827775 - J Biol Chem. 1960 May;235:1265-73 – reference: 13475353 - J Biol Chem. 1957 Oct;228(2):701-12 – reference: 14206604 - Proc Natl Acad Sci U S A. 1964 Aug;52:371-9 – reference: 14329291 - Biochim Biophys Acta. 1965 Mar 1;101:6-15 – reference: 5353899 - Biochem Biophys Res Commun. 1969 Nov 6;37(4):718-22 – reference: 13475355 - J Biol Chem. 1957 Oct;228(2):729-42 – reference: 13672971 - J Biol Chem. 1959 Jul;234(7):1822-7 – reference: 4961641 - J Biol Chem. 1967 Jul 10;242(13):3135-41 – reference: 14482181 - Biochem J. 1961 Oct;81:1-8 |
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Mendeley... The enzyme, l -glutamine d -fructose 6-phosphate amidotransferase (EC 2.6.1.16) of Neurospora crassa , which catalyzes the formation of glucosamine 6-phosphate... The enzyme, l-glutamine d-fructose 6-phosphate amidotransferase (EC 2.6.1.16) of Neurospora crassa, which catalyzes the formation of glucosamine 6-phosphate... |
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| SubjectTerms | antagonists & inhibitors Anti-Bacterial Agents Anti-Bacterial Agents - pharmacology Binding Sites biosynthesis botany Carbon Isotopes Cell Wall Cell Wall - metabolism Chitin Chitin - biosynthesis drug effects Electrophoresis enzymology Feedback Glucosamine Glucosamine - metabolism Glucosamine - pharmacology Glucose Glucose - metabolism Glucosyltransferases Glucosyltransferases - antagonists & inhibitors Hexosephosphates Hexosephosphates - metabolism isolation & purification metabolism Neurospora Neurospora - drug effects Neurospora - enzymology Neurospora - metabolism pharmacology Physiology and Metabolism Plant Science and Plant Products plants Spectrophotometry Transaminases Transaminases - antagonists & inhibitors Transaminases - isolation & purification Transaminases - metabolism Uracil Nucleotides Uracil Nucleotides - metabolism Uracil Nucleotides - pharmacology |
| Title | Feedback Inhibition of l-Glutamine d-Fructose 6-Phosphate Amidotransferase by Uridine Diphosphate N-Acetylglucosamine in Neurospora crassa |
| URI | http://jb.asm.org/content/103/3/588.abstract https://cir.nii.ac.jp/crid/1871146593012189440 https://www.ncbi.nlm.nih.gov/pubmed/5474877 https://www.proquest.com/docview/2985991028 https://www.proquest.com/docview/47136608 https://www.proquest.com/docview/84715692 https://pubmed.ncbi.nlm.nih.gov/PMC248130 |
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