Purification and characterization of developmentally regulated AMP deaminase from Dictyostelium discoideum
AMP deaminase, the enzyme that catalyzes the conversion of adenosine monophosphate (AMP) to inosine monophosphate (IMP) and ammonia, was purified from the cellular slime mold, Dictyostelium discoideum in the nutrient-deprived state. The native enzyme had an apparent molecular weight of 199000 dalton...
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| Veröffentlicht in: | Differentiation (London) 1991-04, Vol.46 (3), p.153-160 |
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| creator | Malliaros, David P. Kozwich, Diane L. Jahngen, Edwin G.E. |
| description | AMP deaminase, the enzyme that catalyzes the conversion of adenosine monophosphate (AMP) to inosine monophosphate (IMP) and ammonia, was purified from the cellular slime mold,
Dictyostelium discoideum in the nutrient-deprived state. The native enzyme had an apparent molecular weight of 199000 daltons. Its apparent Km was 1.6
mM and its K
max was 1.0 μmol min
-1 mg
-1, as measured by the release of IMP From AMP. The enzyme, like other AMP deaminases, was found to be activated by ATP, and inhibited either by GTP or inorganic phosphate. It was also specific for the deamination of AMP. Deaminase activity was increased either when vegetative cells were placed in a nutrient-deprived medium (for up to 6 h) or when vegetative cells were treated with the drug hadacidin. In cells actively growing in complete media, enzyme activity was more non-specific, hydrolyzing adenosine as well as AMP. AMP deaminase in
D. discoideum appears to be stage-specific and developmentally regulated, possibly serving to regulate the adenylated nucleotide pool and the interconversion to guanylated nucleotides during early morphodifferentiation. |
| doi_str_mv | 10.1111/j.1432-0436.1991.tb00876.x |
| format | Article |
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Dictyostelium discoideum in the nutrient-deprived state. The native enzyme had an apparent molecular weight of 199000 daltons. Its apparent Km was 1.6
mM and its K
max was 1.0 μmol min
-1 mg
-1, as measured by the release of IMP From AMP. The enzyme, like other AMP deaminases, was found to be activated by ATP, and inhibited either by GTP or inorganic phosphate. It was also specific for the deamination of AMP. Deaminase activity was increased either when vegetative cells were placed in a nutrient-deprived medium (for up to 6 h) or when vegetative cells were treated with the drug hadacidin. In cells actively growing in complete media, enzyme activity was more non-specific, hydrolyzing adenosine as well as AMP. AMP deaminase in
D. discoideum appears to be stage-specific and developmentally regulated, possibly serving to regulate the adenylated nucleotide pool and the interconversion to guanylated nucleotides during early morphodifferentiation.</description><identifier>ISSN: 0301-4681</identifier><identifier>EISSN: 1432-0436</identifier><identifier>DOI: 10.1111/j.1432-0436.1991.tb00876.x</identifier><identifier>PMID: 1916064</identifier><language>eng</language><publisher>Oxford, UK: Elsevier B.V</publisher><subject>Adenosine Triphosphate - pharmacology ; AMP Deaminase - chemistry ; AMP Deaminase - isolation & purification ; AMP Deaminase - metabolism ; Animals ; Antibiotics, Antineoplastic - pharmacology ; Biochemistry. Physiology. Immunology. Molecular biology ; Biological and medical sciences ; Chromatography ; Cyclophosphamide - pharmacology ; Dactinomycin - pharmacology ; Dictyostelium - enzymology ; Dictyostelium - growth & development ; Dictyostelium discoideum ; Dose-Response Relationship, Drug ; Freeze Drying ; Fundamental and applied biological sciences. Psychology ; Gene Expression Regulation, Enzymologic ; Glycine - analogs & derivatives ; Glycine - pharmacology ; Guanosine Triphosphate - pharmacology ; Invertebrates ; Molecular Weight ; Phosphates - pharmacology ; Protozoa ; Sonication ; Substrate Specificity</subject><ispartof>Differentiation (London), 1991-04, Vol.46 (3), p.153-160</ispartof><rights>1991 International Society of Differentiation</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4903-68bd1db3630b7f847f6c7b6109bd0b862472b912643fb98de87c839f995940c83</citedby><cites>FETCH-LOGICAL-c4903-68bd1db3630b7f847f6c7b6109bd0b862472b912643fb98de87c839f995940c83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0301468111602454$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4429766$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1916064$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Malliaros, David P.</creatorcontrib><creatorcontrib>Kozwich, Diane L.</creatorcontrib><creatorcontrib>Jahngen, Edwin G.E.</creatorcontrib><title>Purification and characterization of developmentally regulated AMP deaminase from Dictyostelium discoideum</title><title>Differentiation (London)</title><addtitle>Differentiation</addtitle><description>AMP deaminase, the enzyme that catalyzes the conversion of adenosine monophosphate (AMP) to inosine monophosphate (IMP) and ammonia, was purified from the cellular slime mold,
Dictyostelium discoideum in the nutrient-deprived state. The native enzyme had an apparent molecular weight of 199000 daltons. Its apparent Km was 1.6
mM and its K
max was 1.0 μmol min
-1 mg
-1, as measured by the release of IMP From AMP. The enzyme, like other AMP deaminases, was found to be activated by ATP, and inhibited either by GTP or inorganic phosphate. It was also specific for the deamination of AMP. Deaminase activity was increased either when vegetative cells were placed in a nutrient-deprived medium (for up to 6 h) or when vegetative cells were treated with the drug hadacidin. In cells actively growing in complete media, enzyme activity was more non-specific, hydrolyzing adenosine as well as AMP. AMP deaminase in
D. discoideum appears to be stage-specific and developmentally regulated, possibly serving to regulate the adenylated nucleotide pool and the interconversion to guanylated nucleotides during early morphodifferentiation.</description><subject>Adenosine Triphosphate - pharmacology</subject><subject>AMP Deaminase - chemistry</subject><subject>AMP Deaminase - isolation & purification</subject><subject>AMP Deaminase - metabolism</subject><subject>Animals</subject><subject>Antibiotics, Antineoplastic - pharmacology</subject><subject>Biochemistry. Physiology. Immunology. Molecular biology</subject><subject>Biological and medical sciences</subject><subject>Chromatography</subject><subject>Cyclophosphamide - pharmacology</subject><subject>Dactinomycin - pharmacology</subject><subject>Dictyostelium - enzymology</subject><subject>Dictyostelium - growth & development</subject><subject>Dictyostelium discoideum</subject><subject>Dose-Response Relationship, Drug</subject><subject>Freeze Drying</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Glycine - analogs & derivatives</subject><subject>Glycine - pharmacology</subject><subject>Guanosine Triphosphate - pharmacology</subject><subject>Invertebrates</subject><subject>Molecular Weight</subject><subject>Phosphates - pharmacology</subject><subject>Protozoa</subject><subject>Sonication</subject><subject>Substrate Specificity</subject><issn>0301-4681</issn><issn>1432-0436</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkE2P1SAYhYnRjNfRn2DSGOOuFVoGiguTyVznIxnjLHRN-HhRbmi5QjvO9ddL05txq2wgnPMeDg9CbwhuSFnvdw2hXVtj2rGGCEGaSWPcc9Y8PEGbR-kp2uAOk5qynjxHL3Le4eJiLTlBJ0QQhhndoN3dnLzzRk0-jpUabWV-qKTMBMn_Xi-jqyzcQ4j7AcZJhXCoEnyfg5rAVuef74qqBj-qDJVLcai23kyHmCcIfh4q67OJ3sI8vETPnAoZXh33U_Tt8tPXi-v69svVzcX5bW2owF3Nem2J1R3rsOaup9wxwzUjWGiLdelPeasFaRntnBa9hZ6bvhNOiDNBcTmeondr7j7FnzPkSQ6lA4SgRohzloQRzilejB9Wo0kx5wRO7pMfVDpIguUCWu7kQlMuNOUCWh5By4cy_Pr4yqwHsH9HV7JFf3vUVTYquKRG4_OjjdJWcMaK7eNq--UDHP6jgNzeXJKzrgRs1wAoSO89JJmNh9GA9QnMJG30__KdPwpYse0</recordid><startdate>199104</startdate><enddate>199104</enddate><creator>Malliaros, David P.</creator><creator>Kozwich, Diane L.</creator><creator>Jahngen, Edwin G.E.</creator><general>Elsevier B.V</general><general>Blackwell Publishing Ltd</general><general>Blackwell</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>M81</scope><scope>P64</scope></search><sort><creationdate>199104</creationdate><title>Purification and characterization of developmentally regulated AMP deaminase from Dictyostelium discoideum</title><author>Malliaros, David P. ; Kozwich, Diane L. ; Jahngen, Edwin G.E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4903-68bd1db3630b7f847f6c7b6109bd0b862472b912643fb98de87c839f995940c83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Adenosine Triphosphate - pharmacology</topic><topic>AMP Deaminase - chemistry</topic><topic>AMP Deaminase - isolation & purification</topic><topic>AMP Deaminase - metabolism</topic><topic>Animals</topic><topic>Antibiotics, Antineoplastic - pharmacology</topic><topic>Biochemistry. Physiology. Immunology. Molecular biology</topic><topic>Biological and medical sciences</topic><topic>Chromatography</topic><topic>Cyclophosphamide - pharmacology</topic><topic>Dactinomycin - pharmacology</topic><topic>Dictyostelium - enzymology</topic><topic>Dictyostelium - growth & development</topic><topic>Dictyostelium discoideum</topic><topic>Dose-Response Relationship, Drug</topic><topic>Freeze Drying</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Glycine - analogs & derivatives</topic><topic>Glycine - pharmacology</topic><topic>Guanosine Triphosphate - pharmacology</topic><topic>Invertebrates</topic><topic>Molecular Weight</topic><topic>Phosphates - pharmacology</topic><topic>Protozoa</topic><topic>Sonication</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Malliaros, David P.</creatorcontrib><creatorcontrib>Kozwich, Diane L.</creatorcontrib><creatorcontrib>Jahngen, Edwin G.E.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Differentiation (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Malliaros, David P.</au><au>Kozwich, Diane L.</au><au>Jahngen, Edwin G.E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of developmentally regulated AMP deaminase from Dictyostelium discoideum</atitle><jtitle>Differentiation (London)</jtitle><addtitle>Differentiation</addtitle><date>1991-04</date><risdate>1991</risdate><volume>46</volume><issue>3</issue><spage>153</spage><epage>160</epage><pages>153-160</pages><issn>0301-4681</issn><eissn>1432-0436</eissn><abstract>AMP deaminase, the enzyme that catalyzes the conversion of adenosine monophosphate (AMP) to inosine monophosphate (IMP) and ammonia, was purified from the cellular slime mold,
Dictyostelium discoideum in the nutrient-deprived state. The native enzyme had an apparent molecular weight of 199000 daltons. Its apparent Km was 1.6
mM and its K
max was 1.0 μmol min
-1 mg
-1, as measured by the release of IMP From AMP. The enzyme, like other AMP deaminases, was found to be activated by ATP, and inhibited either by GTP or inorganic phosphate. It was also specific for the deamination of AMP. Deaminase activity was increased either when vegetative cells were placed in a nutrient-deprived medium (for up to 6 h) or when vegetative cells were treated with the drug hadacidin. In cells actively growing in complete media, enzyme activity was more non-specific, hydrolyzing adenosine as well as AMP. AMP deaminase in
D. discoideum appears to be stage-specific and developmentally regulated, possibly serving to regulate the adenylated nucleotide pool and the interconversion to guanylated nucleotides during early morphodifferentiation.</abstract><cop>Oxford, UK</cop><pub>Elsevier B.V</pub><pmid>1916064</pmid><doi>10.1111/j.1432-0436.1991.tb00876.x</doi><tpages>8</tpages></addata></record> |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Adenosine Triphosphate - pharmacology AMP Deaminase - chemistry AMP Deaminase - isolation & purification AMP Deaminase - metabolism Animals Antibiotics, Antineoplastic - pharmacology Biochemistry. Physiology. Immunology. Molecular biology Biological and medical sciences Chromatography Cyclophosphamide - pharmacology Dactinomycin - pharmacology Dictyostelium - enzymology Dictyostelium - growth & development Dictyostelium discoideum Dose-Response Relationship, Drug Freeze Drying Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Enzymologic Glycine - analogs & derivatives Glycine - pharmacology Guanosine Triphosphate - pharmacology Invertebrates Molecular Weight Phosphates - pharmacology Protozoa Sonication Substrate Specificity |
| title | Purification and characterization of developmentally regulated AMP deaminase from Dictyostelium discoideum |
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