Purification and properties of an acid phosphomonoesterase from Neurospora crassa
dc.contributor.author | Kuo, Mau-Huai | en_US |
dc.contributor.author | Blumenthal, Harold J. | en_US |
dc.date.accessioned | 2006-04-13T14:57:01Z | |
dc.date.available | 2006-04-13T14:57:01Z | |
dc.date.issued | 1961-09-02 | en_US |
dc.identifier.citation | Kuo, Mau-Huai, Blumenthal, Harold J. (1961/09/02)."Purification and properties of an acid phosphomonoesterase from Neurospora crassa." Biochimica et Biophysica Acta 52(1): 13-29. <http://hdl.handle.net/2027.42/32350> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B73G9-486T547-NB/2/ce1bcd151552f8327c5bc1c380a523a9 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/32350 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=14460641&dopt=citation | en_US |
dc.description.abstract | An acid phosphomonoesterase was purified 1400-fold from mycelium of Neurospora crassa with a 40% recovery. The enzyme had a pH maximum of 5.6 with [beta]-glycerol phosphate or glucosamine 6-phosphate as substrates, and cation or cofactor requirements could not be demonstrated. The substrate specificity of the enzyme was studied, using 46 compounds, [alpha]-glycerol phosphate being hydrolyzed most rapidly. When a free amino group and a phosphomonoester group were attached to adjacent carbon atoms, the compound either would not serve as a substrate or was slowly hydrolyzed. Deoxyguanosine 5'-phosphate and thymidine 5'-phosphate were not hydrolyzed although all other nucleoside monophosphates tested were able to serve as substrates. Fluoride and (+)tartrate were competitive inhibitors for the hydrolysis of [beta]-glycerol phosphate, while concentrations of thyroxine that completely inhibited the hydrolysis of acetyl phosphate did not affect the hydrolysis of [beta]-glycerol phosphate or p-nitrophenyl phosphate. No evidence was obtained for the presence of more than one phosphomonoesterase in the purified enzyme preparation. These properties distinguish this enzyme from previously described microbial phosphomonoesterases. The possibility of this acid phosphomonoesterase participating in metabolic control systems in N. crassa was discussed. | en_US |
dc.format.extent | 1105579 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Purification and properties of an acid phosphomonoesterase from Neurospora crassa | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Bacteriology, The University of Michigan Medical School, Ann Arbor, Mich., U.S.A. | en_US |
dc.contributor.affiliationum | Department of Bacteriology, The University of Michigan Medical School, Ann Arbor, Mich., U.S.A. | en_US |
dc.identifier.pmid | 14460641 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/32350/1/0000421.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0006-3002(61)90899-X | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.