{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,11]],"date-time":"2025-11-11T22:13:08Z","timestamp":1762899188869},"reference-count":42,"publisher":"Microbiology Society","issue":"6","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2001,6,1]]},"DOI":"10.1099\/00221287-147-6-1525","type":"journal-article","created":{"date-parts":[[2015,8,26]],"date-time":"2015-08-26T14:15:00Z","timestamp":1440598500000},"page":"1525-1533","source":"Crossref","is-referenced-by-count":22,"title":["Substrate analysis and molecular cloning of the extracellular alkaline phosphatase of Streptomyces griseus The GenBank accession number for the sequence reported in this paper is AJ278740."],"prefix":"10.1099","volume":"147","author":[{"given":"Rute S","family":"Moura","sequence":"first","affiliation":[{"name":"Instituto de Biotecnolog\u0131\u0301a de Le\u00f3n INBIOTEC, Parque Cient\u0131\u0301fico de Le\u00f3n, Avda del Real no. 1, 24006 Le\u00f3n, Spain1"}]},{"given":"Juan F","family":"Mart\u0131\u0301n","sequence":"additional","affiliation":[{"name":"Area de Microbiolo\u0131\u0301a, Facultad de Ciencias Biol\u00f3gicas y Ambientales, Universidad de Le\u00f3n, 24071 Le\u00f3n, Spain2"},{"name":"Instituto de Biotecnolog\u0131\u0301a de Le\u00f3n INBIOTEC, Parque Cient\u0131\u0301fico de Le\u00f3n, Avda del Real no. 1, 24006 Le\u00f3n, Spain1"}]},{"given":"Alicia","family":"Mart\u0131\u0301n","sequence":"additional","affiliation":[{"name":"Area de Microbiolo\u0131\u0301a, Facultad de Ciencias Biol\u00f3gicas y Ambientales, Universidad de Le\u00f3n, 24071 Le\u00f3n, Spain2"}]},{"given":"Paloma","family":"Liras","sequence":"additional","affiliation":[{"name":"Area de Microbiolo\u0131\u0301a, Facultad de Ciencias Biol\u00f3gicas y Ambientales, Universidad de Le\u00f3n, 24071 Le\u00f3n, Spain2"},{"name":"Instituto de Biotecnolog\u0131\u0301a de Le\u00f3n INBIOTEC, Parque Cient\u0131\u0301fico de Le\u00f3n, Avda del Real no. 1, 24006 Le\u00f3n, Spain1"}]}],"member":"345","reference":[{"key":"R1","doi-asserted-by":"crossref","first-page":"4685","DOI":"10.1128\/JB.172.8.4685-4689.1990","article-title":"Nucleotide sequence of the Pseudomonas aeruginosa pho B gene, the regulatory gene for the phosphate regulon","volume":"172","author":"Anba","year":"1990","journal-title":"J Bacteriol"},{"key":"R2","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/0378-1119(90)90139-I","article-title":"Phosphate control of pab S gene transcription during candicidin biosynthesis","volume":"93","author":"Asturias","year":"1990","journal-title":"Gene"},{"key":"R3","doi-asserted-by":"crossref","first-page":"4551","DOI":"10.1128\/JB.173.15.4551-4557.1991","article-title":"Nucleotide sequence and characterization of the gene for secreted alkaline phosphatase from Lysobacter enzymogenes","volume":"173","author":"Au","year":"1991","journal-title":"J Bacteriol"},{"key":"R4","first-page":"2089","article-title":"The agarase gene ( dag A) of Streptomyces coelicolor A3(2): affinity purification and characterization of the cloned gene product","volume":"133","author":"Bibb","year":"1987","journal-title":"J Gen Microbiol"},{"key":"R5","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1007\/s002530051040","article-title":"Cloning, expression in Streptomyces lividans and biochemical characterization of a endo-beta-1,4-xylanase of Thermomonospora alba ULJB1 with cellulose-binding","volume":"48","author":"Blanco","year":"1997","journal-title":"Appl Microbiol Biotechnol"},{"key":"R6","doi-asserted-by":"crossref","first-page":"2181","DOI":"10.1111\/j.1365-2958.1991.tb02148.x","article-title":"Separate promoters direct expression of pho AIII, a member of the Bacillus subtilis alkaline phosphatase multigene family, during phosphate starvation and sporulation","volume":"5","author":"Chenust","year":"1991","journal-title":"Mol Microbiol"},{"key":"R7","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1038\/31159","article-title":"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence","volume":"393","author":"Cole","year":"1998","journal-title":"Nature"},{"key":"R8","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1007\/BF00633844","article-title":"Cloning and characterization of a gene of Streptomyces griseus that increases production of extracellular enzymes in several Streptomyces","volume":"222","author":"Daza","year":"1990","journal-title":"Mol Gen Genet"},{"key":"R9","doi-asserted-by":"crossref","first-page":"2041","DOI":"10.1099\/13500872-142-8-2041","article-title":"A Bacillus subtilis secreted phosphodiesterase\/alkaline phosphatase is the product of a Pho regulon gene, phoD","volume":"142","author":"Eder","year":"1996","journal-title":"Microbiology"},{"key":"R10","doi-asserted-by":"crossref","first-page":"6368","DOI":"10.1128\/JB.174.20.6368-6376.1992","article-title":"Cloning and nucleotide sequence of cel A1, an endo-beta-1,4-glucanase-encoding gene from Streptomyces halstedii JM8","volume":"174","author":"Ferna\u0301ndez-Abalos","year":"1992","journal-title":"J Bacteriol"},{"key":"R11","doi-asserted-by":"crossref","first-page":"4790","DOI":"10.1128\/JB.169.10.4790-4795.1987","article-title":"Characterization of Pi-repressible enzymes secreted in culture media by Neurospora crassa wild-type cells and null-type mutants","volume":"169","author":"Furukawa","year":"1987","journal-title":"J Bacteriol"},{"key":"R12","doi-asserted-by":"crossref","first-page":"2451","DOI":"10.1128\/JB.173.8.2451-2458.1991","article-title":"Characterization, expression in Streptomyces lividans , and processing of the amylase of Streptomyces griseus IMRU 3570: two different amylases are derived from the same gene by an intracellular processing mechanism","volume":"173","author":"Garc\u0131\u0301a-Gonza\u0301lez","year":"1991","journal-title":"J Bacteriol"},{"key":"R13","doi-asserted-by":"crossref","first-page":"7065","DOI":"10.1128\/JB.172.12.7065-7070.1990","article-title":"Extracellular Ca2+-dependent inducible alkaline phosphatase from the extremely halophilic archaebacterium Haloarcula marismortui","volume":"172","author":"Goldman","year":"1990","journal-title":"J Bacteriol"},{"key":"R14","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1139\/cjm-46-1-59","article-title":"Characterization and overproduction of the Escherichia coli app A encoded bifunctional enzyme that exhibits both phytase and acid phosphatase activities","volume":"46","author":"Golovan","year":"2000","journal-title":"Can J Microbiol"},{"key":"R15","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1107\/S0907444998015285","article-title":"Preliminary X-ray crystallographic analysis of a novel phytase from a Bacillus amyloliquefaciens strain","volume":"55","author":"Ha","year":"1999","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"R16","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1038\/72421","article-title":"Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states","volume":"7","author":"Ha","year":"2000","journal-title":"Nat Struct Biol"},{"key":"R17","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/0378-1119(93)90620-I","article-title":"Cloning, characterization and overexpression of the phytase-encoding gene ( phyA ) of Aspergillus niger","volume":"127","author":"van Hartingsveldt","year":"1993","journal-title":"Gene"},{"key":"R18","doi-asserted-by":"crossref","first-page":"4683","DOI":"10.1093\/nar\/14.11.4683","article-title":"A new method for predicting signal sequence cleavage sites","volume":"14","author":"von Heijne","year":"1986","journal-title":"Nucleic Acids Res"},{"key":"R19","volume-title":"Genetic Manipulation in Streptomyces: a Laboratory Manual","author":"Hopwood","year":"1985"},{"key":"R20","doi-asserted-by":"crossref","first-page":"1077","DOI":"10.1016\/S0021-9258(17)35285-7","article-title":"Bacillus subtilis alkaline phosphatases III and IV. Cloning, sequencing and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure","volume":"266","author":"Hulett","year":"1991","journal-title":"J Biol Chem"},{"key":"R21","first-page":"319","article-title":"Structure and function of Escherichia coli alkaline phosphatase","volume-title":"Phosphate in Microorganisms, Cellular and Molecular Biology","author":"Kantrowitz","year":"1994"},{"key":"R22","doi-asserted-by":"crossref","first-page":"2079","DOI":"10.1128\/AEM.64.6.2079-2085.1998","article-title":"Isolation, characterization, molecular gene cloning, and sequencing of a novel phytase from Bacillus subtilis","volume":"64","author":"Kerovuo","year":"1998","journal-title":"Appl Environ Microbiol"},{"key":"R23","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"R24","doi-asserted-by":"crossref","first-page":"6593","DOI":"10.1128\/JB.171.12.6593-6599.1989","article-title":"Phosphate regulon in members of the family Enterobacteriaceae : comparison of the pho B- pho R operons of E. coli , Shigella dysenteriae and Klebsiella pneumoniae","volume":"171","author":"Lee","year":"1989","journal-title":"J Bacteriol"},{"key":"R25","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1016\/S0076-6879(57)03459-X","article-title":"Characterization of phosphorous compounds by acid lability","volume":"3","author":"Leloir","year":"1957","journal-title":"Methods Enzymol"},{"key":"R26","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1038\/72371","article-title":"Crystal structures of Escherichia coli phytase and its complex with phytate","volume":"7","author":"Lim","year":"2000","journal-title":"Nat Struct Biol"},{"key":"R27","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1099\/00221287-102-2-269","article-title":"Sequential expression of macromolecule biosynthesis and candicidin formation in Streptomyces griseus","volume":"102","author":"Liras","year":"1977","journal-title":"J Gen Microbiol"},{"key":"R28","first-page":"213","article-title":"Molecular mechanisms for the control by phosphate of the biosynthesis of antibiotics and other secondary metabolites","volume-title":"Regulation of Secondary Metabolism in Actinomycetes","author":"Mart\u0131\u0301n","year":"1989"},{"key":"R29","doi-asserted-by":"crossref","first-page":"925","DOI":"10.1002\/bit.260170611","article-title":"Kinetics of biosynthesis of polyene macrolide antibiotics in batch cultures: cell maturation time","volume":"17","author":"Mart\u0131\u0301n","year":"1975","journal-title":"Biotechnol Bioeng"},{"key":"R30","doi-asserted-by":"crossref","first-page":"600","DOI":"10.7164\/antibiotics.32.600","article-title":"Isolation of mutants deregulated in phosphate control of candicidin biosynthesis","volume":"32","author":"Mart\u0131\u0301n","year":"1979","journal-title":"J Antibiot"},{"key":"R31","first-page":"140","article-title":"Phosphate control of antibiotic biosynthesis at the transcriptional level","volume-title":"Phosphate in Microorganisms: Cellular and Molecular Biology","author":"Mart\u0131\u0301n","year":"1994"},{"key":"R32","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1099\/00221287-143-1-245","article-title":"The phytase subfamily of histidine acid phosphatases: isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila","volume":"143","author":"Mitchell","year":"1997","journal-title":"Microbiology"},{"key":"R33","doi-asserted-by":"crossref","first-page":"6005","DOI":"10.1016\/S0021-9258(18)68738-1","article-title":"Reproducible high yield sequencing of proteins electrophoretically separated and transfered to an inert support","volume":"263","author":"Moos","year":"1988","journal-title":"J Biol Chem"},{"key":"R34","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1111\/j.1574-6968.1999.tb08787.x","article-title":"Nucleotide sequence of the gene for alkaline phosphatase of Thermus caldophilus GK24 and characteristics of the deduced primary structure of the enzyme","volume":"180","author":"Park","year":"1999","journal-title":"FEMS Microbiol Lett"},{"key":"R35","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/0378-1119(93)90224-Q","article-title":"The cloning and sequencing of the genes encoding phytase ( phy ) and pH 2\u00b75-optimum acid phosphatase ( aph ) from Aspergillus niger var. awamori","volume":"133","author":"Piddington","year":"1993","journal-title":"Gene"},{"key":"R36","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1128\/JB.171.2.767-774.1989","article-title":"Cloning, sequencing and characterization of the principal acid phosphatase, the pho C product from Zymomonas mobilis","volume":"171","author":"Pond","year":"1989","journal-title":"J Bacteriol"},{"key":"R37","doi-asserted-by":"crossref","first-page":"1102","DOI":"10.1128\/JB.151.3.1102-1108.1982","article-title":"Purification and properties of phytate-specific phosphatase from Bacillus subtilis","volume":"151","author":"Powar","year":"1982","journal-title":"J Bacteriol"},{"key":"R38","volume-title":"Molecular Cloning: a Laboratory Manual","author":"Sambrook","year":"1989"},{"key":"R39","doi-asserted-by":"crossref","first-page":"3611","DOI":"10.1111\/j.1365-2958.1992.tb01797.x","article-title":"The gene encoding the cellulase (Avicelase) Cel1 from Streptomyces reticuli and analysis of protein domains","volume":"6","author":"Schlochtermeier","year":"1992","journal-title":"Mol Microbiol"},{"key":"R40","first-page":"145","article-title":"Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications","volume":"24","author":"Towbin","year":"1992","journal-title":"Biotechnology"},{"key":"R41","doi-asserted-by":"crossref","first-page":"6427","DOI":"10.1128\/JB.172.11.6427-6434.1990","article-title":"\u03b2-Lactamase expression in Streptomyces cacaoi","volume":"172","author":"Urabe","year":"1990","journal-title":"J Bacteriol"},{"key":"R42","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1007\/BF00269860","article-title":"Cloning, characterization and expression of an \u03b1-amylase gene from Streptomyces griseus IMRU 3570","volume":"225","author":"Vigal","year":"1991","journal-title":"Mol Gen Genet"}],"container-title":["Microbiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.microbiologyresearch.org\/content\/journal\/micro\/10.1099\/00221287-147-6-1525?crawler=true","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,5,20]],"date-time":"2022-05-20T23:17:01Z","timestamp":1653088621000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.microbiologyresearch.org\/content\/journal\/micro\/10.1099\/00221287-147-6-1525"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2001,6,1]]},"references-count":42,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2001,6,1]]}},"URL":"https:\/\/doi.org\/10.1099\/00221287-147-6-1525","relation":{},"ISSN":["1350-0872","1465-2080"],"issn-type":[{"value":"1350-0872","type":"print"},{"value":"1465-2080","type":"electronic"}],"subject":[],"published":{"date-parts":[[2001,6,1]]}}}