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http://purl.uniprot.org/citations/7639519http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7639519http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7639519http://www.w3.org/2000/01/rdf-schema#comment"Protein geranylgeranyltransferase type-I (PGGTase-I) catalyzes alkylation of the cysteine residue in proteins containing a consensus C-terminal CaaX sequence ending in leucine by the C20 hydrocarbon moiety in geranylgeranyl diphosphate (GGPP). The Saccharomyces cerevisiae genes encoding the alpha (RAM2) and beta (CDC43) subunits of PGGTase-I were translationally coupled by overlapping the RAM2-CDC43 stop-start codons and by locating a ribosome-binding site near the 3' end of RAM2. Recombinant PGGTase-I was overproduced in Escherichia coli to give approximately 8% of total cellular protein and purified 12-fold to > 95% homogeneity in two steps by ion-exchange and immunoaffinity chromatography. The purified heterodimer contained alpha- and beta-subunits with molecular masses of 34 and 42 kDa, respectively. A continuous fluorescence assay was developed to measure PGGTase-I activity. The recombinant enzyme showed maximal activity at pH 7.5 and required both Mg2+ and Zn2+. Michaelis constants for GGPP (1.0 microM) and dansyl-Gly-Cys-Ile-Ile-Leu (2.4 microM) were similar to those reported for yeast protein farnesyltransferase (PFTase) with farnesyl diphosphate and dansyl-Gly-Cys-Val-Ile-Ala; Vmax = 0.20 mumol min-1 mg-1 for recombinant yeast PGGTase-I was similar to that reported for yeast PFTase."xsd:string
http://purl.uniprot.org/citations/7639519http://purl.org/dc/terms/identifier"doi:10.1006/abbi.1995.1384"xsd:string
http://purl.uniprot.org/citations/7639519http://purl.org/dc/terms/identifier"doi:10.1006/abbi.1995.1384"xsd:string
http://purl.uniprot.org/citations/7639519http://purl.uniprot.org/core/author"Poulter C.D."xsd:string
http://purl.uniprot.org/citations/7639519http://purl.uniprot.org/core/author"Poulter C.D."xsd:string
http://purl.uniprot.org/citations/7639519http://purl.uniprot.org/core/author"Stirtan W.G."xsd:string
http://purl.uniprot.org/citations/7639519http://purl.uniprot.org/core/author"Stirtan W.G."xsd:string
http://purl.uniprot.org/citations/7639519http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7639519http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7639519http://purl.uniprot.org/core/name"Arch. Biochem. Biophys."xsd:string
http://purl.uniprot.org/citations/7639519http://purl.uniprot.org/core/name"Arch. Biochem. Biophys."xsd:string
http://purl.uniprot.org/citations/7639519http://purl.uniprot.org/core/pages"182-190"xsd:string
http://purl.uniprot.org/citations/7639519http://purl.uniprot.org/core/pages"182-190"xsd:string
http://purl.uniprot.org/citations/7639519http://purl.uniprot.org/core/title"Yeast protein geranylgeranyltransferase type-I: overproduction, purification, and characterization."xsd:string
http://purl.uniprot.org/citations/7639519http://purl.uniprot.org/core/title"Yeast protein geranylgeranyltransferase type-I: overproduction, purification, and characterization."xsd:string
http://purl.uniprot.org/citations/7639519http://purl.uniprot.org/core/volume"321"xsd:string
http://purl.uniprot.org/citations/7639519http://purl.uniprot.org/core/volume"321"xsd:string
http://purl.uniprot.org/citations/7639519http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7639519
http://purl.uniprot.org/citations/7639519http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7639519
http://purl.uniprot.org/citations/7639519http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7639519
http://purl.uniprot.org/citations/7639519http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7639519
http://purl.uniprot.org/uniprot/P29703http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7639519
http://purl.uniprot.org/uniprot/P18898http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/7639519