| http://purl.uniprot.org/citations/1520276 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/1520276 | http://www.w3.org/2000/01/rdf-schema#comment | "The ATP-dependent resynthesis of tubulin from tyrosine and untyrosinated tubulin was examined to establish the most probable steady-state kinetic mechanism of the tubulin: tyrosine ligase (ADP-forming). Three pair-wise sets of initial rate experiments, involving variation of two substrates pair-wise with the third substrate held at a high (but non-saturating) level, yielded convergent-line data, a behaviour that is diagnostic for sequential mechanisms. Michaelis constants were 14 microM, 1.9 microM and 17 microM for ATP, untyrosinated tubulin and L-tyrosine respectively, and the maximal velocity was 0.2 microM/min. AMP was a competitive inhibitor with respect to ATP, and a non-competitive inhibitor versus either tubulin or tyrosine. Likewise, L-dihydroxyphenylalanine acted competitively relative to tyrosine and non-competitively with respect to either ATP or tubulin. These findings directly support a random sequential mechanism. Product inhibition patterns with ADP were also consistent with this assignment; however, inhibition studies were not practical with either orthophosphate or tyrosinated tubulin because both were very weak inhibitors. Substrate protection of the enzyme against alkylation by N-ethylmaleimide and thermal inactivation, along with evidence of enzyme binding to ATP-Sepharose and tubulin-Sepharose, also supports the idea that this three-substrate enzyme reaction exhibits a random substrate addition pathway."xsd:string |
| http://purl.uniprot.org/citations/1520276 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj2860243"xsd:string |
| http://purl.uniprot.org/citations/1520276 | http://purl.uniprot.org/core/author | "Allison R.D."xsd:string |
| http://purl.uniprot.org/citations/1520276 | http://purl.uniprot.org/core/author | "Purich D.L."xsd:string |
| http://purl.uniprot.org/citations/1520276 | http://purl.uniprot.org/core/author | "Deans N.L."xsd:string |
| http://purl.uniprot.org/citations/1520276 | http://purl.uniprot.org/core/date | "1992"xsd:gYear |
| http://purl.uniprot.org/citations/1520276 | http://purl.uniprot.org/core/name | "Biochem J"xsd:string |
| http://purl.uniprot.org/citations/1520276 | http://purl.uniprot.org/core/pages | "243-251"xsd:string |
| http://purl.uniprot.org/citations/1520276 | http://purl.uniprot.org/core/title | "Steady-state kinetic mechanism of bovine brain tubulin: tyrosine ligase."xsd:string |
| http://purl.uniprot.org/citations/1520276 | http://purl.uniprot.org/core/volume | "286"xsd:string |
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