By Dietmar Schomburg, A. Chang, Ida Schomburg
The Springer guide of Enzymes offers concise info on a few 5,000 enzymes sufficiently good characterised – and here's the second one, up to date variation. Their program in analytical, man made and biotechnology techniques in addition to in nutrients undefined, and for medicinal remedies is extra. info sheets are prepared of their EC-Number series. the recent version displays huge development in enzymology: the full fabric has greater than doubled, and the total second version contains 39 volumes plus Synonym Index. beginning in 2009, all newly categorised enzymes are taken care of in complement Volumes.
Read or Download Class 2 . Transferases IX: EC 188.8.131.52 - 184.108.40.206 (Springer Handbook of Enzymes) PDF
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Additional resources for Class 2 . Transferases IX: EC 220.127.116.11 - 18.104.22.168 (Springer Handbook of Enzymes)
Less than a 2fold change in Km for ATP, the inherent ATPase activity increases by 3fold. The mutant enzyme has turnover-numbers for homoserine esters that are only 10% that of homoserine, but has higher affinity for the esters than for L-homoserine itself. L-Cys, a strong inhibitor of the wild-type enzyme, is 50fold less effective as inhibitor of the mutant enzyme. L-Thr no longer inhibits the mutant enzyme. Unlike the wild-type enzyme, addition of lOmM L-homoserine to the mutant enzyme has no protective effect on the number of arginyl residues titrated with (p-hydroxyphenyl)glyoxal )  6 Stability Temperature stability 50 <4> (<4>, stable up to in absence of ligands )  57 <4> (<4>, half-life is 10 min in absence of L-Thr ot L-homoserine )  Additional information <1, 2> (<1>, homoserine and MgATP2- protect against heat inactivation ; <2>, homoserine and MgATP2- do not protect against heat inactivation ) [1, 2] General stability information <9>, enzyme stored with 3 mM ATP loses 50% of its activity after two freezing cycles.
Biol. : The y subunit of phosphorylase kinase contains a pseudosubstrate sequence. Eur. J. : Expression, purification and crystallisation of phosphorylase kinase catalytic domain. J. Mol. : Characterization of the regulatory domain of the y-subunit of phosphorylase kinase. The two noncontiguous calmodulin-binding subdomains are also autoinhibitory. J. Biol. : Isolation and properties of the active y subunit of phosphorylase kinase. J. Biol. : Divalent cations but not other activators enhance phosphorylase kinases affinity for glycogen phosphorylase.
4> )  P ADP + 4-phospho-L-norvaline S ATP + D-homoserine <4> (<4>, 32% of the turnover number with Lhomoserine ) (Reversibility: ? 9% of the turnover number with L-homoserine ) (Reversibility: ? <4> )  P ADP + ? 9% of the turnover number with L-homoserine ) (Reversibility: ? 2% of the turnover number with L-homoserine ) (Reversibility: ? <4> [4,12]) [4, 12] P ? S ATP + L-homoserine <1-11> (Reversibility: ? <1-11> [1-17]) [1-17] P ADP + O-phospho-L-homoserine <1-11> [1-17] S ATP + L-homoserine ethyl ester <4> (<4>, 74% of the turnover number with L-homoserine ) (Reversibility: ?