Class 2 • Transferases IX: EC 2.7.1.38–2.7.1.112 by Professor Dietmar Schomburg, Dr. Ida Schomburg, Dr. Antje

By Professor Dietmar Schomburg, Dr. Ida Schomburg, Dr. Antje Chang (eds.)

Springer instruction manual of Enzymes presents info on enzymes sufficiently good characterised. It bargains concise and entire descriptions of a few 5,000 enzymes and their program components. information sheets are prepared of their EC-Number series and the volumes themselves are prepared in line with enzyme classes.

This new, moment version displays huge development in enzymology: many enzymes are newly categorized or reclassified. every one access is correlated with references and a number of resource organisms. New datafields are created: program and engineering (for the houses of enzymes the place the series has been changed). the full quantity of fabric inside the instruction manual has greater than doubled in order that the full moment version includes 39 volumes in addition to a Synonym Index. furthermore, beginning in 2009, all newly categorised enzymes are taken care of in complement Volumes.

Springer instruction manual of Enzymes is a perfect resource of knowledge for researchers in biochemistry, biotechnology, natural and analytical chemistry, and meals sciences, in addition to for medicinal applications.

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J. : Identification of the Ca 2 + -dependent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase. ; Nishizuka, Y: Liver glycogen phosphorylase kinase. Partial purification and characterization. J. Biol. : Liver phosphorylase b kinase. Cyclic-AMP-mediated activation and properties of the partially purified rat-liver enzyme. Eur. J. : Chemical and regulatory properties of phosphorylase kinase and cyclic AMP-dependent protein kinase. Adv. Enzymol. Relat. Areas Mol.

J. : Phosphorylase kinase. The Enzymes, 3rd. Ed. : The effect of Mg 2+ on the Ca 2 + -binding properties of non-activated phosphorylase kinase. Eur. J. : Identification of the Ca 2 + -dependent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase. ; Nishizuka, Y: Liver glycogen phosphorylase kinase. Partial purification and characterization. J. Biol. : Liver phosphorylase b kinase. Cyclic-AMP-mediated activation and properties of the partially purified rat-liver enzyme.

J. Biol. : Divalent cations but not other activators enhance phosphorylase kinases affinity for glycogen phosphorylase. 39 Systematic name ATP:L-homoserine O-phosphotransferase Recommended name homoserine kinase Synonyms HSK homoserine kinase (phosphorylating) kinase (phosphorylating), homoserine kinase, homoserine (phosphorylating) CAS registry number 9026-58-8 2 Source Organism <1> <2> <3> <4> <5> <6> <7> <8> <9> <10> <11> Hordeum vulgare [1] Visum sativum (L. cv. 39 chanism of the enzyme does not involve a catalytic base for activating the phosphoryl acceptor hydroxyl but instead is mediated via a transition state stabilization mechanism [16]) Reaction type phospho group transfer Natural substrates and products S ATP + L-homoserine <2, 3, 4, 5, 7, 8, 9, 10, 11> (<2, 3>, the enzyme catalyzes a reaction common to synthesis of Thr, He and Met in plants [2, 3]; <3>, the enzyme is a potential control point in the biosyntic pathway for Thr, He and Met [3]; <5>, enzyme of L-Thr synthesis [5]; <7>, the enzyme is not involved in the regulation of methionine, threonine and isoleucine biosynthesis [8]; <8>, the enzyme plays an important role in the regulation of the threonine biosynthesis [9]; <8>, enzyme of threonine biosynthesis [10]; <4>, enzyme in the aspartate pathway of amino acid biosynthesis [12]; <9>, formation of O-phospho-L-homoserine, a branch point intermediate in the pathways for Met and Thr in plants [13]; <4>, key enzyme in the aspartate pathway of amino acid biosynthesis in E.

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