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Literature summary extracted from

  • Krishna, S.S.; Zhou, T.; Daugherty, M.; Osterman, A.; Zhang, H.
    Structural basis for the catalysis and substrate specificity of homoserine kinase (2001), Biochemistry, 40, 10810-10818.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.39 crystals are grown by the hanging drop vapor diffusion method Methanocaldococcus jannaschii
2.7.1.39 the enzyme ternary complexes with its amino acid substrate and ATP analogues determined by X-ray crystallography Methanocaldococcus jannaschii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.39 ATP + L-homoserine Methanocaldococcus jannaschii fourth enzyme in the aspartate pathway of amino acid biosynthesis ADP + O-phospho-L-homoserine
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Organism

EC Number Organism UniProt Comment Textmining
2.7.1.39 Methanocaldococcus jannaschii Q58504
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Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.39 ATP + L-homoserine = ADP + O-phospho-L-homoserine the catalytic mechanism 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 Methanocaldococcus jannaschii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.39 ATP + L-homoserine
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Methanocaldococcus jannaschii ADP + O-phospho-L-homoserine
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?
2.7.1.39 ATP + L-homoserine fourth enzyme in the aspartate pathway of amino acid biosynthesis Methanocaldococcus jannaschii ADP + O-phospho-L-homoserine
-
?