Literature summary for 2.7.1.39 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.

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Crystallization (Commentary)

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Methanocaldococcus jannaschii	Q58504	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
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	a

Substrates and Products (Substrate)

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

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Release 2023.1 (January 2023)