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L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+

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-
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L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
bifunctional enzyme showing aspartate kinase, 2.7.2.4, and homoserine dehydrogenase activities
-
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
bifunctional enzyme showing aspartate kinase, EC 2.7.2.4, and homoserine dehydrogenase activities
-
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
bifunctional enzyme showing aspartate kinase, EC 2.7.2.4, and homoserine dehydrogenase activities
-
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
bifunctional enzyme showing aspartate kinase, EC 2.7.2.4, and homoserine dehydrogenase activities
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
ordered bi bi kinetic mechanism in which nicotinamide cofactor binds first and leaves last in the reaction sequence
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
role of conserved water molecules and a lysine residue in hydride transfer between the substrate and the cofactor. Lys105, which is located at the interface of the catalytic and cofactor-binding sites, mediates the hydride transfer step of the reaction mechanism of the enzyme. Potential reaction mechanisms for homoserine dehydrogenase, overview
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
L-homoserine oxidation by StHSD proceeds through a sequentially ordered mechanism in which NAD+ binds to the free form of the enzyme, after which L-homoserine binds to the enzyme-NAD+ complex
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
proposed reaction mechanisms of hydride transfer from L-homoserine in the active site of Paracoccidioides brasiliensis homoserine dehydrogenase (HSD), Glu218 accepts a proton from the hydroxyl group of L-homoserine, which donates a hydride to the nC-4 carbon of NAD+. Lys233, Lys122, and the water molecule at position 374 (Wat374) serve to bind the substrate
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
two possible catalytic mechanisms of homoserine oxidation. (a) Lys99 is the acidx02base catalytic residue. The hydroxy group of L-Hse is activated by protonated Lys195, and a proton from the Od of L-Hse is captured by the deprotonated Lys99. Lys99 exists in the simple proton pathway, in which a proton can go in and out of an active site easily. (b) Lys195 is drown as an acidx02base catalytic residue. L-Hse and Asp191 exist deep inside of the active site and have no interaction to the surface. Thus, the direct proton pathway from Lys195 to the bulk water region cannot be realized. Lys99 and Lys195 of TtHSD are essential for catalysis
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
L-homoserine oxidation by StHSD proceeds through a sequentially ordered mechanism in which NAD+ binds to the free form of the enzyme, after which L-homoserine binds to the enzyme-NAD+ complex
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-
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
proposed reaction mechanisms of hydride transfer from L-homoserine in the active site of Paracoccidioides brasiliensis homoserine dehydrogenase (HSD), Glu218 accepts a proton from the hydroxyl group of L-homoserine, which donates a hydride to the nC-4 carbon of NAD+. Lys233, Lys122, and the water molecule at position 374 (Wat374) serve to bind the substrate
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-
L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H + H+
role of conserved water molecules and a lysine residue in hydride transfer between the substrate and the cofactor. Lys105, which is located at the interface of the catalytic and cofactor-binding sites, mediates the hydride transfer step of the reaction mechanism of the enzyme. Potential reaction mechanisms for homoserine dehydrogenase, overview
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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DL-aspartate 4-semialdehyde + NADPH + H+
L-homoserine + NADP+
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r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NADH
L-homoserine + NAD+
-
-
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r
L-aspartate 4-semialdehyde + NADH + H+
L-homoserine + NAD+
-
-
-
-
r
L-aspartate 4-semialdehyde + NADPH
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
L-homoserine + NADP+
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H + H+
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
additional information
?
-
L-aspartate 4-semialdehyde + NAD(P)H

L-homoserine + NAD(P)+
-
-
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r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
kinetic mechanism
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
third reaction in the pathway between aspartate and the amino acids threonine, isoleucine, methionine
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r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
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r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
third reaction in the pathway between aspartate and the amino acids threonine, isoleucine, methionine
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r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
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?
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
?
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
?
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
kinetic mechanism
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
essential step in amino acids L-methionine, L-threonine, and L-isoleucine biosynthesis
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?
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
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r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
Thermophilic bacterium
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-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
-
r
L-aspartate 4-semialdehyde + NADPH

L-homoserine + NADP+
-
-
-
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?
L-aspartate 4-semialdehyde + NADPH
L-homoserine + NADP+
-
-
-
-
r
L-aspartate 4-semialdehyde + NADPH
L-homoserine + NADP+
-
part of the aspartate pathway of amino acid biosynthesis
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-
r
L-aspartate 4-semialdehyde + NADPH
L-homoserine + NADP+
-
-
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r
L-aspartate 4-semialdehyde + NADPH + H+

L-homoserine + NADP+
-
-
-
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?
L-aspartate 4-semialdehyde + NADPH + H+
L-homoserine + NADP+
-
-
-
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?
L-aspartate 4-semialdehyde + NADPH + H+
L-homoserine + NADP+
-
-
-
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r
L-homoserine + NAD(P)+

L-aspartate 4-semialdehyde + NAD(P)H
-
-
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?
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
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r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
Thermophilic bacterium
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-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
-
r
L-homoserine + NAD(P)+

L-aspartate 4-semialdehyde + NAD(P)H + H+
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H + H+
-
-
-
r
L-homoserine + NAD+

L-aspartate 4-semialdehyde + NADH + H+
-
-
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?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NADP+

L-aspartate 4-semialdehyde + NADPH
-
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH
-
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH
-
-
-
-
?
L-homoserine + NADP+

L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
the binding of L-homoserine is the rate limiting factor for L-homoserine oxidation
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
the binding of L-homoserine is the rate limiting factor for L-homoserine oxidation
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
no activity of the wild-type enzyme with NADP+, but only with enzyme mutants R40A and K57A
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
no activity of the wild-type enzyme with NADP+, but only with enzyme mutants R40A and K57A
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
additional information

?
-
enzyme BsHSD exclusively prefers NADP+ to NAD+
-
-
-
additional information
?
-
-
enzyme BsHSD exclusively prefers NADP+ to NAD+
-
-
-
additional information
?
-
enzyme BsHSD exclusively prefers NADP+ to NAD+
-
-
-
additional information
?
-
the bifunctional enzyme also exhibits aspartokinase activity, EC 2.7.2.4
-
-
-
additional information
?
-
the bifunctional enzyme also exhibits aspartokinase activity, EC 2.7.2.4
-
-
-
additional information
?
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enzyme does not show aspartate kinase activity
-
-
?
additional information
?
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enzyme does not show aspartate kinase activity
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-
?
additional information
?
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enzyme does not show aspartate kinase activity
-
-
?
additional information
?
-
-
enzyme does not show aspartate kinase activity
-
-
?
additional information
?
-
the bifunctional enzyme also exhibits aspartokinase (AK) activity, EC 2.7.2.4. It shows substantial activities of both AK and homoserine dehydrogenase (HseDH)
-
-
-
additional information
?
-
-
the bifunctional enzyme also exhibits aspartokinase (AK) activity, EC 2.7.2.4. It shows substantial activities of both AK and homoserine dehydrogenase (HseDH)
-
-
-
additional information
?
-
the bifunctional enzyme also exhibits aspartokinase (AK) activity, EC 2.7.2.4. It shows substantial activities of both AK and homoserine dehydrogenase (HseDH)
-
-
-
additional information
?
-
the bifunctional enzyme also exhibits aspartokinase (AK) activity, EC 2.7.2.4. It shows substantial activities of both AK and homoserine dehydrogenase (HseDH)
-
-
-
additional information
?
-
the bifunctional enzyme also exhibits aspartokinase (AK) activity, EC 2.7.2.4. It shows substantial activities of both AK and homoserine dehydrogenase (HseDH)
-
-
-
additional information
?
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substrates binding modes, overview
-
-
-
additional information
?
-
-
substrates binding modes, overview
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NADPH
L-homoserine + NADP+
-
part of the aspartate pathway of amino acid biosynthesis
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H + H+
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
L-aspartate 4-semialdehyde + NAD(P)H

L-homoserine + NAD(P)+
-
kinetic mechanism
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
third reaction in the pathway between aspartate and the amino acids threonine, isoleucine, methionine
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
third reaction in the pathway between aspartate and the amino acids threonine, isoleucine, methionine
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
kinetic mechanism
-
-
r
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
essential step in amino acids L-methionine, L-threonine, and L-isoleucine biosynthesis
-
-
?
L-aspartate 4-semialdehyde + NAD(P)H
L-homoserine + NAD(P)+
-
-
-
-
r
L-homoserine + NAD(P)+

L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H
-
-
-
r
L-homoserine + NAD(P)+

L-aspartate 4-semialdehyde + NAD(P)H + H+
-
-
-
r
L-homoserine + NAD(P)+
L-aspartate 4-semialdehyde + NAD(P)H + H+
-
-
-
r
L-homoserine + NAD+

L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
r
L-homoserine + NAD+
L-aspartate 4-semialdehyde + NADH + H+
-
-
-
?
L-homoserine + NADP+

L-aspartate 4-semialdehyde + NADPH
-
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH
-
-
-
-
?
L-homoserine + NADP+

L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
r
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
L-homoserine + NADP+
L-aspartate 4-semialdehyde + NADPH + H+
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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(2S)-2-[[4-(propan-2-yl)phenyl]sulfanyl]propanenitrile
-
(S)-2-amino-4-oxo-5-hydroxypentanoic acid
-
RI-331
(S)-2-N-[(S)-leucyl]amino-5-hydroxy-4-oxopentanoic acid
-
-
1-tert-butyl-4-[(difluoromethyl)sulfanyl]benzene
-
1-[(1S,2S)-2-(bromomethyl)cyclopropyl]-4-[(trifluoromethyl)sulfanyl]benzene
-
2,2'-[thiobis[[2-(1,1-dimethylethyl)-5-methyl-4,1-phenylene]oxy]]bis-acetic acid diethyl ester
-
-
3-[(4-tert-butylphenyl)sulfanyl]propane-1-thiol
-
4,4'-sulfanediylbis[2-(propan-2-yl)phenol]
-
4,4'-thiobis[2-(1,1-dimethylethyl)]-5-methyl-phenol
-
-
4,4'-thiobis[2-(1,1-dimethylethyl)]-phenol
-
-
4,4'-thiobis[2-(1-methylethyl)]-phenol
-
-
4,4'-thiobis[5-methyl-2-(1-methylethyl)]-phenol
-
-
4,4'-[1,2-ethanediylbis(thio)]bis[2,6-bis(1-methylpropyl)]-phenol
-
-
4,4'-[1,2-ethanediylbis(thio)]bis[2-(1,1-dimethylethyl)-6-methyl]-phenol
-
-
4-(1-methylheptyl)-1,3-benzenediol
-
-
4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol
4-[[2-(2-furanyl)ethyl]thio]-phenol
-
-
4-[[[4-(1,1-dimethylethyl)phenyl]thio]methyl]-2,6-bis(1-methylethyl)-phenol
-
-
5-hydroxy-4-oxo-L-norvaline
HONV, the mechanism of antifungal action of HONV dipeptides (determined against Candida albicans strain ATCC 10231 cells in three different growth media) involves uptake by the oligopeptide transport system, subsequent intracellular cleavage by cytosolic peptidases, and inhibition of homoserine dehydrogenase by the released HONV. Chemical synthesis of HONV and construction of HONV dipeptides as potential antifungal agents, overview. Six dipeptides with L-alanine, L-valine, L-norvaline (Nva), L-leucine, L-isoleucine, and L-phenylalanine as the N-terminal residues are obtained, Gly-HONV and D-Leu-HONV are synthesized and evaluated for comparative purposes. Antifungal in vitro activity and MIC values of HONV and its dipeptides, overview. Activity of HONV strongly depends on growth medium composition. Dipeptide (S)-2-N-[(R)-leucyl]amino-5-hydroxy-4-oxopentanoic acid (D-Leu-HONV) is inactive in all growth media. Antifungal activity of the compounds against different Candida species. Lack of activity of HONV-containing dipeptides against the Candida albicans opt1-opt5DELTA ptr2DELTA ptr22DELTA mutant clearly indicates that these compounds are transported to Candida albicans cells by the oligopeptide transport system, most probably by the di-tripeptide permeases Ptr2p and Ptr22, uptake rates into Candida albicans strain ATCC 10231 cells at pH 5.0 and pH 7.0 are determined, the initial uptake velocities are generally higher at pH 5.0 than at pH 7.0
bis(4-chlorophenyl)ethyloxiranyl-silane
-
-
D-threonine
Thermophilic bacterium
-
slight
DL-allo-threonine
Thermophilic bacterium
-
-
glycyl-5-hydroxy-4-oxo-L-norvaline
i.e. (S)-2-N-glycylamino-5-hydroxy-4-oxopentanoic acid
H-(1,2,4-triazol-3-yl)-DL-alanine
-
-
L-alanyl-5-hydroxy-4-oxo-L-norvaline
i.e. (S)-2-N-[(S)-alanyl]amino-5-hydroxy-4-oxopentanoic acid
L-isoleucyl-5-hydroxy-4-oxo-L-norvaline
i.e. (S)-2-N-[(S)-isoleucyl]amino-5-hydroxy-4-oxopentanoic acid
L-lysine
allosteric regulation of recombinant engineered homoserine dehydrogenase by nonnatural inhibitor L-lysine
L-norvalyl-5-hydroxy-4-oxo-L-norvaline
i.e. (S)-2-N-[(S)-norvalyl]amino-5-hydroxy-4-oxopentanoic acid
L-phenylalanyl-5-hydroxy-4-oxo-L-norvaline
i.e. (S)-2-N-[(S)-phenylalanyl]amino-5-hydroxy-4-oxopentanoic acid
L-valyl-5-hydroxy-4-oxo-L-norvaline
i.e. (S)-2-N-[(S)-valyl]amino-5-hydroxy-4-oxopentanoic acid
NADH
acts as a competitive inhibitor of NAD+, product inhibition, non-competitive inhibition versus L-homoserine
p-chloromercuribenzoate
-
-
Zinc15967722
MIC/MCF is 0.032 mg/ml
Zinc20611644
MIC/MCF is 0.128 mg/ml
Zinc2123137
MIC/MCF is 0.008 mg/ml
[2-(1,1-dimethylethyl)-4-[[5-(1,1-dimethylethyl)-4-hydroxy-2-methylphenyl]thio]-5-methylphenoxy]-acetic acid ethyl ester
-
-
4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol

competitive to L-aspartate 4-semialdehyde, enzyme binding structure anaysis from crystal structure, overview
4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol
-
4-(4-hydroxy-3-isopropylphenylthio)-2-isopropylphenol
-
Amphotericin B

MIC value against strain Pb18 is 0.12 mg/ml
Amphotericin B
MIC value against strain Pb18 is 0.06 mg/ml
itraconazole

MIC value against strain Pb18 is 0.007 mg/ml
itraconazole
MIC value against strain Pb18 is 0.007 mg/ml
L-cysteine

-
-
L-cysteine
-
slight inhibition of chloroplast isozyme, strong inhibition of cytoplasmic isozyme
L-cysteine
-
slight inhibition of chloroplast isozyme, strong inhibition of cytoplasmic isozyme
L-cysteine
competitive versus L-homoserine, uncompetitive versus cofactors NAD+ and NADP+. 95% inhibition at 10 mM. The feedback inhibition of StHSD by cysteine occurs through the formation of an enzyme-NAD-cysteine complex. Cysteine situates within the homoserine binding site, formation of a covalent bond between cysteine and the nicotinamide ring. Cysteine interacts with six residues (Gly156, Thr157, Tyr183, Glu185, Asp191, and Lys200) in the StHSD active site, binding structure analysis, overview
L-cysteine
Thermophilic bacterium
-
slight
L-serine

-
-
L-serine
allosteric inhibitor
L-serine
14% inhibition at 10 mM
L-threonine

strong inhibition of both enzyme activities, aspartate dehydrogenase and aspartate kinase activity, by decreasing the affinity of the enzyme for substrate and cofactors, kinetic effects
L-threonine
-
the regulatory domain of the enzyme contains 2 binding sites, interaction with Gln443 leads to inhibition of the aspartate kinase activity and facilitates the binding of a second threonine on Gln524 leading to inhibition of the homoserine dehydrogenase activity, inhibition of the forward reactions
L-threonine
the enzyme activity is subjected to feedback regulation by L-threonine
L-threonine
the natural threonine binding sites of the enzyme are predicted and verified by mutagenesis experiments
L-threonine
-
degree of inhibition depends on age of plant; sensitive and insensitive isozymes
L-threonine
-
sensitive and insensitive isozymes
L-threonine
-
degree of inhibition depends on age of plant; sensitive and insensitive isozymes
L-threonine
-
weakly inhibits reverse but not forward reaction
L-threonine
allosteric inhibitor
L-threonine
Thermophilic bacterium
-
-
L-threonine
-
not inhibitory
L-threonine
-
degree of inhibition depends on age of plant; sensitive and insensitive isozymes
methionine

-
-
methionine
-
weakly inhibits reverse but not forward reaction
NADP+

-
-
NADP+
NADP+ does not act as a cofactor for this enzyme, but as a strong inhibitor of NAD+-dependent oxidation of Hse, evaluation of the factors responsible for the NADP+-mediated inhibition
Thr

-
-
Thr
-
90% inhibition of homoserine dehydrogenase 2 at 10 mM
threonine

-
feedback inhibition, one isozyme is resistant and another is sensitive to threonine inhibition, 46.9% inhibition at 1 mM, 63.9% at 5 mM
threonine
-
the methionine-producing strain contains a deregulated homoserine dehydrogenase that is not sensitive to feedback inhibition as the wild-type enzyme
Zinc203432

MIC value is 0.032 mg/ml
Zinc203432
MIC value is 0.064 mg/ml
Zinc273730

MIC value is 0.064 mg/ml
Zinc273730
MIC value is 0.064. Zinc273730 makes important contacts with Gly215, Tyr216, Thr217, and Glu218
additional information

-
Lys, Met, and S-2-aminoethyl-L-cysteine do not affect HSDH activity at 1-5 mM
-
additional information
the natural threonine binding sites of the enzyme are engineered to a lysine binding pocket. The reengineered enzyme only responds to lysine inhibition but not to threonine
-
additional information
-
the natural threonine binding sites of the enzyme are engineered to a lysine binding pocket. The reengineered enzyme only responds to lysine inhibition but not to threonine
-
additional information
L-homoserine inhibits the activity of aspartokinase encoded by metL
-
additional information
enzyme is not inhibited by other aspartate-derived amino acids than threonine
-
additional information
enzyme is not inhibited by other aspartate-derived amino acids than threonine
-
additional information
enzyme is not inhibited by other aspartate-derived amino acids than threonine
-
additional information
-
enzyme is not inhibited by other aspartate-derived amino acids than threonine
-
additional information
-
Thr does not inhibit homoserine dehydrogenase 1
-
additional information
inhibitor docking study, overview
-
additional information
molecular docking simulations and inhibitor screening, virtual screening simulations with 187841 molecules purchasable from the Zinc database. 14 molecules are selected and analyzed by the use of absorption, distribution, metabolism, excretion, and toxicity criteria, resulting in four compounds for in vitro assays. Synergistic effects of HS1 and HS2 in combination with itraconazole against Paracoccidioides brasiliensis. Zinc1531037 and Zinc52986906 are not inhibitory
-
additional information
-
molecular docking simulations and inhibitor screening, virtual screening simulations with 187841 molecules purchasable from the Zinc database. 14 molecules are selected and analyzed by the use of absorption, distribution, metabolism, excretion, and toxicity criteria, resulting in four compounds for in vitro assays. Synergistic effects of HS1 and HS2 in combination with itraconazole against Paracoccidioides brasiliensis. Zinc1531037 and Zinc52986906 are not inhibitory
-
additional information
PbHSD inhibitor screening using the Zinc library, molecular dynamics simulations of PbHSD and ligand docking, electrostatic contacts between protein residues and the respective ligand atoms, overview. The selected ligands remain bound to the protein by a common mechanism throughout the simulation. Cytotoxicity evaluation in HeLa and Vero cells
-
additional information
-
PbHSD inhibitor screening using the Zinc library, molecular dynamics simulations of PbHSD and ligand docking, electrostatic contacts between protein residues and the respective ligand atoms, overview. The selected ligands remain bound to the protein by a common mechanism throughout the simulation. Cytotoxicity evaluation in HeLa and Vero cells
-
additional information
molecular docking simulations and inhibitor screening, virtual screening simulations with 187841 molecules purchasable from the Zinc database. 14 Molecules are selected and analyzed by the use of absorption, distribution, metabolism, excretion, and toxicity criteria, resulting in four compounds for in vitro assays. Zinc1531037 and Zinc52986906 are not inhibitory
-
additional information
-
molecular docking simulations and inhibitor screening, virtual screening simulations with 187841 molecules purchasable from the Zinc database. 14 Molecules are selected and analyzed by the use of absorption, distribution, metabolism, excretion, and toxicity criteria, resulting in four compounds for in vitro assays. Zinc1531037 and Zinc52986906 are not inhibitory
-
additional information
-
no inhibition by [2-(1,1-dimethylethyl)-4-[[5-(1,1-dimethylethyl)-4-hydroxy-2-methylphenyl]thio]-5-methylphenoxy]-acetic acid and 4-amino-butyric acid 2-tert-butyl-4-(3-tert-butyl-4-hydroxy-phenylsulfanyl)-phenyl ester
-
additional information
tHSD is poorly inhibited by less than 5% by 10 mM L-methionine, L-isoleucine, or L-threonine, all of which are final products in the aspartate pathway, and by L-lysine
-
additional information
-
tHSD is poorly inhibited by less than 5% by 10 mM L-methionine, L-isoleucine, or L-threonine, all of which are final products in the aspartate pathway, and by L-lysine
-
additional information
L-homoserine oxidation of the Thermotoga maritima enzyme is almost impervious to inhibition by L-threonine, while L-threonine inhibits AK activity in a cooperative manner. The distinctive sequence of the regulatory domain in Thermotoga maritima AK-HseDH is likely responsible for the unique sensitivity to L-threonine. The quaternary structure of this enzyme is not affected by L-threonine
-
additional information
-
L-homoserine oxidation of the Thermotoga maritima enzyme is almost impervious to inhibition by L-threonine, while L-threonine inhibits AK activity in a cooperative manner. The distinctive sequence of the regulatory domain in Thermotoga maritima AK-HseDH is likely responsible for the unique sensitivity to L-threonine. The quaternary structure of this enzyme is not affected by L-threonine
-
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0.04
aspartate 4-semialdehyde
-
isozyme II
5.5
ATP
pH 8.0, 37°C, purified recombinant soluble enzyme
0.1
DL-aspartate 4-semialdehyde
-
-
11.6
L-aspartate
pH 8.0, 37°C, purified recombinant soluble enzyme
0.066 - 2.19
L-aspartate 4-semialdehyde
0.013 - 35.08
L-homoserine
additional information
additional information
-
0.066
L-aspartate 4-semialdehyde

-
isozyme I
0.08
L-aspartate 4-semialdehyde
-
threonine insensitive isozyme
0.098
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25°C
0.1
L-aspartate 4-semialdehyde
-
isozyme I
0.13 - 0.15
L-aspartate 4-semialdehyde
-
threonine resistant isozyme
0.15
L-aspartate 4-semialdehyde
-
threonine resistant isozyme
0.15
L-aspartate 4-semialdehyde
-
threonine-resistant enzyme, pH and temperature not specified in the publication
0.17
L-aspartate 4-semialdehyde
-
-
0.24 - 0.25
L-aspartate 4-semialdehyde
-
threonine sensitive isozyme
0.25
L-aspartate 4-semialdehyde
-
threonine sensitive isozyme
0.25
L-aspartate 4-semialdehyde
-
threonine-sensitive enzyme, pH and temperature not specified in the publication
0.36 - 0.4
L-aspartate 4-semialdehyde
-
isozyme II
0.5
L-aspartate 4-semialdehyde
-
-
0.5
L-aspartate 4-semialdehyde
-
threonine sensitive isozyme
0.569
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25°C
0.845
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25°C
1.19
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25°C
1.25
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25°C
2.19
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25°C
0.013
L-homoserine

-
-
0.2
L-homoserine
pH 10.0, 50°C, recombinant enzyme, with NADP+
0.21
L-homoserine
pH 8.0, 30°C, oxidized enzyme
0.275
L-homoserine
cosubstrate NADP+, pH 8.0, 25°C
0.41
L-homoserine
-
recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, homoserine dehydrogenase activity
0.54
L-homoserine
pH 8.0, 30°C, reduced enzyme
0.68
L-homoserine
-
recombinant isolated catalytic HDH-domain containing the interface region, homoserine dehydrogenase activity
0.69
L-homoserine
cosubstrate NADP+, pH 8.0, 25°C
1.08
L-homoserine
cosubstrate NADP+, pH 8.0, 25°C
1.08
L-homoserine
pH 9.5, 50°C, recombinant enzyme, with NAD+
1.2
L-homoserine
-
recombinant wild-type bifunctional holoenzyme, homoserine dehydrogenase activity
1.81
L-homoserine
recombinant enzyme, pH 10.5, 55°C
5.2
L-homoserine
pH 8.0, 37°C, purified recombinant soluble enzyme
6.1
L-homoserine
pH 9.0, 50°C, recombinant enzyme
9.57
L-homoserine
cosubstrate NAD+, pH 8.0, 25°C
13.4
L-homoserine
cosubstrate NAD+, pH 8.0, 25°C
17.2
L-homoserine
-
recombinant isolated catalytic HDH-domain not containing the interface region, homoserine dehydrogenase activity
17.4
L-homoserine
cosubstrate NAD+, pH 8.0, 25°C
35.08
L-homoserine
pH 9.0, 25°C, recombinant enzyme
0.05
NAD+

pH 9.0, 50°C, recombinant mutant K57A
0.31
NAD+
pH 8.0, 30°C, oxidized enzyme
0.32
NAD+
pH 9.0, 50°C, recombinant wild-type enzyme
0.33
NAD+
pH 8.0, 30°C, reduced enzyme
0.74
NAD+
pH 9.5, 50°C, recombinant enzyme
0.95
NAD+
pH 9.0, 50°C, recombinant mutant R40A
0.158
NADH

pH 8.0, 25°C
0.46
NADH
-
isoenzyme II, at pH 7.5, temperature not specified in the publication
0.034
NADP+

pH 8.0, 25°C
0.039
NADP+
pH 9.0, 25°C, recombinant enzyme
0.04
NADP+
pH 9.0, 50°C, recombinant mutant R40A
0.06
NADP+
pH 9.0, 50°C, recombinant mutant K57A
0.064
NADP+
recombinant enzyme, pH 10.5, 55°C
0.11
NADP+
pH 10.0, 50°C, recombinant enzyme
0.166
NADP+
pH 8.0, 37°C, purified recombinant soluble enzyme
0.17 - 0.18
NADP+
Thermophilic bacterium
-
-
0.235
NADP+
pH 8.0, 25°C
0.245
NADP+
pH 8.0, 25°C
0.027
NADPH

-
isozyme II
0.028
NADPH
pH 8.0, 25°C
0.031
NADPH
-
threonine sensitive isozyme
0.032 - 0.036
NADPH
-
threonine resistant isozyme
0.036
NADPH
-
threonine resistant isozyme
0.036
NADPH
-
threonine-resistant enzyme, pH and temperature not specified in the publication
0.039
NADPH
pH 8.0, 25°C
0.04
NADPH
-
threonine sensitive isozyme
0.04
NADPH
-
threonine-sensitive enzyme, pH and temperature not specified in the publication
0.043
NADPH
-
threonine sensitive isozyme
additional information
additional information

kinetics
-
additional information
additional information
-
kinetics
-
additional information
additional information
Michaelis-Menten steady-state kinetics
-
additional information
additional information
-
Michaelis-Menten steady-state kinetics
-
additional information
additional information
enzyme HseDH shows typical Michaelis-Menten kinetics for oxidation
-
additional information
additional information
kinetic profile
-
additional information
additional information
-
kinetic profile
-
additional information
additional information
the binding of L-homoserine is the rate limiting factor for L-homoserine oxidation, Michaelis-Menten kinetics, overview
-
additional information
additional information
-
the binding of L-homoserine is the rate limiting factor for L-homoserine oxidation, Michaelis-Menten kinetics, overview
-
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2.8 - 22.58
L-aspartate 4-semialdehyde
11.58
L-aspartate 4-semialdehyde

-
cosubstrate NADPH, pH 8.0, 25°C
2.8
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25°C
9.68
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25°C
11.58
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25°C
12.98
L-aspartate 4-semialdehyde
cosubstrate NADPH, pH 8.0, 25°C
19.3
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25°C
22.58
L-aspartate 4-semialdehyde
cosubstrate NADH, pH 8.0, 25°C
7
L-homoserine

cosubstrate NAD+, pH 8.0, 25°C
0.042
L-homoserine
cosubstrate NADP+, pH 8.0, 25°C
10.15
L-homoserine
cosubstrate NAD+, pH 8.0, 25°C
24
L-homoserine
-
recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, homoserine dehydrogenase activity
0.052
L-homoserine
cosubstrate NADP+, pH 8.0, 25°C
0.07
L-homoserine
cosubstrate NADP+, pH 8.0, 25°C
0.24
L-homoserine
-
recombinant wild-type bifunctional holoenzyme, homoserine dehydrogenase activity
0.51
L-homoserine
-
recombinant isolated catalytic HDH-domain not containing the interface region, homoserine dehydrogenase activity
1.07
L-homoserine
pH 9.0, 25°C, recombinant enzyme
0.042
L-homoserine
-
cosubstrate NADP+, pH 8.0, 25°C
1.43
L-homoserine
cosubstrate NAD+, pH 8.0, 25°C
0.042
L-homoserine
cosubstrate NADP+, pH 8.0, 25°C
3.3
L-homoserine
-
recombinant isolated catalytic HDH-domain containing the interface region, homoserine dehydrogenase activity
7
L-homoserine
cosubstrate NAD+, pH 8.0, 25°C
96.1
NAD+

pH 9.0, 50°C, recombinant mutant R40A
48.5
NAD+
pH 9.0, 50°C, recombinant mutant K57A
70.1
NAD+
pH 9.0, 50°C, recombinant wild-type enzyme
6.66
NAD+
pH 9.5, 50°C, recombinant enzyme
1.1
NADP+

pH 9.0, 25°C, recombinant enzyme
2.12
NADP+
pH 10.0, 50°C, recombinant enzyme
26.7
NADP+
pH 9.0, 50°C, recombinant mutant K57A
3.4
NADP+
pH 9.0, 50°C, recombinant mutant R40A
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evolution

the catalytic region of the enzyme is unique, the nucleotide-binding domain conforms to the Rossmann fold-like conventional NAD(P)-dependent dehydrogenases
evolution
enzyme homoserine dehydrogenase (HSD) belongs to the family of oxidoreductases and is essential for the biosynthesis of threonine (Thr), methionine (Met), and lysine (Lys) in the metabolic pathway of fungi and plants
evolution
enzyme homoserine dehydrogenase (HSD) belongs to the family of oxidoreductases and is essential for the biosynthesis of threonine (Thr), methionine (Met), and lysine (Lys) in the metabolic pathway of fungi and plants
evolution
structure-function analysis and comparisons
evolution
the orientation of the three domains in the bifunctional aspartate kinase-homoserine dehydrogenase (AK-HseDH) homologue found in Thermotoga maritima totally differs from those observed in previously known AK-HseDHs, the domains line up in the order HseDH, AK, and regulatory domain
evolution
-
enzyme homoserine dehydrogenase (HSD) belongs to the family of oxidoreductases and is essential for the biosynthesis of threonine (Thr), methionine (Met), and lysine (Lys) in the metabolic pathway of fungi and plants
-
evolution
-
the orientation of the three domains in the bifunctional aspartate kinase-homoserine dehydrogenase (AK-HseDH) homologue found in Thermotoga maritima totally differs from those observed in previously known AK-HseDHs, the domains line up in the order HseDH, AK, and regulatory domain
-
evolution
-
enzyme homoserine dehydrogenase (HSD) belongs to the family of oxidoreductases and is essential for the biosynthesis of threonine (Thr), methionine (Met), and lysine (Lys) in the metabolic pathway of fungi and plants
-
evolution
-
the catalytic region of the enzyme is unique, the nucleotide-binding domain conforms to the Rossmann fold-like conventional NAD(P)-dependent dehydrogenases
-
evolution
-
the orientation of the three domains in the bifunctional aspartate kinase-homoserine dehydrogenase (AK-HseDH) homologue found in Thermotoga maritima totally differs from those observed in previously known AK-HseDHs, the domains line up in the order HseDH, AK, and regulatory domain
-
evolution
-
the orientation of the three domains in the bifunctional aspartate kinase-homoserine dehydrogenase (AK-HseDH) homologue found in Thermotoga maritima totally differs from those observed in previously known AK-HseDHs, the domains line up in the order HseDH, AK, and regulatory domain
-
malfunction

HOM6 deletions cause translational arrest in cells grown under amino acid starvation conditions. HOM6 deletion reduces Candida albicans cell adhesion to polystyrene, which is a common plastic used in many medical devices. HOM6-homozygous mutants are hypersensitive to hygromycin B and cycloheximide as compared with wild-type, HOM6-heterozygous, and HOM6-reintegrated strains. HOM6 deletion affects translation and leads to the accumulation of free ribosomes
malfunction
the chemical mutagen ENU causes a mutation in the homoserine serine dehydrogenase enzyme which diverted the aspartyl-beta-semialdehyde to bind with 2,3-dihydrodipicolinate synthase to participate in the L-lysine synthesis through 2,3 meso-diaminopimelate (Meso-Dap). Being a recombinant for diaminopimelate dehydrogenase (ddh), the auxotrophic mutant for the homoserine dehydrogenase follows the ddh pathway by overexpression of ddh by deviating the acetyltransferase and succinyl transferase is the reason for the high yield of L-lysine production
malfunction
-
the chemical mutagen ENU causes a mutation in the homoserine serine dehydrogenase enzyme which diverted the aspartyl-beta-semialdehyde to bind with 2,3-dihydrodipicolinate synthase to participate in the L-lysine synthesis through 2,3 meso-diaminopimelate (Meso-Dap). Being a recombinant for diaminopimelate dehydrogenase (ddh), the auxotrophic mutant for the homoserine dehydrogenase follows the ddh pathway by overexpression of ddh by deviating the acetyltransferase and succinyl transferase is the reason for the high yield of L-lysine production
-
malfunction
-
the chemical mutagen ENU causes a mutation in the homoserine serine dehydrogenase enzyme which diverted the aspartyl-beta-semialdehyde to bind with 2,3-dihydrodipicolinate synthase to participate in the L-lysine synthesis through 2,3 meso-diaminopimelate (Meso-Dap). Being a recombinant for diaminopimelate dehydrogenase (ddh), the auxotrophic mutant for the homoserine dehydrogenase follows the ddh pathway by overexpression of ddh by deviating the acetyltransferase and succinyl transferase is the reason for the high yield of L-lysine production
-
malfunction
-
the chemical mutagen ENU causes a mutation in the homoserine serine dehydrogenase enzyme which diverted the aspartyl-beta-semialdehyde to bind with 2,3-dihydrodipicolinate synthase to participate in the L-lysine synthesis through 2,3 meso-diaminopimelate (Meso-Dap). Being a recombinant for diaminopimelate dehydrogenase (ddh), the auxotrophic mutant for the homoserine dehydrogenase follows the ddh pathway by overexpression of ddh by deviating the acetyltransferase and succinyl transferase is the reason for the high yield of L-lysine production
-
malfunction
-
the chemical mutagen ENU causes a mutation in the homoserine serine dehydrogenase enzyme which diverted the aspartyl-beta-semialdehyde to bind with 2,3-dihydrodipicolinate synthase to participate in the L-lysine synthesis through 2,3 meso-diaminopimelate (Meso-Dap). Being a recombinant for diaminopimelate dehydrogenase (ddh), the auxotrophic mutant for the homoserine dehydrogenase follows the ddh pathway by overexpression of ddh by deviating the acetyltransferase and succinyl transferase is the reason for the high yield of L-lysine production
-
malfunction
-
HOM6 deletions cause translational arrest in cells grown under amino acid starvation conditions. HOM6 deletion reduces Candida albicans cell adhesion to polystyrene, which is a common plastic used in many medical devices. HOM6-homozygous mutants are hypersensitive to hygromycin B and cycloheximide as compared with wild-type, HOM6-heterozygous, and HOM6-reintegrated strains. HOM6 deletion affects translation and leads to the accumulation of free ribosomes
-
malfunction
-
the chemical mutagen ENU causes a mutation in the homoserine serine dehydrogenase enzyme which diverted the aspartyl-beta-semialdehyde to bind with 2,3-dihydrodipicolinate synthase to participate in the L-lysine synthesis through 2,3 meso-diaminopimelate (Meso-Dap). Being a recombinant for diaminopimelate dehydrogenase (ddh), the auxotrophic mutant for the homoserine dehydrogenase follows the ddh pathway by overexpression of ddh by deviating the acetyltransferase and succinyl transferase is the reason for the high yield of L-lysine production
-
malfunction
-
the chemical mutagen ENU causes a mutation in the homoserine serine dehydrogenase enzyme which diverted the aspartyl-beta-semialdehyde to bind with 2,3-dihydrodipicolinate synthase to participate in the L-lysine synthesis through 2,3 meso-diaminopimelate (Meso-Dap). Being a recombinant for diaminopimelate dehydrogenase (ddh), the auxotrophic mutant for the homoserine dehydrogenase follows the ddh pathway by overexpression of ddh by deviating the acetyltransferase and succinyl transferase is the reason for the high yield of L-lysine production
-
metabolism

homoserine dehydrogenase (HSD) is an oxidoreductase in the aspartic acid pathway. The L-homoserine produced by this enzyme at the first branch point of the aspartic acid pathway is a precursor for essential amino acids such as L-threonine, L-methionine and L-isoleucine
metabolism
homoserine dehydrogenase (HSD) is an oxidoreductase that is involved in the reversible conversion of L-aspartate semialdehyde to L-homoserine in a dinucleotide cofactor-dependent reduction reaction. HSD is thus a crucial intermediate enzyme linked to the biosynthesis of several essential amino acids such as lysine, methionine, isoleucine and threonine
metabolism
homoserine dehydrogenase activity and is involved in the biosynthesis of methionine and threonine
metabolism
homoserine dehydrogenase is a key enzyme in the L-threonine pathway
metabolism
biosynthetic pathway from L-aspartate to L-homoserine involving the bifunctional enzyme, overview
metabolism
homoserine dehydrogenase (HSD) catalyzes the reversible conversion of L-aspartate-4-semialdehyde to L-homoserine in the aspartate pathway for the biosynthesis of lysine, methionine, threonine, and isoleucine
metabolism
-
homoserine dehydrogenase (HSD) catalyzes the reversible conversion of L-aspartate-4-semialdehyde to L-homoserine in the aspartate pathway for the biosynthesis of lysine, methionine, threonine, and isoleucine
-
metabolism
-
biosynthetic pathway from L-aspartate to L-homoserine involving the bifunctional enzyme, overview
-
metabolism
-
homoserine dehydrogenase (HSD) is an oxidoreductase in the aspartic acid pathway. The L-homoserine produced by this enzyme at the first branch point of the aspartic acid pathway is a precursor for essential amino acids such as L-threonine, L-methionine and L-isoleucine
-
metabolism
-
homoserine dehydrogenase (HSD) is an oxidoreductase that is involved in the reversible conversion of L-aspartate semialdehyde to L-homoserine in a dinucleotide cofactor-dependent reduction reaction. HSD is thus a crucial intermediate enzyme linked to the biosynthesis of several essential amino acids such as lysine, methionine, isoleucine and threonine
-
metabolism
-
homoserine dehydrogenase is a key enzyme in the L-threonine pathway
-
metabolism
-
homoserine dehydrogenase activity and is involved in the biosynthesis of methionine and threonine
-
metabolism
-
biosynthetic pathway from L-aspartate to L-homoserine involving the bifunctional enzyme, overview
-
metabolism
-
biosynthetic pathway from L-aspartate to L-homoserine involving the bifunctional enzyme, overview
-
physiological function

contrary to wild-type MGA3 cells that secrete 0.4 g/l L-lysine and 59 g/l L-glutamate under optimised fed batch methanol fermentation, the hom-1 mutant M168-20 secretes 11 g/l L-lysine and 69 g/l of L-glutamate. Overproduction of pyruvate carboxylase and its mutant enzyme P455S in M168-20 has no positive effect on the volumetric L-lysine yield and the L-lysine yield on methanol, and causes significantly reduced volumetric L-glutamate yield and L-glutamate yield on methanol
physiological function
homoserine dehydrogenase catalyzes an NAD(P)-dependent reversible reaction between L-homoserine and aspartate 4-semialdehyde and is involved in the aspartate pathway
physiological function
the enzyme coordinates a critical branch point of the metabolic pathway that leads to the synthesis of bacterial cell-wall components such as L-lysine and m-DAP in addition to other amino acids such as L-threonine, L-methionine and L-isoleucine. The kinetic behaviour of Staphylococcus aureus HSD is not altered in the presence of plausible allosteric inhibitors such as L-threonine and L-serine
physiological function
the enzyme is involved in cell-wall maintenance and essential amino acid biosynthesis. Homoserine dehydrogenase catalyzes a reaction at the branch point of the pathway leading to lysine biosynthesis. This pathway is also referred to as the diaminopimelate (dap) pathway
physiological function
the enzyme is naturally allosterically regulated by threonine and isoleucine
physiological function
aspartate kinase (AK, EC 2.7.2.4) and homoserine dehydrogenase (HseDH) are involved in the biosynthetic pathway from L-aspartate to L-homoserine (Hse) in plants and microorganisms. Hse is a common precursor for the synthesis of L-methionine, L-threonine, and L-isoleucine. At the first step in this pathway, L-aspartate is phosphorylated to beta-aspartyl phosphate (beta-Ap) by AK
physiological function
homoserine dehydrogenase (HSD) is an important regulatory enzyme in the aspartate pathway, which mediates synthesis of methionine, threonine and isoleucine from aspartate
physiological function
the homoserine dehydrogenase enzyme is essentially required for the biosynthesis of methionine, threonine, and isoleucine in fungi
physiological function
-
aspartate kinase (AK, EC 2.7.2.4) and homoserine dehydrogenase (HseDH) are involved in the biosynthetic pathway from L-aspartate to L-homoserine (Hse) in plants and microorganisms. Hse is a common precursor for the synthesis of L-methionine, L-threonine, and L-isoleucine. At the first step in this pathway, L-aspartate is phosphorylated to beta-aspartyl phosphate (beta-Ap) by AK
-
physiological function
-
homoserine dehydrogenase (HSD) is an important regulatory enzyme in the aspartate pathway, which mediates synthesis of methionine, threonine and isoleucine from aspartate
-
physiological function
-
the homoserine dehydrogenase enzyme is essentially required for the biosynthesis of methionine, threonine, and isoleucine in fungi
-
physiological function
-
the enzyme coordinates a critical branch point of the metabolic pathway that leads to the synthesis of bacterial cell-wall components such as L-lysine and m-DAP in addition to other amino acids such as L-threonine, L-methionine and L-isoleucine. The kinetic behaviour of Staphylococcus aureus HSD is not altered in the presence of plausible allosteric inhibitors such as L-threonine and L-serine
-
physiological function
-
the enzyme is involved in cell-wall maintenance and essential amino acid biosynthesis. Homoserine dehydrogenase catalyzes a reaction at the branch point of the pathway leading to lysine biosynthesis. This pathway is also referred to as the diaminopimelate (dap) pathway
-
physiological function
-
homoserine dehydrogenase catalyzes an NAD(P)-dependent reversible reaction between L-homoserine and aspartate 4-semialdehyde and is involved in the aspartate pathway
-
physiological function
-
aspartate kinase (AK, EC 2.7.2.4) and homoserine dehydrogenase (HseDH) are involved in the biosynthetic pathway from L-aspartate to L-homoserine (Hse) in plants and microorganisms. Hse is a common precursor for the synthesis of L-methionine, L-threonine, and L-isoleucine. At the first step in this pathway, L-aspartate is phosphorylated to beta-aspartyl phosphate (beta-Ap) by AK
-
physiological function
-
aspartate kinase (AK, EC 2.7.2.4) and homoserine dehydrogenase (HseDH) are involved in the biosynthetic pathway from L-aspartate to L-homoserine (Hse) in plants and microorganisms. Hse is a common precursor for the synthesis of L-methionine, L-threonine, and L-isoleucine. At the first step in this pathway, L-aspartate is phosphorylated to beta-aspartyl phosphate (beta-Ap) by AK
-
physiological function
-
contrary to wild-type MGA3 cells that secrete 0.4 g/l L-lysine and 59 g/l L-glutamate under optimised fed batch methanol fermentation, the hom-1 mutant M168-20 secretes 11 g/l L-lysine and 69 g/l of L-glutamate. Overproduction of pyruvate carboxylase and its mutant enzyme P455S in M168-20 has no positive effect on the volumetric L-lysine yield and the L-lysine yield on methanol, and causes significantly reduced volumetric L-glutamate yield and L-glutamate yield on methanol
-
additional information

structural basis for the catalytic mechanism of homoserine dehydrogenase, the cofactor-binding site and catalytic site are docked with the cofactor NADP+ and L-homoserine, respectively, modelling, overview
additional information
-
structural basis for the catalytic mechanism of homoserine dehydrogenase, the cofactor-binding site and catalytic site are docked with the cofactor NADP+ and L-homoserine, respectively, modelling, overview
additional information
structure homology modelling using the template, homoserine dehydrogenase from Thiobacillus denitrificans, PDB ID 3MTJ, three-dimensional structure analysis and molecular dynamics simulation, overview. Identification of substrate- and cofactor-binding regions. In L-aspartate semialdehyde binding, the substrate docks to the protein involving residues Thr163, Asp198, and Glu192, which may be important because they form a hydrogen bond with the enzyme. Key recognition residues are Lys107 and Lys207
additional information
binding of L-Hse and NADPH induces the conformational changes of TtHSD from an open to a closed form: the mobile loop containing Glu180 approaches to fix L-Hse and NADPH, and both Lys99 and Lys195 make hydrogen bonds with the hydroxy group of L-Hse. The ternary complex of TtHSDs in the closed form mimicks a Michaelis complex better than the previously reported open form structures from other species. Lys99 seems to be the acidx02base catalytic residue of HSD. The substrate L-Hse and the nicotinamide-ribose moiety of the cofactor NADPH are bound to a crevice formed at the interface between the substrate and nucleotide binding domains. In contrast, the adenosine group of NADPH is located at the surface of the enzyme. The open-closed conformational change may play an important role in the formation of the enzymex02substrate-cofactor complex and subsequent enzymatic catalysis
additional information
-
binding of L-Hse and NADPH induces the conformational changes of TtHSD from an open to a closed form: the mobile loop containing Glu180 approaches to fix L-Hse and NADPH, and both Lys99 and Lys195 make hydrogen bonds with the hydroxy group of L-Hse. The ternary complex of TtHSDs in the closed form mimicks a Michaelis complex better than the previously reported open form structures from other species. Lys99 seems to be the acidx02base catalytic residue of HSD. The substrate L-Hse and the nicotinamide-ribose moiety of the cofactor NADPH are bound to a crevice formed at the interface between the substrate and nucleotide binding domains. In contrast, the adenosine group of NADPH is located at the surface of the enzyme. The open-closed conformational change may play an important role in the formation of the enzymex02substrate-cofactor complex and subsequent enzymatic catalysis
additional information
molecular docking analysis of aspartyl-beta-semi aldehyde with homoserine dehydrogenase, modeling
additional information
structure homology modeling of enzyme with bound substrate NAD+ and L-homoserine using the Saccharomyces cerevisiae enzyme (PDB ID 1EBU) as template, binding analysis, overview. The model with the best output is subjected to gradient minimization, redocking, and molecular dynamics simulation
additional information
-
structure homology modeling of enzyme with bound substrate NAD+ and L-homoserine using the Saccharomyces cerevisiae enzyme (PDB ID 1EBU) as template, binding analysis, overview. The model with the best output is subjected to gradient minimization, redocking, and molecular dynamics simulation
additional information
three-dimensional structure homology modeling using the crystal structure of HSD from Mycolicibacterium hassiacum (PDB ID 6DZS) as a template, overview
additional information
-
three-dimensional structure homology modeling using the crystal structure of HSD from Mycolicibacterium hassiacum (PDB ID 6DZS) as a template, overview
additional information
-
molecular docking analysis of aspartyl-beta-semi aldehyde with homoserine dehydrogenase, modeling
-
additional information
-
structure homology modelling using the template, homoserine dehydrogenase from Thiobacillus denitrificans, PDB ID 3MTJ, three-dimensional structure analysis and molecular dynamics simulation, overview. Identification of substrate- and cofactor-binding regions. In L-aspartate semialdehyde binding, the substrate docks to the protein involving residues Thr163, Asp198, and Glu192, which may be important because they form a hydrogen bond with the enzyme. Key recognition residues are Lys107 and Lys207
-
additional information
-
molecular docking analysis of aspartyl-beta-semi aldehyde with homoserine dehydrogenase, modeling
-
additional information
-
three-dimensional structure homology modeling using the crystal structure of HSD from Mycolicibacterium hassiacum (PDB ID 6DZS) as a template, overview
-
additional information
-
molecular docking analysis of aspartyl-beta-semi aldehyde with homoserine dehydrogenase, modeling
-
additional information
-
molecular docking analysis of aspartyl-beta-semi aldehyde with homoserine dehydrogenase, modeling
-
additional information
-
structure homology modeling of enzyme with bound substrate NAD+ and L-homoserine using the Saccharomyces cerevisiae enzyme (PDB ID 1EBU) as template, binding analysis, overview. The model with the best output is subjected to gradient minimization, redocking, and molecular dynamics simulation
-
additional information
-
structural basis for the catalytic mechanism of homoserine dehydrogenase, the cofactor-binding site and catalytic site are docked with the cofactor NADP+ and L-homoserine, respectively, modelling, overview
-
additional information
-
molecular docking analysis of aspartyl-beta-semi aldehyde with homoserine dehydrogenase, modeling
-
additional information
-
molecular docking analysis of aspartyl-beta-semi aldehyde with homoserine dehydrogenase, modeling
-
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hexamer
in absence of L-threonine
homopentamer or homohexamer
?

x * 35492, sequence calculation
?
-
x * 85000, SDS-PAGE, threonine sensitive isozyme
dimer

2 * 40600, calculated, 2 * 40000, SDS-PAGE
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 40000, SDS-PAGE
dimer
StHSD is composed of a nucleotide-binding region (residues 1-130 and 285-304), a dimerization region (residues 131-145 and 256-284), and a catalytic region (residues 146-255). Presence of a disulfide bond formed between two cysteine residues (position 304) in the C-terminal regions of the two subunits
dimer
-
StHSD is composed of a nucleotide-binding region (residues 1-130 and 285-304), a dimerization region (residues 131-145 and 256-284), and a catalytic region (residues 146-255). Presence of a disulfide bond formed between two cysteine residues (position 304) in the C-terminal regions of the two subunits
-
dimer
-
x * 89000 + x * 93000, SDS-PAGE, threonine sensitive isozyme
dimer
-
2 * 38000, SDS-PAGE, threonine resistant isozyme
homodimer

2 * 36925, sequence calculation, 2 * 40000, SDS-PAGE
homodimer
-
2 * 36925, sequence calculation, 2 * 40000, SDS-PAGE
-
homodimer
the enzyme is a dimer in solution as well as in the crystal. Enzyme HSD from stapylococcus aureus is an elongated molecule with three domains: a nucleotide cofactor binding domain at the N-terminus, a central catalytic domain and a C-terminal ACT domain, structure overview
homodimer
-
the enzyme is a dimer in solution as well as in the crystal. Enzyme HSD from stapylococcus aureus is an elongated molecule with three domains: a nucleotide cofactor binding domain at the N-terminus, a central catalytic domain and a C-terminal ACT domain, structure overview
-
homodimer
dimeric enzyme structure, overview
homodimer
-
dimeric enzyme structure, overview
-
homopentamer or homohexamer

x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation
homopentamer or homohexamer
-
x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation
-
homopentamer or homohexamer
-
x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation
-
homopentamer or homohexamer
-
x * 81000, recombinant enzyme, SDS-PAGE, x * 81433, sequence calculation
-
tetramer

in presence of L-threonine
tetramer
4 * 48300, about sequence calculation, 4 x 42800-48500, recombinant His-tagged enzyme, SDS-PAGE
tetramer
-
4 * 48300, about sequence calculation, 4 x 42800-48500, recombinant His-tagged enzyme, SDS-PAGE
-
tetramer
-
4 * 55000, SDS-PAGE
tetramer
-
x * 89000 + x * 93000, SDS-PAGE, threonine sensitive isozyme
additional information

-
primary and secondary structure comparison, the bifunctional enzyme contains 2 homologous subdomains defined by a common loop-alpha helix-loop-beta strand-loop-beta strand motif, the enzymes' regulatory domain is composed of 2 subdomains, amino acid residues 414-453 and 495-534
additional information
the unusual oligomeric assembly can be attributed to the additional C-terminal ACT domain of enzyme BsHSD. Circular dichroism spectroscopy analysis exhibits a typical pattern for alpha/beta proteins, the enzyme structure includes a Rossman fold. The enzyme's nucleotide-binding domain and substrate-binding domain are commonly found in all HSDs from any organism, but the C-terminal ACT domain is an additional regulatory domain that is present in only a subset of HSDs
additional information
-
the unusual oligomeric assembly can be attributed to the additional C-terminal ACT domain of enzyme BsHSD. Circular dichroism spectroscopy analysis exhibits a typical pattern for alpha/beta proteins, the enzyme structure includes a Rossman fold. The enzyme's nucleotide-binding domain and substrate-binding domain are commonly found in all HSDs from any organism, but the C-terminal ACT domain is an additional regulatory domain that is present in only a subset of HSDs
additional information
-
the unusual oligomeric assembly can be attributed to the additional C-terminal ACT domain of enzyme BsHSD. Circular dichroism spectroscopy analysis exhibits a typical pattern for alpha/beta proteins, the enzyme structure includes a Rossman fold. The enzyme's nucleotide-binding domain and substrate-binding domain are commonly found in all HSDs from any organism, but the C-terminal ACT domain is an additional regulatory domain that is present in only a subset of HSDs
-
additional information
structure homology modelling, three-dimensional structure analysis and molecular dynamics simulation, overview
additional information
-
structure homology modelling, three-dimensional structure analysis and molecular dynamics simulation, overview
-
additional information
-
structural basis for the catalytic mechanism of homoserine dehydrogenase, overview
additional information
structural basis for the catalytic mechanism of homoserine dehydrogenase, overview
additional information
-
structural basis for the catalytic mechanism of homoserine dehydrogenase, overview
-
additional information
enzyme TtHSD folds into a dimer with a noncrystallographic 2fold axis. The subunit comprises three conserved domains of HSDs and a flexible tail at the C-terminus. The nucleotide-binding domain (residues 1-119 and 288-309) assumes an alpha/beta Rossmann fold with five beta-strands and four alpha-helices. The dimerization domain (residues 120-140 and 261-287) comprises two alpha-helices and two beta-strands that interact with the corresponding domain of the other subunit of the dimer to form an alpha/beta structure with the four-stranded beta-sheet. The substrate-binding domain (residues 141-260) comprises four beta-strands and five alpha-helices. The flexible tail at the C-terminus (310-332) extends from the nucleotide-binding domain to the substrate-binding domain
additional information
-
enzyme TtHSD folds into a dimer with a noncrystallographic 2fold axis. The subunit comprises three conserved domains of HSDs and a flexible tail at the C-terminus. The nucleotide-binding domain (residues 1-119 and 288-309) assumes an alpha/beta Rossmann fold with five beta-strands and four alpha-helices. The dimerization domain (residues 120-140 and 261-287) comprises two alpha-helices and two beta-strands that interact with the corresponding domain of the other subunit of the dimer to form an alpha/beta structure with the four-stranded beta-sheet. The substrate-binding domain (residues 141-260) comprises four beta-strands and five alpha-helices. The flexible tail at the C-terminus (310-332) extends from the nucleotide-binding domain to the substrate-binding domain
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for the purified ligand-free recombinant wild-type enzyme: sitting drop vapor diffusion method, mixing of 0.001 ml of 12.0 mg/ml protein solution with an equal volume of mother liquor composed of 0.1 M potassium phosphate, pH 6.2, and 20% MPD, 2 days, 20°C, for the homoserine-bound K57A mutant enzyme: sitting drop vapor diffusion method, mixing of 0.002 ml of 10 mg/ml protein solution containing 1 mM homoserine with 0.002 ml of mother liquor containing 16% polyethylene glycol monomethyl ether 2000 and 0.1 M citrate buffer, pH 6.5, 7 days, 20°C, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement and modelling
10 mg/ml purified recombinant enzyme, in TAPS, pH 8.5, in complex with inhibitor 4,4'-thiobis[2-(1-methylethyl)-phenol] in a molar ratio of 1:1, precipitant solution contains either 0.1 CHES, pH 9.5, 35% PEG 600 or 0.1 M CHES, pH 8.5, 40% PEG 400, and 0.2 M NaCl, 0.005 ml protein complex solution are equilibrated against 0.7 ml of precipitant solution using sitting drop technique, 3 months, X-ray diffraction structure determination and analysis at 3.0 A resolution, modeling
-
purified enzyme, crystallization at different pH values in the range of pH 6.0-8.5, hanging drop and sitting drop methods of vapour diffusion, 8 mg/ml protein solution is mixed with reservoir solution, different conditions involving addition of 0.2 M magnesium acetate and PEG 3350 or 8000, and 3.5% glycerol, overview. X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution
purified enzyme, crystallization at different pH values in the range of pH 6.0-8.5, X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution
purified enzyme StHSD complexed with cysteine and NAD+, hanging drop vapour diffusion method, mixing of 0.002 ml of 5 mg/ml protein solution with 0.002 ml of reservoir solution containing 23% w/v PEG 3350, 0.2 M di-ammonium tartrate, 0.001 ml of 20 mM NAD+, and 0.001 ml of 100 mM cysteine, and equilibration against 0.1 ml of reservoir solution, 12°C, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement using the StHSD structure (PDB ID 4YDR) as an initial phasing model
purified recombinant enzyme in oxidized and in reduced form, hanging drop vapor diffusion method, for the oxidized form: mixing of 0.0015 ml of 5.9 mg/ml protein solution with 0.0015 ml of reservoir solution, pH 4.1, containing 9.5% w/v PEG 3350, 19% w/v PEG 400, 0.19 M magnesium chloride, and 2.5% DMSO, for the reduced form: soaking of the oxidized enzyme crystals in a solution consisting of 0.003 ml of reservoir solution and 0.001 ml of 200 mM DTT for 60 min prior to the first diffraction data collection, 12°C, X-ray diffraction structure determmination and analysis at 1.60-1.83 A resolution, molecular replacement and modelling
purified wild-type homoserine dehydrogenase in apoform, complexed with L-homoserine and NADPH in a closed form, and enzyme mutants K99A and K195A complexed with L-Hse and NADP+, hanging-drop vapour-diffusion method, mixing of 0.002 ml of 5 mg/ml protein in 5 mM Tris-HCl, pH 7.5, and in case of the ligand complex forms 15 mM of each ligand, with 0.002 ml of reservoir solution containing 3.3-4.0 M sodium formate and 50 mM CAPS, pH 10.0, X-ray diffraction structure determination and analysis at 1.83 A, 2.00 A, 1.87 A, and 1.93 A resolution, respectively, molecular replacement method using the TtHSDx02L-Hse structure (PDB ID 5XDF) as the search model
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