Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.17.7.4 extracted from

  • Altincicek, B.; Duin, E.C.; Reichenberg, A.; Hedderich, R.; Kollas, A.K.; Hintz, M.; Wagner, S.; Wiesner, J.; Beck, E.; Jomaa, H.
    LytB protein catalyzes the terminal step of the 2-C-methyl-D-erythritol-4-phosphate pathway of isoprenoid biosynthesis (2002), FEBS Lett., 532, 437-440.
    View publication on PubMed
Search for more literature for 1.17.7.4

Cloned(Commentary)

Cloned (Comment) Organism
gene lytB, expression as His-tagged enzyme in Escherichia coli strain XL1-Blue Aquifex aeolicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.59
-
 (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate recombinant enzyme, pH 7.5, 60°C Aquifex aeolicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ Aquifex aeolicus
-
 dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
 r
isopentenyl diphosphate + NAD(P)+ + H2O Aquifex aeolicus part of isoprenoid biosynthesis (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
-
 r
isopentenyl diphosphate + NAD(P)+ + H2O Aquifex aeolicus 2-C-methyl-D-erithritol-4-phosphate pathway (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
-
 r

Organism

Organism UniProt Comment Textmining
Aquifex aeolicus O67625 gene lytB
-

Oxidation Stability

Oxidation Stability Organism
highly sensitive to O2, 21% remaining activity after incubation in air for 10 min Aquifex aeolicus

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged protein from Escherichia coli strain Xl1-Blue, to 95% homogeneity Aquifex aeolicus

Reaction

Reaction Comment Organism Reaction ID
isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+ reaction mechanism Aquifex aeolicus
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.6
-
 recombinant enzyme Aquifex aeolicus

Storage Stability

Storage Stability Organism
-20°C, purified enzyme, 20 mM Tris-HCl, pH 8.0, 95% remaining activity after 2 weeks Aquifex aeolicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
 Aquifex aeolicus isopentenyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O producing a 5:1 mixture of isopentenyl diphosphate and dimethyallyl diphosphate r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
 Aquifex aeolicus dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O
-
 r
(E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
 Aquifex aeolicus dimethylallyl diphosphate + 2 oxidized ferredoxin [iron-sulfur] cluster + H2O producing a 5:1 mixture of isopentenyl diphosphate and dimethyallyl diphosphate r
isopentenyl diphosphate + NAD(P)+ + H2O part of isoprenoid biosynthesis Aquifex aeolicus (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
-
 r
isopentenyl diphosphate + NAD(P)+ + H2O 2-C-methyl-D-erithritol-4-phosphate pathway Aquifex aeolicus (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H
-
 r

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
 Aquifex aeolicus

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
48 72 half-maximal activity at 48°C and 72°C Aquifex aeolicus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
65
-
 stable Aquifex aeolicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.7
-
 (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate recombinant enzyme, pH 7.5, 60°C Aquifex aeolicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 7.5
-
 Aquifex aeolicus