1.14.11.56: L-proline cis-4-hydroxylase
This is an abbreviated version!
For detailed information about L-proline cis-4-hydroxylase, go to the full flat file.
Word Map on EC 1.14.11.56
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1.14.11.56
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cis-4-hydroxy-l-proline
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sinorhizobium
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meliloti
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dioxygenase
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hydroxylases
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regioselectivity
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loti
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chop
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non-heme
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mesorhizobium
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synthesis
- 1.14.11.56
- cis-4-hydroxy-l-proline
-
sinorhizobium
- meliloti
- dioxygenase
- hydroxylases
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regioselectivity
- loti
-
chop
-
non-heme
-
mesorhizobium
- synthesis
Reaction
Synonyms
cis-P4H, L-proline cis-4-hydroxylase, MlP4H, mlr6283, R03107, SmP4H
ECTree
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General Information
General Information on EC 1.14.11.56 - L-proline cis-4-hydroxylase
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evolution
physiological function
additional information
proline hydroxylases are representative members of the nonheme Fe2+/2-oxoglutarate-dependent dioxygenase family
evolution
proline hydroxylases are representative members of the nonheme Fe2+/2-oxoglutarate-dependent dioxygenase family
the enzyme catalyze the hydroxylation of L-proline, generating cis-4-hydroxy-L-proline, as well as the hydroxylation of L-pipecolic acid (L-Pip), generating two regioisomers, cis-5-hydroxypipecolate and cis-3-hydroxypipecolate in a 6:4 ratio
physiological function
the enzyme catalyze the hydroxylation of L-proline, generating cis-4-hydroxy-L-proline, as well as the hydroxylation of L-pipecolic acid (L-Pip), generating two regioisomers, cis-5-hydroxypipecolate and cis-3-hydroxypipecolate in a 6:4 ratio
I95, I97, and E114 are active site residues, the active site was composed of a distorted jelly roll beta-sheet core, which is sandwiched by the N-terminal and C-terminal alpha-helical domains
additional information
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I95, I97, and E114 are active site residues, the active site was composed of a distorted jelly roll beta-sheet core, which is sandwiched by the N-terminal and C-terminal alpha-helical domains
additional information
V95, V97, and G114 are active site residues, a structure homology model of the SmP4H triple mutant V97F/V95W/E114G is constructed based on the MlP4H crystal structure
additional information
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V95, V97, and G114 are active site residues, a structure homology model of the SmP4H triple mutant V97F/V95W/E114G is constructed based on the MlP4H crystal structure