| Entry |
|
|---|
| Name |
methylornithine synthase;
PylB
|
|---|
| Class |
Isomerases;
Intramolecular transferases;
Transferring other groups
|
|---|
| Sysname |
L-lysine carboxy-aminomethylmutase
|
|---|
| Reaction(IUBMB) |
L-lysine = (3R)-3-methyl-D-ornithine [RN: R10010]
|
|---|
| Reaction(KEGG) |
|
|---|
| Substrate |
|
|---|
| Product |
(3R)-3-methyl-D-ornithine [CPD: C20277]
|
|---|
| Comment |
The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes. Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule. The reaction is part of the biosynthesis pathway of pyrrolysine, a naturally occurring amino acid found in some archaeal methyltransferases.
|
|---|
| History |
EC 5.4.99.58 created 2012
|
|---|
| Pathway |
| ec01120 | Microbial metabolism in diverse environments |
|
|---|
| Orthology |
| K16180 | methylornithine synthase |
|
|---|
| Genes |
» show all
|
|---|
| Reference |
|
|---|
| Authors |
Gaston MA, Zhang L, Green-Church KB, Krzycki JA |
|---|
| Title |
The complete biosynthesis of the genetically encoded amino acid pyrrolysine from lysine. |
|---|
| Journal |
|
|---|
| Sequence |
|
|---|
| Reference |
|
|---|
| Authors |
Quitterer F, List A, Eisenreich W, Bacher A, Groll M |
|---|
| Title |
Crystal structure of methylornithine synthase (PylB): insights into the pyrrolysine biosynthesis. |
|---|
| Journal |
|
|---|
| Sequence |
|
|---|
| Other DBs |
| ExPASy - ENZYME nomenclature database: | 5.4.99.58 |
|
|---|
| LinkDB |
|
|---|
