6.1.1.26: pyrrolysine-tRNAPyl ligase

This is an abbreviated version!
For detailed information about pyrrolysine-tRNAPyl ligase, go to the full flat file.

Word Map on EC 6.1.1.26

6.1.1.26

synthetases

methanosarcina

amber

aminoacylation

mazei

ncaas

anticodon

aarss

barkeri

pylts

histidyl-trnas

hisrs

hafniense

desulfitobacterium

methanosarcinaceae

trnacua

phers

phenylalanyl-trna

seryl-trna

non-cognate

glyrs

molecular biology

synthesis

Reaction

Synonyms

class II aminoacyl-tRNA synthetase, DhaPylSc, LysZ-RS, More, PylRS, PylS, PylSc, PylSn, pyrrolysyl-tRNA synthetase

ECTree

6 Ligases

6.1 Forming carbon-oxygen bonds

6.1.1 Ligases forming aminoacyl-tRNA and related compounds

6.1.1.26 pyrrolysine-tRNAPyl ligase

Advanced search results

Do not include text mining results

Include

results (more...)

Include

results (more...)

Results	in table
97	AA Sequence
3	Application
28	Cloned(Commentary)
21	Cofactor
12	Crystallization (Commentary)
11	General Information
4	kcat/KM [mM/s]
19	KM Value [mM]
10	Metals/Ions
2	Molecular Weight [Da]
39	Natural Substrates/ Products (Substrates)
66	Organism
1	Pathway
67	PDB ID
9	pH Optimum
49	Protein Variants
15	Purification (Commentary)
1	Reaction
45	Reference
90	Substrates and Products (Substrate)
14	Subunits
83	Synonyms
1	Systematic Name
9	Temperature Optimum [°C]
13	Turnover Number [1/s]

Systematic Name

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Systematic Name on EC 6.1.1.26 - pyrrolysine-tRNAPyl ligase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide

Go to Systematic Name Search

L-pyrrolysine:tRNAPyl ligase (AMP-forming)

In organisms such as Methanosarcina barkeri that incorporate the modified amino acid pyrrolysine (Pyl) into certain methylamine methyltransferases, an unusual tRNAPyl, with a CUA anticodon, can be charged directly with pyrrolysine by this class II aminoacyl---tRNA ligase. The enzyme is specific for pyrrolysine as substrate as it cannot be replaced by lysine or any of the other natural amino acids [1].