Any feedback?
No. of entries
Information on EC 2.1.1.B112 - archaeal lysine methyltransferase 4
for references in articles please use BRENDA:EC2.1.1.B112
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Old data from external sources may still be available.
Please check here for current data: EC unknown
Please check here for current data: EC unknown
preliminary BRENDA-supplied EC number
EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.B112 archaeal lysine methyltransferase 4
The expected taxonomic range for this enzyme is: Saccharolobus islandicus
Reaction Schemes
show+
=
+
[protein] N6-methyl-L-lysine
Synonyms
akmt4, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aKMT4
SiRe_1449
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + [protein] L-lysine = S-adenosyl-L-homocysteine + [protein] N6-methyl-L-lysine
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + [Cren7-chromatin-protein] L-lysine
S-adenosyl-L-homocysteine + [Cren7-chromatin-protein] N6-methyl-L-lysine
S-adenosyl-L-methionine + [Csl4-protein] L-lysine
S-adenosyl-L-homocysteine + [Csl4-protein] N6-methyl-L-lysine
S-adenosyl-L-methionine + [helicase MCM]-L-lysine
S-adenosyl-L-homocysteine + [helicase MCM]-N6-methyl-L-lysine
S-adenosyl-L-methionine + [Rrp4-protein] L-lysine
S-adenosyl-L-homocysteine + [Rrp4-protein] N6-methyl-L-lysine
S-adenosyl-L-methionine + [Rrp42-protein] L-lysine
S-adenosyl-L-homocysteine + [Rrp42-protein] N6-methyl-L-lysine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [Sul7d-chromatin-protein] L-lysine
S-adenosyl-L-homocysteine + [Sul7d-chromatin-protein] N6-methyl-L-lysine
additional information
?
-
Substrates: the enzyme can self-methylate intramolecularly. The substrates Sul7d, RPL11, and Cren7 inhibit automethylation in a concentration-dependent manner. This suggests that the enzyme transfers a methyl group from incoming S-adenosyl-L-methionine to itself in the absence of substrates. When the enzyme associates with the proper substrates, however, the enzyme prefers to transfer the methyl group to the substrates rather than to itself
Products: -
Products: -
?
S-adenosyl-L-methionine + [Cren7-chromatin-protein] L-lysine
S-adenosyl-L-homocysteine + [Cren7-chromatin-protein] N6-methyl-L-lysine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [Cren7-chromatin-protein] L-lysine
S-adenosyl-L-homocysteine + [Cren7-chromatin-protein] N6-methyl-L-lysine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [Csl4-protein] L-lysine
S-adenosyl-L-homocysteine + [Csl4-protein] N6-methyl-L-lysine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [Csl4-protein] L-lysine
S-adenosyl-L-homocysteine + [Csl4-protein] N6-methyl-L-lysine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [helicase MCM]-L-lysine
S-adenosyl-L-homocysteine + [helicase MCM]-N6-methyl-L-lysine
Substrates: -
Products: MCM, an archaeal homolog of Mcm2-7 eukaryotic replicative helicase, is methylated by aKMT4 in vitro
Products: MCM, an archaeal homolog of Mcm2-7 eukaryotic replicative helicase, is methylated by aKMT4 in vitro
?
S-adenosyl-L-methionine + [helicase MCM]-L-lysine
S-adenosyl-L-homocysteine + [helicase MCM]-N6-methyl-L-lysine
Substrates: -
Products: MCM, an archaeal homolog of Mcm2-7 eukaryotic replicative helicase, is methylated by aKMT4 in vitro
Products: MCM, an archaeal homolog of Mcm2-7 eukaryotic replicative helicase, is methylated by aKMT4 in vitro
?
S-adenosyl-L-methionine + [Rrp4-protein] L-lysine
S-adenosyl-L-homocysteine + [Rrp4-protein] N6-methyl-L-lysine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [Rrp4-protein] L-lysine
S-adenosyl-L-homocysteine + [Rrp4-protein] N6-methyl-L-lysine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [Sul7d-chromatin-protein] L-lysine
S-adenosyl-L-homocysteine + [Sul7d-chromatin-protein] N6-methyl-L-lysine
Substrates: the enzyme methylates Sul7d in the chromatin context
Products: -
Products: -
?
S-adenosyl-L-methionine + [Sul7d-chromatin-protein] L-lysine
S-adenosyl-L-homocysteine + [Sul7d-chromatin-protein] N6-methyl-L-lysine
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [Sul7d-chromatin-protein] L-lysine
S-adenosyl-L-homocysteine + [Sul7d-chromatin-protein] N6-methyl-L-lysine
Substrates: the enzyme methylates Sul7d in the chromatin context
Products: -
Products: -
?
S-adenosyl-L-methionine + [Sul7d-chromatin-protein] L-lysine
S-adenosyl-L-homocysteine + [Sul7d-chromatin-protein] N6-methyl-L-lysine
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + [Sul7d-chromatin-protein] L-lysine
S-adenosyl-L-homocysteine + [Sul7d-chromatin-protein] N6-methyl-L-lysine
S-adenosyl-L-methionine + [Sul7d-chromatin-protein] L-lysine
S-adenosyl-L-homocysteine + [Sul7d-chromatin-protein] N6-methyl-L-lysine
Substrates: the enzyme methylates Sul7d in the chromatin context
Products: -
Products: -
?
S-adenosyl-L-methionine + [Sul7d-chromatin-protein] L-lysine
S-adenosyl-L-homocysteine + [Sul7d-chromatin-protein] N6-methyl-L-lysine
Substrates: the enzyme methylates Sul7d in the chromatin context
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
DNA
increased activity on Sul7d, but not Cren7, in the presence of DNA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00112
[Sul7d-chromatin-protein] L-lysine
pH 8.0, 50°C, in presence of DNA
-
0.00397
[Sul7d-chromatin-protein] L-lysine
pH 8.0, 50°C, in absence of DNA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 80
30°C: about 40% of maximal activity, 80°C: about 40% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
MCM, an archaeal homolog of Mcm2-7 eukaryotic replicative helicase, is methylated by aKMT4 in vitro. Mono-methylation of these lysine residues occurs coincidently in the endogenous MCM protein. The helicase activity of mini-chromosome maintenance (MCM) is stimulated by methylation, particularly at temperatures over 70°C. The methylated MCM shows optimal DNA unwinding activity after heat-treatment between 76 and 82°C. After methylation, the half life of MCM helicase is dramatically extended at 80°C. The methylated sites are located on the accessible protein surface, which might modulate the intra- and inter-molecular interactions through changing the hydrophobicity and surface charge
physiological function
-
MCM, an archaeal homolog of Mcm2-7 eukaryotic replicative helicase, is methylated by aKMT4 in vitro. Mono-methylation of these lysine residues occurs coincidently in the endogenous MCM protein. The helicase activity of mini-chromosome maintenance (MCM) is stimulated by methylation, particularly at temperatures over 70°C. The methylated MCM shows optimal DNA unwinding activity after heat-treatment between 76 and 82°C. After methylation, the half life of MCM helicase is dramatically extended at 80°C. The methylated sites are located on the accessible protein surface, which might modulate the intra- and inter-molecular interactions through changing the hydrophobicity and surface charge
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). KMT_SACI5
Saccharolobus islandicus (strain REY15A)
161
0
18154
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G38A
additional information
additional information
aKMT4-8A mutant (a mutant with all eight lysine residues mutated to alanine): automethylation is almost completely removed in the presence of substrates, such as Cren7 and Sul7d. Retains significant automethylation activity in the absence of substrates. Mutant with abrogated automethylation shows a more than 150% increase in methylation of substrates
additional information
-
aKMT4-8A mutant (a mutant with all eight lysine residues mutated to alanine): automethylation is almost completely removed in the presence of substrates, such as Cren7 and Sul7d. Retains significant automethylation activity in the absence of substrates. Mutant with abrogated automethylation shows a more than 150% increase in methylation of substrates
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
91.1
melting temperature. Melting temperature is not significantly changed in presence of substrates MCM or S-adenosyl-L-methionine
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Niu, Y.; Xia, Y.; Wang, S.; Li, J.; Niu, C.; Li, X.; Zhao, Y.; Xiong, H.; Li, Z.; Lou, H.; Cao, Q.
A prototypic lysine methyltransferase 4 from archaea with degenerate sequence specificity methylates chromatin proteins Sul7d and Cren7 in different patterns
J. Biol. Chem.
288
13728-13740
2013
Saccharolobus islandicus (F0NBH8), Saccharolobus islandicus Rey15A (F0NBH8)
brenda
Xia, Y.; Niu, Y.; Cui, J.; Fu, Y.; Chen, X.S.; Lou, H.; Cao, Q.
The helicase activity of hyperthermophilic archaeal MCM is enhanced at high temperatures by lysine methylation
Front. Microbiol.
6
1247
2015
Saccharolobus islandicus (F0NBH8), Saccharolobus islandicus Rey15A (F0NBH8)
brenda
EXTERNAL LINKS (specific for EC-Number 2.1.1.B112)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
