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Information on EC 2.1.1.59 - [cytochrome c]-lysine N-methyltransferase
for references in articles please use BRENDA:EC2.1.1.59
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.59 [cytochrome c]-lysine N-methyltransferase
IUBMB Comments
One of a group of enzymes methylating proteins; see also the family of histone-lysine N-methyltransferases (previously EC 2.1.1.43) and EC 2.1.1.60 calmodulin-lysine N-methyltransferase.
The enzyme appears in viruses and cellular organisms
- 2.1.1.59
-
unmethylated
- neurospora
- horse
-
iso-1-cytochrome
-
apocytochrome
-
14cmethyl
- s-transferase
- crassa
-
epsilon-n-trimethyllysine
-
trimethylated
Reaction Schemes
showSynonyms
cytochrome c methyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cytochrome c (lysine) methyltransferase
-
-
-
-
cytochrome c methyltransferase
-
-
-
-
cytochrome c-specific protein methylase III
-
-
-
-
cytochrome c-specific protein-lysine methyltransferase
-
-
-
-
methyltransferase, cytochrome c (lysine)
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + [cytochrome c]-L-lysine = S-adenosyl-L-homocysteine + [cytochrome c]-N6-methyl-L-lysine
S-adenosyl-L-methionine + [cytochrome c]-L-lysine = S-adenosyl-L-homocysteine + [cytochrome c]-N6-methyl-L-lysine
specific methylation site, 1 lysine in cytochrome c, comparison
-
S-adenosyl-L-methionine + [cytochrome c]-L-lysine = S-adenosyl-L-homocysteine + [cytochrome c]-N6-methyl-L-lysine
specific methylation site, 1 lysine in cytochrome c, comparison
-
S-adenosyl-L-methionine + [cytochrome c]-L-lysine = S-adenosyl-L-homocysteine + [cytochrome c]-N6-methyl-L-lysine
hybrid ping-pong mechanism
-
S-adenosyl-L-methionine + [cytochrome c]-L-lysine = S-adenosyl-L-homocysteine + [cytochrome c]-N6-methyl-L-lysine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:[cytochrome c]-L-lysine N6-methyltransferase
One of a group of enzymes methylating proteins; see also the family of histone-lysine N-methyltransferases (previously EC 2.1.1.43) and EC 2.1.1.60 calmodulin-lysine N-methyltransferase.
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CAS REGISTRY NUMBER
COMMENTARY
82047-78-7
-
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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 + CNBr peptide
?
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
S-adenosyl-L-methionine + myoglobin L-lysine
S-adenosyl-L-homocysteine + myoglobin N6-methyl-L-lysine
-
Substrates: 10% activity compared to cytochrome c
Products: -
Products: -
?
S-adenosyl-L-methionine + [apocytochrome c]-L-lysine
S-adenosyl-L-homocysteine + [apocytochrome c]-N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
r
S-adenosyl-L-methionine + [cytochrome c]-L-lysine
S-adenosyl-L-homocysteine + [cytochrome c]-N6-methyl-L-lysine
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: horse heart cytochrome c-72
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: horse heart cytochrome c-72
Products: a single lysine residue at position 72 of horse heart cytochrome c is methylated
Products: a single lysine residue at position 72 of horse heart cytochrome c is methylated
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: horse heart cytochrome c-72
Products: mixture of epsilon-N-monomethyllysine, epsilon-N-dimethyllysine and epsilon-N-trimethyllysine in the ratio 1:3:4
Products: mixture of epsilon-N-monomethyllysine, epsilon-N-dimethyllysine and epsilon-N-trimethyllysine in the ratio 1:3:4
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: important features in determining methyl-accepting activity: 1. reactive site such as-X-Lys-Lys-Y-, 2. length of polypeptide chain, 3. tertiary structure
Products: a single lysine residue at position 72 of horse heart cytochrome c is methylated
Products: a single lysine residue at position 72 of horse heart cytochrome c is methylated
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: important features in determining methyl-accepting activity: 1. reactive site such as-X-Lys-Lys-Y-, 2. length of polypeptide chain, 3. tertiary structure
Products: mixture of epsilon-N-monomethyllysine, epsilon-N-dimethyllysine and epsilon-N-trimethyllysine in the ratio 1:3:4
Products: mixture of epsilon-N-monomethyllysine, epsilon-N-dimethyllysine and epsilon-N-trimethyllysine in the ratio 1:3:4
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: does not randomly methylate cytochrome c, but shows absolute specificity for some amino acid sequences
Products: a single lysine residue at position 72 of horse heart cytochrome c is methylated
Products: a single lysine residue at position 72 of horse heart cytochrome c is methylated
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: does not randomly methylate cytochrome c, but shows absolute specificity for some amino acid sequences
Products: mixture of epsilon-N-monomethyllysine, epsilon-N-dimethyllysine and epsilon-N-trimethyllysine in the ratio 1:3:4
Products: mixture of epsilon-N-monomethyllysine, epsilon-N-dimethyllysine and epsilon-N-trimethyllysine in the ratio 1:3:4
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: also CNBr peptides of horse heart cytochrome c can serve as substrates, overview
Products: a single lysine residue at position 72 of horse heart cytochrome c is methylated
Products: a single lysine residue at position 72 of horse heart cytochrome c is methylated
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: also CNBr peptides of horse heart cytochrome c can serve as substrates, overview
Products: mixture of epsilon-N-monomethyllysine, epsilon-N-dimethyllysine and epsilon-N-trimethyllysine in the ratio 1:3:4
Products: mixture of epsilon-N-monomethyllysine, epsilon-N-dimethyllysine and epsilon-N-trimethyllysine in the ratio 1:3:4
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: overview: substrate activity of various cytochromes c
Products: a single lysine residue at position 72 of horse heart cytochrome c is methylated
Products: a single lysine residue at position 72 of horse heart cytochrome c is methylated
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: overview: substrate activity of various cytochromes c
Products: mixture of epsilon-N-monomethyllysine, epsilon-N-dimethyllysine and epsilon-N-trimethyllysine in the ratio 1:3:4
Products: mixture of epsilon-N-monomethyllysine, epsilon-N-dimethyllysine and epsilon-N-trimethyllysine in the ratio 1:3:4
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: specific for unmethylated cytochrome c
Products: a single lysine residue at position 72 of horse heart cytochrome c is methylated
Products: a single lysine residue at position 72 of horse heart cytochrome c is methylated
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: specific for unmethylated cytochrome c
Products: 9:17:74
Products: 9:17:74
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: specific for unmethylated cytochrome c
Products: mixture of epsilon-N-monomethyllysine, epsilon-N-dimethyllysine and epsilon-N-trimethyllysine in the ratio 1:3:4
Products: mixture of epsilon-N-monomethyllysine, epsilon-N-dimethyllysine and epsilon-N-trimethyllysine in the ratio 1:3:4
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: recombinant substrate iso-1-apocytochrome c
Products: mixture of epsilon-N-monomethyllysine, epsilon-N-dimethyllysine and epsilon-N-trimethyllysine in the ratio 1:3:4
Products: mixture of epsilon-N-monomethyllysine, epsilon-N-dimethyllysine and epsilon-N-trimethyllysine in the ratio 1:3:4
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: horse heart cytochrome c-72
Products: a single lysine residue at position 72 of horse heart cytochrome c is methylated
Products: a single lysine residue at position 72 of horse heart cytochrome c is methylated
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: horse heart cytochrome c-72
Products: 9:17:74
Products: 9:17:74
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: horse heart cytochrome c-72
Products: mixture of epsilon-N-monomethyllysine, epsilon-N-dimethyllysine and epsilon-N-trimethyllysine in the ratio 1:3:4
Products: mixture of epsilon-N-monomethyllysine, epsilon-N-dimethyllysine and epsilon-N-trimethyllysine in the ratio 1:3:4
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: overview: substrate activity of various cytochromes c
Products: a single lysine residue at position 72 of horse heart cytochrome c is methylated
Products: a single lysine residue at position 72 of horse heart cytochrome c is methylated
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: overview: substrate activity of various cytochromes c
Products: 9:17:74
Products: 9:17:74
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: overview: substrate activity of various cytochromes c
Products: mixture of epsilon-N-monomethyllysine, epsilon-N-dimethyllysine and epsilon-N-trimethyllysine in the ratio 1:3:4
Products: mixture of epsilon-N-monomethyllysine, epsilon-N-dimethyllysine and epsilon-N-trimethyllysine in the ratio 1:3:4
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: specific for unmethylated cytochrome c
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: horse heart cytochrome c-72
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: trimethylation of recombinant iso-1-cytochrome c of lysine at position 72
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: in vivo methylation of cytochrome c in yeast occurs probably before cytochrome c is attached to the mitochondria
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: regulation of enzyme and cytochrome c substrate is not in parallel manner
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: lysine-72 of horse cytochrome c is a poor acceptor
Products: uptake of methyl groups occurs only at lysine residue 8 and the terminal proline residue
Products: uptake of methyl groups occurs only at lysine residue 8 and the terminal proline residue
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: Crithidia cytochrome c-557 is far the best substrate
Products: uptake of methyl groups occurs only at lysine residue 8 and the terminal proline residue
Products: uptake of methyl groups occurs only at lysine residue 8 and the terminal proline residue
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: avian cytochromes c are much better substrates than those from mammalian sources
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: horse heart cytochrome c-72
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: does not randomly methylate cytochrome c, but shows absolute specificity for some amino acid sequences
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: also CNBr peptides of horse heart cytochrome c can serve as substrates, overview
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: overview: substrate activity of various cytochromes c
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + [cytochrome c]-L-lysine
S-adenosyl-L-homocysteine + [cytochrome c]-N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
r
S-adenosyl-L-methionine + [cytochrome c]-L-lysine
S-adenosyl-L-homocysteine + [cytochrome c]-N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
r
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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 + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: in vivo methylation of cytochrome c in yeast occurs probably before cytochrome c is attached to the mitochondria
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: regulation of enzyme and cytochrome c substrate is not in parallel manner
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + cytochrome c L-lysine
S-adenosyl-L-homocysteine + cytochrome c N6-methyl-L-lysine
-
Substrates: -
Products: -
Products: -
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-homocysteine
-
competitive versus S-adenosyl-L-methionine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
CNBr peptide
-
residue 1-65 or residue 66-104 of horse heart cytochrome c
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
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.
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). CTM1_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
585
0
68284
Swiss-Prot
-
CTM1_KLULA
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
503
0
58504
Swiss-Prot
-
CTM1_CANGA
Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138)
551
0
63533
Swiss-Prot
-
CTM1_EREGS
Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
478
0
53392
Swiss-Prot
other Location (Reliability: 2)
A6ZT17_YEAS7
Saccharomyces cerevisiae (strain YJM789)
585
0
68256
TrEMBL
other Location (Reliability: 1)
B3LSM4_YEAS1
Saccharomyces cerevisiae (strain RM11-1a)
585
0
68256
TrEMBL
-
B5VK44_YEAS6
Saccharomyces cerevisiae (strain AWRI1631)
585
0
68314
TrEMBL
-
C7GLZ5_YEAS2
Saccharomyces cerevisiae (strain JAY291)
585
0
68256
TrEMBL
-
C8Z9Q2_YEAS8
Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse)
585
0
68256
TrEMBL
-
G2WFI3_YEASK
Saccharomyces cerevisiae (strain Kyokai no. 7 / NBRC 101557)
585
0
68210
TrEMBL
-
H0GHF6_SACCK
Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
584
0
67983
TrEMBL
-
N1P9F1_YEASC
Saccharomyces cerevisiae (strain CEN.PK113-7D)
585
0
68284
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme is stabilized by addition of 66% ammonium sulfate during storage
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partially
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of gluthathione-S-transferase-tagged Cmt1p in Saccharomyces cerevisiae and of His-tagged in Escherichia coli, Myc-tagged
-
in vitro transcription and translation of full length iso-1-cytochrome c gene, serves as substrate
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Valentine, J.; Pettigrew, G.W.
A cytochrome c methyltransferase from Crithidia oncopelti
Biochem. J.
201
329-338
1982
Strigomonas oncopelti
brenda
Nochumson, S.; Durban, E.; Kim, S.; Paik, W.K.
Cytochrome c-specific protein methylase III from Neurospora crassa
Biochem. J.
165
11-18
1977
Neurospora crassa
brenda
Durban, E.; Nochumson, S.; Kim, S.; Ki Paik, W.
Cytochrome c-specific protein-lysine methyltransferase from Neurospora crassa. Purification, characterization, and substrate requirements
J. Biol. Chem.
253
1427-1435
1978
Neurospora crassa
brenda
Park, K.S.; Frost, B.; Tuck, M.; Ho, L.L.; Kim, S.; Paik, W.K.
Enzymatic methylation of in vitro synthesized apocytochrome c enhances its transport into mitochondria
J. Biol. Chem.
262
14702-14708
1987
Saccharomyces cerevisiae
brenda
Polevoda, B.; Martzen, M.R.; Das, B.; Phizicky, E.M.; Sherman, F.
Cytochrome c methyltransferase, Ctm1p, of yeast
J. Biol. Chem.
275
20508-20513
2000
Saccharomyces cerevisiae
brenda
Durban, E.; Kim, S.; Jun, G.J.; Paik, W.K.
Cytochrome c-specific protein-lysine methyltransferase from Neurospora crassa: kinetic mechanism
Korean J. Biochem.
15
19-24
1983
Neurospora crassa
-
brenda
Paik, W.K.; DiMaria, P.
Enzymatic methylation and demethylation of protein-bound lysine residues
Methods Enzymol.
106
274-287
1984
Neurospora crassa
brenda
DiMaria, P.; Kim, S.; Paik, W.K.
Cytochrome c specific methylase from wheat germ
Biochemistry
21
1036-1044
1982
Triticum aestivum
brenda
DiMaria, P.; Polastro, E.; DeLange, R.J.; Kim, S.; Paik, W.K.
Studies on cytochrome c methylation in yeast
J. Biol. Chem.
254
4645-4652
1979
Saccharomyces cerevisiae
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