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Information on EC 2.3.2.B1 - lipid II:alanine alanyl transferase
for references in articles please use BRENDA:EC2.3.2.B1
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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
2.3 Acyltransferases
2.3.2 Aminoacyltransferases
2.3.2.B1 lipid II:alanine alanyl transferase
The expected taxonomic range for this enzyme is: Streptococcus pneumoniae
Reaction Schemes
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REACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-alanyl-tRNA = UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl)-D-alanyl-D-alanine + tRNA
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine:alanine N6-alanyltransferase
-
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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
ditrans,ocatacis-undecaprenyl diphosphoryl (GlcNAc-beta-(1->4))MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-Ala-tRNa
ditrans,ocatacis-undecaprenyl diphosphoryl (GlcNAc-beta-(1->4))MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl)-D-alanyl-D-alanine + tRNA
-
Substrates: -
Products: -
Products: -
?
ditrans,ocatacis-undecaprenyl diphosphoryl MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-alanyl-tRNA
? + tRNA
-
Substrates: i.e. lipid I
Products: -
Products: -
?
ditrans,ocatacis-undecaprenyl diphosphoryl MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanyl-L-alanyl-gamma-D-glutamyl-L-lysine + alanyl-tRNA
? + tRNA
-
Substrates: -
Products: -
Products: -
?
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-alanyl-tRNA
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl)-D-alanyl-D-alanine + tRNA
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-seryl-tRNA
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-seryl)-D-alanyl-D-alanine + tRNA
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-alanyl-tRNA
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl)-D-alanyl-D-alanine + tRNA
-
Substrates: MurMPn16 of penicillin-susceptible strain Pn16 supports serylation more than alanylation both in vivo and in vitro
Products: -
Products: -
?
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-alanyl-tRNA
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl)-D-alanyl-D-alanine + tRNA
-
Substrates: in vivo and in vitro, in the presence of the appropriate acyl-tRNA, MurM alanylates the peptidoglycan-amino group of the stem peptide lysine in preference to its serylation
Products: -
Products: -
?
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-alanyl-tRNA
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl)-D-alanyl-D-alanine + tRNA
-
Substrates: MurMPn16 of penicillin-susceptible strain Pn16 supports serylation more than alanylation both in vivo and in vitro
Products: -
Products: -
?
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-alanyl-tRNA
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl)-D-alanyl-D-alanine + tRNA
-
Substrates: in vivo and in vitro, in the presence of the appropriate acyl-tRNA, MurM alanylates the peptidoglycan-amino group of the stem peptide lysine in preference to its serylation
Products: -
Products: -
?
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-alanyl-tRNA
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl)-D-alanyl-D-alanine + tRNA
-
Substrates: MurMPn16 of penicillin-susceptible strain Pn16 supports serylation more than alanylation both in vivo and in vitro
Products: -
Products: -
?
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-alanyl-tRNA
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl)-D-alanyl-D-alanine + tRNA
-
Substrates: in vivo and in vitro, in the presence of the appropriate acyl-tRNA, MurM alanylates the peptidoglycan-amino group of the stem peptide lysine in preference to its serylation
Products: -
Products: -
?
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-seryl-tRNA
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-seryl)-D-alanyl-D-alanine + tRNA
-
Substrates: MurMPn16 of penicillin-susceptible strain Pn16 supports serylation more than alanylation both in vivo and in vitro
Products: -
Products: -
?
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-seryl-tRNA
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-seryl)-D-alanyl-D-alanine + tRNA
-
Substrates: in vivo and in vitro, in the presence of the appropriate acyl-tRNA, MurM alanylates the peptidoglycan-amino group of the stem peptide lysine in preference to its serylation
Products: -
Products: -
?
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-seryl-tRNA
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-seryl)-D-alanyl-D-alanine + tRNA
-
Substrates: MurMPn16 of penicillin-susceptible strain Pn16 supports serylation more than alanylation both in vivo and in vitro
Products: -
Products: -
?
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine + L-seryl-tRNA
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-seryl)-D-alanyl-D-alanine + tRNA
-
Substrates: MurMPn16 of penicillin-susceptible strain Pn16 supports serylation more than alanylation both in vivo and in vitro
Products: -
Products: -
?
additional information
?
-
Substrates: a 30-amino acid long sequence within the MurM protein is the main determinant of the specificity of the reaction, the addition of alanine versus serine
Products: -
Products: -
?
additional information
?
-
-
Substrates: differing stem peptide structures of penicillin-resistant strain 159 and penicillin-susceptible strain Pn16 are caused by the profoundly greater catalytic efficiency of MurM159 compared with MurMPn16 brought about by sequence variation between these enzymes and, to a lesser extent, differences in the in vivo tRNAAla:tRNASer ratio in strains 159 and Pn16. Enzyme MurM additionally recognizes the acceptor stem and/or the TPSIC loop stem of the tRNAAla
Products: -
Products: -
?
additional information
?
-
-
Substrates: MurM acts during the lipid-linked stages of peptidoglycan synthesis.The D-alanyl-D-alanine of the stem peptide and the lipid II N-acetylglucosaminyl group are not essential for substrate recognition. epsilon-Carboxylation of the lysine of the stem peptide is not tolerated. Differing stem peptide structures of penicillin-resistant strain 159 and penicillin-susceptible strain Pn16 are caused by the profoundly greater catalytic efficiency of MurM159 compared with MurMPn16 brought about by sequence variation between these enzymes and, to a lesser extent, differences in the in vivo tRNAAla:tRNASer ratio in strains 159 and Pn16. Enzyme MurM additionally recognizes the acceptor stem and/or the TPSIC loop stem of the tRNAAla
Products: -
Products: -
?
additional information
?
-
-
Substrates: differing stem peptide structures of penicillin-resistant strain 159 and penicillin-susceptible strain Pn16 are caused by the profoundly greater catalytic efficiency of MurM159 compared with MurMPn16 brought about by sequence variation between these enzymes and, to a lesser extent, differences in the in vivo tRNAAla:tRNASer ratio in strains 159 and Pn16. Enzyme MurM additionally recognizes the acceptor stem and/or the TPSIC loop stem of the tRNAAla
Products: -
Products: -
?
additional information
?
-
-
Substrates: MurM acts during the lipid-linked stages of peptidoglycan synthesis.The D-alanyl-D-alanine of the stem peptide and the lipid II N-acetylglucosaminyl group are not essential for substrate recognition. epsilon-Carboxylation of the lysine of the stem peptide is not tolerated. Differing stem peptide structures of penicillin-resistant strain 159 and penicillin-susceptible strain Pn16 are caused by the profoundly greater catalytic efficiency of MurM159 compared with MurMPn16 brought about by sequence variation between these enzymes and, to a lesser extent, differences in the in vivo tRNAAla:tRNASer ratio in strains 159 and Pn16. Enzyme MurM additionally recognizes the acceptor stem and/or the TPSIC loop stem of the tRNAAla
Products: -
Products: -
?
additional information
?
-
-
Substrates: differing stem peptide structures of penicillin-resistant strain 159 and penicillin-susceptible strain Pn16 are caused by the profoundly greater catalytic efficiency of MurM159 compared with MurMPn16 brought about by sequence variation between these enzymes and, to a lesser extent, differences in the in vivo tRNAAla:tRNASer ratio in strains 159 and Pn16. Enzyme MurM additionally recognizes the acceptor stem and/or the TPSIC loop stem of the tRNAAla
Products: -
Products: -
?
additional information
?
-
-
Substrates: MurM acts during the lipid-linked stages of peptidoglycan synthesis.The D-alanyl-D-alanine of the stem peptide and the lipid II N-acetylglucosaminyl group are not essential for substrate recognition. epsilon-Carboxylation of the lysine of the stem peptide is not tolerated. Differing stem peptide structures of penicillin-resistant strain 159 and penicillin-susceptible strain Pn16 are caused by the profoundly greater catalytic efficiency of MurM159 compared with MurMPn16 brought about by sequence variation between these enzymes and, to a lesser extent, differences in the in vivo tRNAAla:tRNASer ratio in strains 159 and Pn16. Enzyme MurM additionally recognizes the acceptor stem and/or the TPSIC loop stem of the tRNAAla
Products: -
Products: -
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3'-(1-amino ethyl phosphonyl) 2'-deoxyadenosine
-
1 mM, 95% inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.037
ditrans,ocatacis-undecaprenyl diphosphoryl MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
-
pH 7.6, 37°C
0.031
ditrans,ocatacis-undecaprenyl diphosphoryl MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanyl-L-alanyl-gamma-D-glutamyl-L-lysine
-
pH 7.6, 37°C
0.237
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl)-D-alanyl-D-alanine
-
pH 7.6, 37°C
0.035
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
-
pH 7.6, 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.017
ditrans,ocatacis-undecaprenyl diphosphoryl MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
-
pH 7.6, 37°C
0.0157
ditrans,ocatacis-undecaprenyl diphosphoryl MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanyl-L-alanyl-gamma-D-glutamyl-L-lysine
-
pH 7.6, 37°C
0.0031
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl)-D-alanyl-D-alanine
-
pH 7.6, 37°C
0.033
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
-
pH 7.6, 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.205
ditrans,ocatacis-undecaprenyl diphosphoryl MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
-
pH 7.6, 37°C
0.46
ditrans,ocatacis-undecaprenyl diphosphoryl MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanyl-L-alanyl-gamma-D-glutamyl-L-lysine
-
pH 7.6, 37°C
0.013
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl(N6-L-alanyl)-D-alanyl-D-alanine
-
pH 7.6, 37°C
0.948
UDP-MurNAc-L-alanyl-gamma-D-glutamyl-L-lysyl-D-alanyl-D-alanine
-
pH 7.6, 37°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.172
-
substrate L-alanyl-tRNA from penicillin-susceptible strain Pn16, pH 7.6, 37°C
0.175
-
substrate L-alanyl-tRNA from penicillin-resistant strain 159, pH 7.6, 37°C
0.247
-
substrate L-seryl-tRNA from penicillin-resistant strain 159, pH 7.6, 37°C
0.28
-
substrate L-seryl-tRNA from penicillin-resistant strain 159, pH 7.6, 37°C
0.31
-
substrate L-seryl-tRNA from penicillin-susceptible strain Pn16, pH 7.6, 37°C
0.37
-
substrate L-seryl-tRNA from penicillin-susceptible strain Pn16, pH 7.6, 37°C
1.92
-
substrate L-alanyl-tRNA from penicillin-resistant strain 159, pH 7.6, 37°C
2.09
-
substrate L-alanyl-tRNA from penicillin-susceptible strain Pn16, pH 7.6, 37°C
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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
inactivation of the murMN operon by insertion duplication mutagenesis does not cause any significant change in growth rate of the cultures, but leads to the disappearance of all branched muropeptide monomers and dimers accompanied by a parallel increase in the percentage of linear structured stem peptides and in the appearance of novel peptide structures. Allelic replacement of the mosaic murM gene of strain Pen6 with murM of the penicillin-susceptible laboratory strain R36A causes enrichment of the peptidoglycan in linear muropeptides
physiological function
allelic replacement of the mosaic murM gene of strain Pen6 with murM of the penicillin-susceptible laboratory strain R36A causes enrichment of the peptidoglycan in linear muropeptides
physiological function
the muropeptide composition of the pneumococcal cell walls is determined by the particular murM allele carried by the cells. After cloning of different murM alleles from several penicillin-resistant Streptococcus pneumoniae strains, each with a characteristic branched peptide pattern, and transformation into the penicillin-susceptible laboratory strain R36A, all transformants remain penicillin-susceptible, their cell wall composition changing in directions corresponding to the muropeptide pattern of the strain from which the murM allele is derived
physiological function
-
adds L-serine or L-alanine as the first amino acid of a dipeptide branch to the stem peptide lysine of the pneumococcal peptidoglycan. MurM activity is essential for clinical pneumococcal penicillin resistance
physiological function
-
allelic replacement of the mosaic murM gene of strain Pen6 with murM of the penicillin-susceptible laboratory strain R36A causes enrichment of the peptidoglycan in linear muropeptides
-
physiological function
-
inactivation of the murMN operon by insertion duplication mutagenesis does not cause any significant change in growth rate of the cultures, but leads to the disappearance of all branched muropeptide monomers and dimers accompanied by a parallel increase in the percentage of linear structured stem peptides and in the appearance of novel peptide structures. Allelic replacement of the mosaic murM gene of strain Pen6 with murM of the penicillin-susceptible laboratory strain R36A causes enrichment of the peptidoglycan in linear muropeptides
-
physiological function
-
adds L-serine or L-alanine as the first amino acid of a dipeptide branch to the stem peptide lysine of the pneumococcal peptidoglycan. MurM activity is essential for clinical pneumococcal penicillin resistance
-
physiological function
-
adds L-serine or L-alanine as the first amino acid of a dipeptide branch to the stem peptide lysine of the pneumococcal peptidoglycan. MurM activity is essential for clinical pneumococcal penicillin resistance
-
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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). Q9K307_STREE
406
0
47519
TrEMBL
Secretory Pathway (Reliability: 4)
Q9L447_STREE
406
0
47441
TrEMBL
Secretory Pathway (Reliability: 2)
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cressina, E.; Lloyd, A.J.; De Pascale, G.; Mok, B.J.; Caddick, S.; Roper, D.I.; Dowson, C.G.; Bugg, T.D.H.
Inhibition of tRNA-dependent ligase MurM from Streptococcus pneumoniae by phosphonate and sulfonamide inhibitors
Bioorg. Med. Chem.
17
3443-3455
2009
Streptococcus pneumoniae
brenda
Filipe, s.R.; Pinho, M.G.; Tomasz, A.
Characterization of the murMN operon involved in the synthesis of branched peptidoglycan peptides in Streptococcus pneumoniae
J. Biol. Chem.
275
27768-27774
2000
Streptococcus pneumoniae (Q9K307), Streptococcus pneumoniae (Q9L447), Streptococcus pneumoniae Pen6 (Q9K307), Streptococcus pneumoniae R36A (Q9L447)
brenda
Filipe, S.R.; Severina, E.; Tomasz, A.
Functional analysis of Streptococcus pneumoniae MurM reveals the region responsible for its specificity in the synthesis of branched cell wall peptides
J. Biol. Chem.
276
39618-39628
2001
Streptococcus pneumoniae (Q9L447)
brenda
Lloyd, A.J.; Gilbey, A.M.; Blewett, A.M.; De Pascale, G.; El Zoeiby, A.; Levesque, R.C.; Catherwood, A.C.; Tomasz, A.; Bugg, T.D.H.; Roper, D.I.; Dowson, C.G.
Characterization of tRNA-dependent peptide bond formation by MurM in the synthesis of Streptococcus pneumoniae peptidoglycan
J. Biol. Chem.
283
6402-6417
2008
Streptococcus pneumoniae, Streptococcus pneumoniae 159, Streptococcus pneumoniae Pn16
brenda
EXTERNAL LINKS (specific for EC-Number 2.3.2.B1)
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