Any feedback?
Information on EC 2.7.1.170 - anhydro-N-acetylmuramic acid kinase and Organism(s) Escherichia coli and UniProt Accession P77570
for references in articles please use BRENDA:EC2.7.1.170Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.1.170 anhydro-N-acetylmuramic acid kinaseIUBMB Comments
This enzyme, along with EC 4.2.1.126, N-acetylmuramic acid 6-phosphate etherase, is required for the utilization of anhydro-N-acetylmuramic acid in proteobacteria. The substrate is either imported from the medium or derived from the bacterium's own cell wall murein during cell wall recycling. The product N-acetylmuramate 6-phosphate is produced as a 7:1 mixture of the alpha- and beta-anomers.
Specify your search results
Word Map
- 2.7.1.170
- levoglucosan
- adp
-
bioconversion
-
anhydrosugars
-
biofuel
- murein
- peptidoglycan
- aeruginosa
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
1,6-anhydro-n-acetylmuramic acid kinase, anhydro-n-acetylmuramic acid kinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O = ADP + N-acetylmuramate 6-phosphate
catalytic mechanism, molecular docking, dynamics simulation
SYSTEMATIC NAME
IUBMB Comments
ATP:1,6-anhydro-N-acetyl-beta-muramate 6-phosphotransferase
This enzyme, along with EC 4.2.1.126, N-acetylmuramic acid 6-phosphate etherase, is required for the utilization of anhydro-N-acetylmuramic acid in proteobacteria. The substrate is either imported from the medium or derived from the bacterium's own cell wall murein during cell wall recycling. The product N-acetylmuramate 6-phosphate is produced as a 7:1 mixture of the alpha- and beta-anomers.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O
ADP + N-acetyl-beta-muramate 6-phosphate + H+
ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O
ADP + N-acetyl-beta-muramate 6-phosphate + H+
-
-
-
-
?
ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O
ADP + N-acetyl-beta-muramate 6-phosphate + H+
-
-
-
?
ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O
ADP + N-acetyl-beta-muramate 6-phosphate + H+
-
-
-
-
?
ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O
ADP + N-acetyl-beta-muramate 6-phosphate + H+
1,6-anhydro-N-acetyl-beta-muramate is a breakdown product of bacterial peptidoglycan in many Gram-negative bacteria, it is released from murein tripeptide
-
-
?
additional information
?
-
the enzyme utilizes an unusual mechanism whereby the sugar substrate is both cleaved and phosphorylated. N-acetylmuramate cannot be used as a substrate for AnmK
-
-
?
additional information
?
-
-
AnmK does not phosphorylate N-acetyl-muramate
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O
ADP + N-acetyl-beta-muramate 6-phosphate + H+
ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O
ADP + N-acetyl-beta-muramate 6-phosphate + H+
-
-
-
?
ATP + 1,6-anhydro-N-acetyl-beta-muramate + H2O
ADP + N-acetyl-beta-muramate 6-phosphate + H+
1,6-anhydro-N-acetyl-beta-muramate is a breakdown product of bacterial peptidoglycan in many Gram-negative bacteria, it is released from murein tripeptide
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no inhibition by N-acetylmuramate up to 20 mM
-
additional information
-
AnmK is not inhibited by N-acetyl-beta-muramate 6-phosphate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
1,6-anhydro-N-acetyl-beta-muramate
pH and temperature not specified in the publication
1
1,6-anhydro-N-acetyl-beta-muramate
-
in 100 mM Tris-HCl (pH 7.5), 20 mM MgCl2, at 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7000
1,6-anhydro-N-acetyl-beta-muramate
pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
-
from no activity at pH 4.5 and 5% of the maximum activity at pH 6.0, the activity continues to increase to pH 10.0
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
1,6-anhydro-N-acetylmuramic acid is produced during peptidoglucan degeneration by transglycosylases, e.g. AmpD or NagZ. The AnmK reaction product N-acetylmuramate 6-phosphate returns into peptidoglycan recycling
physiological function
enzyme AnmK has plays a role in bacterial resistance to the antibiotic fosfomycin, a classical broad-spectrum antibiotic
physiological function
-
MurQ and AnmK kinase are required for utilization of 1,6-anhydro-N-acetyl-beta-muramate derived either from cell wall murein or imported from the medium
additional information
evolution
1,6-anhydro-N-acetylmuramic acid kinase (AnmK) and levoglucosan kinase (LGK) share significant sequence homology (30-40%) and form a subfamily of anhydrosugar kinases in the sugar kinase family, which is itself part of a larger superfamily of ATPase domain containing proteins (sugar kinase/heat shock protein 70/actin superfamily) that contain conserved structural motifs including the ATP binding domain and an interdomain hinge region that allows the two major domains to rotate relative to each other
evolution
phylogenetic analysis and comparison of 1,6-anhydro-N-acetylmuramic acid kinase with levoglucan kinase and AnmK-like enzymes, molecular docking, dynamics simulation, and homology modelling, overview. AnmK and LGK are conserved proteins, and 187Asp, 212Asp are enzymatic residues, respectively
additional information
three dimensional structure analysis, comparison with levoglucan kinase and AnmK-like enzymes, overview
additional information
-
three dimensional structure analysis, comparison with levoglucan kinase and AnmK-like enzymes, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Sephacel column chromatography, hydroxylapatite column chromatography, and Mono Q column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Uehara, T.; Suefuji, K.; Valbuena, N.; Meehan, B.; Donegan, M.; Park, J.T.
Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate
J. Bacteriol.
187
3643-3649
2005
Escherichia coli, Escherichia coli MG1655
Uehara, T.; Suefuji, K.; Jaeger, T.; Mayer, C.; Park, J.T.
MurQ etherase is required by Escherichia coli in order to metabolize anhydro-N-acetylmuramic acid obtained either from the environment or from its own cell wall
J. Bacteriol.
188
1660-1662
2006
Escherichia coli
Bacik, J.P.; Jarboe, L.R.
Bioconversion of anhydrosugars: emerging concepts and strategies
IUBMB Life
68
700-708
2016
Escherichia coli (P77570), Pseudomonas aeruginosa (Q9I5Q5)
Dai, J.; Qu, H.; Yu, Z.; Yang, J.; Zhang, H.
Computational analysis of AnmK-like kinase: New insights into the cell wall metabolism of fungi
J. Theor. Biol.
379
59-65
2015
Escherichia coli (P77570), Escherichia coli, Shewanella oneidensis (Q8EHB5), Shewanella oneidensis MR-1 / ATCC 700550 (Q8EHB5)
EXTERNAL LINKS (specific for EC-Number 2.7.1.170)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
