About: Muramyl ligase

Facets (new session)
Description
Metadata
Settings
- Rule:
- Inverse Functional Properties:
- "Same As":

About: Muramyl ligase Goto Sponge NotDistinct Permalink

An Entity of Type : yago:Unit108189659, within Data Space : dbpedia.org associated with source document(s)
QRcode icon

http://dbpedia.org/describe/?url=http%3A%2F%2Fdbpedia.org%2Fresource%2FMuramyl_ligase

The bacterial cell wall provides strength and rigidity to counteract internal osmotic pressure, and protection against the environment. The peptidoglycan layer gives the cell wall its strength, and helps maintain the overall shape of the cell. The basic peptidoglycan structure of both Gram-positive and Gram-negative bacteria comprises a sheet of glycan chains connected by short cross-linking polypeptides. Biosynthesis of peptidoglycan is a multi-step (11-12 steps) process comprising three main stages:

Attributes	Values
rdf:type	Thing Biomolecule Biomolecule Protein yago:Abstraction100002137 yago:Family108078020 yago:Group100031264 yago:Organization108008335 yago:YagoLegalActor yago:YagoLegalActorGeo yago:YagoPermanentlyLocatedEntity protein yago:SocialGroup107950920 yago:Unit108189659
rdfs:label	Muramyl ligase (en)
rdfs:comment	The bacterial cell wall provides strength and rigidity to counteract internal osmotic pressure, and protection against the environment. The peptidoglycan layer gives the cell wall its strength, and helps maintain the overall shape of the cell. The basic peptidoglycan structure of both Gram-positive and Gram-negative bacteria comprises a sheet of glycan chains connected by short cross-linking polypeptides. Biosynthesis of peptidoglycan is a multi-step (11-12 steps) process comprising three main stages: (en)
name	Mur_ligase (en)
dcterms:subject	Enzymes of known structure EC 6.3.2 Protein domains
Wikipage page ID	35666184 (xsd:integer)
Wikipage revision ID	1079675685 (xsd:integer)
Link from a Wikipage to another Wikipage	Base (chemistry) Cyanophycin Ubiquitin ligase Enzymes of known structure dbr:Glutamic_acid Peptidoglycan Bacteria Cell (biology) Domain (biology) Gram-negative Gram-positive Amino acid Cell wall Binding (molecular) Glycan Protein domain EC 6.3.2 Protein domains Synthase Biosynthesis Transport dbr:Dihydrofolate_reductase Cytoplasmic membrane Catalysis Sequence motif Sequence (biology) N-acetylglucosamine N-acetylmuramic acid Synthetase Polypeptide Polypeptides Diaminopimelate Zinc dependent phospholipase C Virus structure
Link from a Wikipage to an external page	http://expasy.org/enzyme/6.3.2.10 http://expasy.org/enzyme/6.3.2.13 http://expasy.org/enzyme/6.3.2.8 http://expasy.org/enzyme/6.3.2.9
sameAs	Muramyl ligase Muramyl ligase Muramyl ligase
dbp:wikiPageUsesTemplate	dbt:Enzymes dbt:Infobox_protein_family dbt:InterPro_content dbt:Ligases_CO_CS_and_CN dbt:Portal_bar dbt:Reflist dbt:Short_description
PROSITE	PDOC00773 (en)
SCOP	1 (xsd:integer)
InterPro	IPR000713 (en)
Pfam	PF01225 (en)
Pfam clan	CL0063 (en)
symbol	Mur_ligase (en)
has abstract	The bacterial cell wall provides strength and rigidity to counteract internal osmotic pressure, and protection against the environment. The peptidoglycan layer gives the cell wall its strength, and helps maintain the overall shape of the cell. The basic peptidoglycan structure of both Gram-positive and Gram-negative bacteria comprises a sheet of glycan chains connected by short cross-linking polypeptides. Biosynthesis of peptidoglycan is a multi-step (11-12 steps) process comprising three main stages: 1. * formation of UDP-N-acetylmuramic acid (UDPMurNAc) from N-acetylglucosamine (GlcNAc). 2. * addition of a short polypeptide chain to the UDPMurNAc. 3. * addition of a second GlcNAc to the disaccharide-pentapeptide building block and transport of this unit through the cytoplasmic membrane and incorporation into the growing peptidoglycan layer. Stage two involves four key Mur ubiquitin ligase enzymes: MurC (EC), MurD (EC), MurE (EC) and MurF (EC). These four Mur ligases are responsible for the successive additions of L-alanine, D-glutamate, meso-diaminopimelate or L-lysine, and D-alanyl-D-alanine to UDP-N-acetylmuramic acid. All four Mur ligases are topologically similar to one another, even though they display low sequence identity. They are each composed of three domains: an N-terminal Rossmann-fold domain responsible for binding the UDPMurNAc substrate; a central domain (similar to ATP-binding domains of several ATPases and GTPases); and a C-terminal domain (similar to dihydrofolate reductase fold) that appears to be associated with binding the incoming amino acid. The conserved sequence motifs found in the four Mur enzymes also map to other members of the Mur ligase family, including folylpolyglutamate synthetase, cyanophycin synthetase and the capB enzyme from Bacillales. This family includes UDP-N-acetylmuramate-L-alanine ligase (MurC), UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase (MurE), and UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase (MurF). This entry also includes folylpolyglutamate synthase that transfers glutamate to folylpolyglutamate and cyanophycin synthetase that catalyses the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin). (en)
OPM family	350 (xsd:integer)
OPM protein	1 (xsd:integer)
prov:wasDerivedFrom	wikipedia-en:Muramyl_ligase?oldid=1079675685&ns=0
page length (characters) of wiki page	5604 (xsd:nonNegativeInteger)
Symbol	Mur_ligase
foaf:isPrimaryTopicOf	wikipedia-en:Muramyl_ligase
is Link from a Wikipage to another Wikipage of	Cyanophycin synthase (L-arginine-adding) Cyanophycin synthase (L-aspartate-adding) Chemogenomics Cofactor F430 Mur ligase
is Wikipage redirect of	Mur ligase
is foaf:primaryTopic of	wikipedia-en:Muramyl_ligase

Faceted Search & Find service v1.17_git139 as of Feb 29 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 08.03.3330 as of Mar 19 2024, on Linux (x86_64-generic-linux-glibc212), Single-Server Edition (378 GB total memory, 61 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software