D00417
type: Enzyme
rlcp: p88
rlcp: p393
cath: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
cath: UDP N-Acetylglucosamine Acyltransferase; domain 1
ec: https://purl.uniprot.org/enzyme/2.7.7.23
ec: https://purl.uniprot.org/enzyme/2.3.1.157
csa: 1hv9
uniprot: P0ACC7
uniprot: Q97R46
kegg enzyme: UDP-N-acetylglucosamine diphosphorylase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.23
kegg enzyme: UDP-N-acetylglucosamine pyrophosphorylase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.23
kegg enzyme: uridine diphosphoacetylglucosamine pyrophosphorylase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.23
kegg enzyme: UTP:2-acetamido-2-deoxy-alpha-D-glucose-1-phosphateuridylyltransferase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.23
kegg enzyme: UDP-GlcNAc pyrophosphorylase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.23
kegg enzyme: GlmU uridylyltransferase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.23
kegg enzyme: Acetylglucosamine 1-phosphate uridylyltransferase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.23
kegg enzyme: UDP-acetylglucosamine pyrophosphorylase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.23
kegg enzyme: uridine diphosphate-N-acetylglucosamine pyrophosphorylase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.23
kegg enzyme: uridine diphosphoacetylglucosamine phosphorylase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.23
kegg enzyme: acetylglucosamine 1-phosphate uridylyltransferase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.7.7.23
kegg enzyme: glucosamine-1-phosphate N-acetyltransferase
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/2.3.1.157
kegg pathway: Aminosugars metabolism
kegg cofactor: Magnesium
kegg substrate: UTP
kegg substrate: N-Acetyl-alpha-D-glucosamine 1-phosphate
kegg substrate: acetyl-CoA
kegg substrate: D-glucosamine 1-phosphate
kegg product: Pyrophosphate
kegg product: UDP-N-acetyl-D-glucosamine
kegg product: CoA
kegg product: N-acetyl-D-glucosamine 1-phosphate
pdb: 1fwyA01
pdb: 1fwyB01
pdb: 1fxjA01
pdb: 1fxjB01
pdb: 1hv9A01
pdb: 1hv9B01
pdb: 1g95A01
pdb: 1g97A01
pdb: 1hm0A01
pdb: 1hm0B01
pdb: 1hm8A01
pdb: 1hm8B01
pdb: 1hm9A01
pdb: 1hm9B01
pdb: 1fwyA02
pdb: 1fwyB02
pdb: 1fxjA02
pdb: 1fxjB02
pdb: 1hv9A02
pdb: 1hv9B02
pdb: 1g95A02
pdb: 1g97A02
pdb: 1hm0A02
pdb: 1hm0B02
pdb: 1hm8A02
pdb: 1hm8B02
pdb: 1hm9A02
pdb: 1hm9B02
pdb bound state: Unbound
  compound: UTP
  pdb: 1fwyA01
pdb bound state: Unbound
  compound: UTP
  pdb: 1fwyB01
pdb bound state: Unbound
  compound: UTP
  pdb: 1fxjA01
pdb bound state: Unbound
  compound: UTP
  pdb: 1fxjB01
pdb bound state: Unbound
  compound: UTP
  pdb: 1hv9A01
active site residues resources: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00417#7
active site residues resources: Purification, crystallization and preliminary X-ray data for Escherichia coli GlmU: a bifunctional acetyltransferase/uridyltransferase.
references: Identification of the glmU gene encoding N-acetylglucosamine-1-phosphate uridyltransferase in Escherichia coli.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00417#2
references: Synthesis of 5-IASA-UDP-GlcNAc and its use for the photoaffinity labeling of a novel UDP-GlcNAc pyrophosphorylase.
references: Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00417#5
references: Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily.
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00417#7
references: http://ezcatdb.cbrc.jp/EzCatDB/reference/D00417#8
references: Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture.
references: Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites
references: Purification, crystallization and preliminary X-ray data for Escherichia coli GlmU: a bifunctional acetyltransferase/uridyltransferase.
references: Crystal structure of Escherichia coli glucose-1-phosphate thymidylyltransferase (RffH) complexed with dTTP and Mg2+.
comment: (B4) Moreover, Ser404 as well as mainchain amide of Ala379 stabilizes the negative charge on the thioester carbonyl during the transition state. This protein is a bifunctional enzyme, catalyzing two sequential reactions, with two distinct domains. The first domain functions as a uridylyltransferase (EC 2.7.7.23), which catalyzes the second reaction, whilst the second domain serve as a acetyltransferase (EC 2.3.1.157) that catalyzes the first one (see [4]). (A) Phosphoryl transfer: Papers [6] & [7] mentioned catalytic mechanism of uridylyltransferase (EC 2.7.7.23). The paper [7] proposed a catalytic mechanism, in which transphosphorylation is assumed to proceed through SN2 mechanism. In the proposed mechanism, the reaction proceeds as follows: (A1) A non-esterified phosphate oxygen atom of GlcNAc-1-P makes a nucleophilic attack on the alpha-phosphate group of UTP, forming penta-coordinated phosphorane transition state with the attacking group and leaving group, pyrophosphate. (A2) Here, the transition state might be stabilized by the positive charge of Mg2+ ion, which is bound to the oxygen atoms from the transferred alpha-phosphate group and attacking phosphate group as well as Asp102 and Asn227 (PDB;1g97), and the sidechain amino group of Lys22 (PDB;1g97). On the other hand, the leaving pyrophosphate can be stabilized by Arg15 (PDB;1g97). (A3) The transfer reaction results in the inversion of the configuration at the alpha-phosphate group. (B) Acyl transfer: Paper [9] proposed a catalytic mechanism for acyltransferase (EC 2.3.1.157). According to the paper [9], the reaction proceeds as follows: (B1) Glu348, hydrogen bonding to His362, might modulate the activity of His362. (B2) His362 (PDB;1hm9) function as a general base, which activates the acceptor amine group of glucosamine-1-P, by abstracting a proton from the amine group. (B3) The amine group can make a nucleophilic attack on the acyl group of acetyl-CoA.

Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.90.550.10
catalytic domain: index.html

UDP N-Acetylglucosamine Acyltransferase; domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.160.10.10
catalytic domain: index.html

Aminosugars metabolism
type: KeggPathway
references: KEGG:MAP00530
ec: https://purl.uniprot.org/enzyme/2.7.7.23
ec: https://purl.uniprot.org/enzyme/2.3.1.157

Magnesium
type: KeggCofactor
references: KEGG:C00305
ec: https://purl.uniprot.org/enzyme/2.7.7.23
compound type: divalent metal (Ca2+, Mg2+)
references: CHEBI:18420
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

UTP
type: KeggSubstrate
references: KEGG:C00075
ec: https://purl.uniprot.org/enzyme/2.7.7.23
compound type: amide group
compound type: nucleotide
references: CHEBI:15713
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

N-Acetyl-alpha-D-glucosamine 1-phosphate
type: KeggSubstrate
references: KEGG:C04501
ec: https://purl.uniprot.org/enzyme/2.7.7.23
compound type: amide group
compound type: carbohydrate
compound type: phosphate group/phosphate ion
references: CHEBI:16446
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

acetyl-CoA
type: KeggSubstrate
references: KEGG:C00024
ec: https://purl.uniprot.org/enzyme/2.3.1.157
compound type: amine group
compound type: carbohydrate
compound type: nucleotide
compound type: peptide/protein
compound type: sulfide group
references: CHEBI:15351
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

D-glucosamine 1-phosphate
type: KeggSubstrate
references: KEGG:C06156
ec: https://purl.uniprot.org/enzyme/2.3.1.157
compound type: amine group
compound type: carbohydrate
compound type: phosphate group/phosphate ion
references: CHEBI:27625
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Pyrophosphate
type: KeggProduct
references: KEGG:C00013
ec: https://purl.uniprot.org/enzyme/2.7.7.23
compound type: phosphate group/phosphate ion
references: CHEBI:29888
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

UDP-N-acetyl-D-glucosamine
type: KeggProduct
references: KEGG:C00043
ec: https://purl.uniprot.org/enzyme/2.7.7.23
compound type: amide group
compound type: carbohydrate
compound type: nucleotide
references: CHEBI:16264
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

CoA
type: KeggProduct
references: KEGG:C00010
ec: https://purl.uniprot.org/enzyme/2.3.1.157
compound type: amine group
compound type: carbohydrate
compound type: nucleotide
compound type: peptide/protein
compound type: sulfhydryl group
references: CHEBI:15346
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

N-acetyl-D-glucosamine 1-phosphate
type: KeggProduct
references: KEGG:C04256
ec: https://purl.uniprot.org/enzyme/2.3.1.157
compound type: amide group
compound type: carbohydrate
compound type: phosphate group/phosphate ion
references: CHEBI:7125
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1fwyA01
type: Pdb
references: 1fwy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fwy
catalytic residue: ARG 18;LYS 25
cofactor binding residue: ASP 105;ASN 227(Magnesium binding)
comment: (2.7.7.23)

1fwyB01
type: Pdb
references: 1fwy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fwy
catalytic residue: ARG 18;LYS 25
cofactor binding residue: ASP 105;ASN 227(Magnesium binding)
comment: (2.7.7.23)

1fxjA01
type: Pdb
references: 1fxj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fxj
catalytic residue: ARG 18;LYS 25
cofactor binding residue: ASP 105;ASN 227(Magnesium binding)
comment: (2.7.7.23)

1fxjB01
type: Pdb
references: 1fxj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fxj
catalytic residue: ARG 18;LYS 25
cofactor binding residue: ASP 105;ASN 227(Magnesium binding)
comment: (2.7.7.23)

1hv9A01
type: Pdb
references: 1hv9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hv9
catalytic residue: ARG 18;LYS 25
cofactor binding residue: ASP 105;ASN 227(Magnesium binding)
comment: (2.7.7.23)

1hv9B01
type: Pdb
references: 1hv9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hv9
catalytic residue: ARG 18;LYS 25
cofactor binding residue: ASP 105;ASN 227(Magnesium binding)
comment: (2.7.7.23)

1g95A01
type: Pdb
references: 1g95
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g95
catalytic residue: ARG 15;LYS 22
cofactor binding residue: ASP 102;ASN 227(Magnesium binding)
comment: (2.7.7.23)

1g97A01
type: Pdb
references: 1g97
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g97
catalytic residue: ARG 15;LYS 22
cofactor binding residue: ASP 102;ASN 227(Magnesium binding)
comment: (2.7.7.23)

1hm0A01
type: Pdb
references: 1hm0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hm0
catalytic residue: ARG 15;LYS 22
cofactor binding residue: ASP 102;ASN 227(Magnesium binding)
comment: (2.7.7.23)

1hm0B01
type: Pdb
references: 1hm0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hm0
catalytic residue: ARG 15;LYS 22
cofactor binding residue: ASP 102;ASN 227(Magnesium binding)
comment: (2.7.7.23)

1hm8A01
type: Pdb
references: 1hm8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hm8
catalytic residue: ARG 15;LYS 22
cofactor binding residue: ASP 102;ASN 227(Magnesium binding)
comment: (2.7.7.23)

1hm8B01
type: Pdb
references: 1hm8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hm8
catalytic residue: ARG 15;LYS 22
cofactor binding residue: ASP 102;ASN 227(Magnesium binding)
comment: (2.7.7.23)

1hm9A01
type: Pdb
references: 1hm9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hm9
catalytic residue: ARG 15;LYS 22
cofactor binding residue: ASP 102;ASN 227(Magnesium binding)
comment: (2.7.7.23)

1hm9B01
type: Pdb
references: 1hm9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hm9
catalytic residue: ARG 15;LYS 22
cofactor binding residue: ASP 102;ASN 227(Magnesium binding)
comment: (2.7.7.23)

1fwyA02
type: Pdb
references: 1fwy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fwy
catalytic residue: ; ;
comment: (2.3.1.157) active-site truncated

1fwyB02
type: Pdb
references: 1fwy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fwy
catalytic residue: ; ;
comment: (2.3.1.157) active-site truncated

1fxjA02
type: Pdb
references: 1fxj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fxj
catalytic residue: ; ;
comment: (2.3.1.157) active-site truncated

1fxjB02
type: Pdb
references: 1fxj
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1fxj
catalytic residue: ; ;
comment: (2.3.1.157) active-site truncated

1hv9A02
type: Pdb
references: 1hv9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hv9
catalytic residue: GLU 349;HIS 363;SER 405
main chain in catalysis: ALA 380
comment: (2.3.1.157)

1hv9B02
type: Pdb
references: 1hv9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hv9
catalytic residue: GLU 349;HIS 363;SER 405
main chain in catalysis: ALA 380
comment: (2.3.1.157)

1g95A02
type: Pdb
references: 1g95
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g95
catalytic residue: GLU 348;HIS 362;SER 404
main chain in catalysis: ALA 379
comment: (2.3.1.157)

1g97A02
type: Pdb
references: 1g97
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1g97
catalytic residue: GLU 348;HIS 362;SER 404
main chain in catalysis: ALA 379
comment: (2.3.1.157)

1hm0A02
type: Pdb
references: 1hm0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hm0
catalytic residue: GLU 348;HIS 362;SER 404
main chain in catalysis: ALA 379
comment: (2.3.1.157)

1hm0B02
type: Pdb
references: 1hm0
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hm0
catalytic residue: GLU 348;HIS 362;SER 404
main chain in catalysis: ALA 379
comment: (2.3.1.157)

1hm8A02
type: Pdb
references: 1hm8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hm8
catalytic residue: GLU 348;HIS 362;SER 404
main chain in catalysis: ALA 379
comment: (2.3.1.157)

1hm8B02
type: Pdb
references: 1hm8
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hm8
catalytic residue: GLU 348;HIS 362;SER 404
main chain in catalysis: ALA 379
comment: (2.3.1.157)

1hm9A02
type: Pdb
references: 1hm9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hm9
catalytic residue: GLU 348;HIS 362;SER 404
main chain in catalysis: ALA 379
comment: (2.3.1.157)

1hm9B02
type: Pdb
references: 1hm9
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hm9
catalytic residue: GLU 348;HIS 362;SER 404
main chain in catalysis: ALA 379
comment: (2.3.1.157)

Identification of the glmU gene encoding N-acetylglucosamine-1-phosphate uridyltransferase in Escherichia coli.
type: BibliographicResource
comment: IDENTIFICATION
medline id: 94012475
references: http://www.ncbi.nlm.nih.gov/pubmed/8407787
journal: J Bacteriol
volume: 175
pages: 6150-7
published year: 1993
authors:
  item: Mengin-Lecreulx D
  item: van Heijenoort J
references: P0ACC7

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00417#2
type: BibliographicResource
comment: CHARACTERIZATION
medline id: 94364959
references: http://www.ncbi.nlm.nih.gov/pubmed/8083170
journal: J Bacteriol
volume: 176
pages: 5788-95
published year: 1994
authors:
  item: Mengin-Lecreulx D
  item: van Heijenoort J
title: Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis.
references: P0ACC7

Synthesis of 5-IASA-UDP-GlcNAc and its use for the photoaffinity labeling of a novel UDP-GlcNAc pyrophosphorylase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7653162
journal: Acta Biochim Pol
volume: 42
pages: 55-9
published year: 1995
authors:
  item: Szumilo H
  item: Szumilo T
  item: Elbein AD

Acetyltransfer precedes uridylyltransfer in the formation of UDP-N-acetylglucosamine in separable active sites of the bifunctional GlmU protein of Escherichia coli.
type: BibliographicResource
comment: CHARACTERIZATION
medline id: 96140233
references: http://www.ncbi.nlm.nih.gov/pubmed/8555230
journal: Biochemistry
volume: 35
pages: 579-85
published year: 1996
authors:
  item: Gehring AM
  item: Lees WJ
  item: Mindiola DJ
  item: Walsh CT
  item: Brown ED
references: P0ACC7

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00417#5
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9733680
journal: J Bacteriol
volume: 180
pages: 4799-803
published year: 1998
authors:
  item: Pompeo F
  item: van Heijenoort J
  item: Mengin-Lecreulx D
title: Probing the role of cysteine residues in glucosamine-1-phosphate acetyltransferase activity of the bifunctional GlmU protein from Escherichia coli: site-directed mutagenesis and characterization of the mutant enzymes.

Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10428949
journal: EMBO J
volume: 18
pages: 4096-107
published year: 1999
authors:
  item: Brown K
  item: Pompeo F
  item: Dixon S
  item: Mengin-Lecreulx D
  item: Cambillau C
  item: Bourne Y
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00417#7
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11124906
journal: J Mol Biol
volume: 305
pages: 279-89
published year: 2001
authors:
  item: Kostrewa D
  item: D'Arcy A
  item: Takacs B
  item: Kamber M
title: Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2.33 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 1.96 A resolution.
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

http://ezcatdb.cbrc.jp/EzCatDB/reference/D00417#8
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11084021
journal: J Biol Chem
volume: 276
pages: 3833-9
published year: 2001
authors:
  item: Pompeo F
  item: Bourne Y
  item: van Heijenoort J
  item: Fassy F
  item: Mengin-Lecreulx D
title: Dissection of the bifunctional Escherichia coli N-acetylglucosamine-1-phosphate uridyltransferase enzyme into autonomously functional domains and evidence that trimerization is absolutely required for glucosamine-1-phosphate acetyltransferase activity and cell growth.

Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11118459
journal: J Biol Chem
volume: 276
pages: 11844-51
published year: 2001
authors:
  item: Sulzenbacher G
  item: Gal L
  item: Peneff C
  item: Fassy F
  item: Bourne Y
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Structure of the Escherichia coli GlmU pyrophosphorylase and acetyltransferase active sites
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11329257
journal: Biochemistry
volume: 40
pages: 1913-21
published year: 2001
authors:
  item: Olsen LR
  item: Roderick SL
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Purification, crystallization and preliminary X-ray data for Escherichia coli GlmU: a bifunctional acetyltransferase/uridyltransferase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11173485
journal: Acta Crystallogr D Biol Crystallogr
volume: 57
pages: 296-7
published year: 2001
authors:
  item: Olsen LR
  item: Tian Y
  item: Roderick SL

Crystal structure of Escherichia coli glucose-1-phosphate thymidylyltransferase (RffH) complexed with dTTP and Mg2+.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12171937
journal: J Biol Chem
volume: 277
pages: 44214-9
published year: 2002
authors:
  item: Sivaraman J
  item: Sauve V
  item: Matte A
  item: Cygler M

Analogue
compound: Magnesium
pdb: 1hv9B01
ligand het code: _CO

Analogue
compound: Magnesium
pdb: 1hm9A01
ligand het code: _CA

Analogue
compound: Magnesium
pdb: 1hm9B01
ligand het code: _CA

Analogue
compound: Pyrophosphate
pdb: 1fxjA01
ligand het code: SO4

Analogue
compound: Pyrophosphate
pdb: 1fxjB01
ligand het code: SO4

ReferenceForCatalyticMechanism
reference index: 6
reference section: p.4100-4102

ReferenceForCatalyticMechanism
reference index: 7
reference section: Fig.7, p.286
reference step: 3

ReferenceForCatalyticMechanism
reference index: 9
reference section: p.11851