M00017
type: Enzyme
cath: Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 3
cath: TATA-Binding Protein
ec: https://purl.uniprot.org/enzyme/5.4.2.2
uniprot: P00949
uniprot: P47244
kegg enzyme: phosphoglucomutase
kegg pathway: Glycolysis / Gluconeogenesis
kegg pathway: Pentose phosphate pathway
kegg pathway: Galactose metabolism
kegg pathway: Starch and sucrose metabolism
kegg pathway: Streptomycin biosynthesis
kegg cofactor: Magnesium
kegg substrate: alpha-D-Glucose 1-phosphate
kegg substrate: alpha-D-Ribose 1-phosphate
kegg substrate: alpha-D-Hexose 1-phosphate
kegg product: alpha-D-Glucose 6-phosphate
kegg product: alpha-D-Ribose 5-phosphate
kegg product: alpha-D-Hexose 6-phosphate
kegg intermediate: D-Glucose 1,6-bisphosphate
pdb: 1c47A01
pdb: 1c47B01
pdb: 1c4gA01
pdb: 1c4gB01
pdb: 1jdyA01
pdb: 1jdyB01
pdb: 1lxtA01
pdb: 1lxtB01
pdb: 1vklA01
pdb: 1vklB01
pdb: 2pmgA01
pdb: 2pmgB01
pdb: 3pmgA01
pdb: 3pmgB01
pdb: 1kfiA01
pdb: 1kfiB01
pdb: 1kfqA01
pdb: 1kfqB01
pdb: 1c47A02
pdb: 1c47B02
pdb: 1c4gA02
pdb: 1c4gB02
pdb: 1jdyA02
pdb: 1jdyB02
pdb: 1lxtA02
pdb: 1lxtB02
pdb: 1vklA02
pdb: 1vklB02
pdb: 2pmgA02
pdb: 2pmgB02
pdb: 3pmgA02
pdb: 3pmgB02
pdb: 1kfiA02
pdb: 1kfiB02
pdb: 1kfqA02
pdb: 1kfqB02
pdb: 1c47A03
pdb: 1c47B03
pdb: 1c4gA03
pdb: 1c4gB03
pdb: 1jdyA03
pdb: 1jdyB03
pdb: 1lxtA03
pdb: 1lxtB03
pdb: 1vklA03
pdb: 1vklB03
pdb: 2pmgA03
pdb: 2pmgB03
pdb: 3pmgA03
pdb: 3pmgB03
pdb: 1kfiA03
pdb: 1kfiB03
pdb: 1kfqA03
pdb: 1kfqB03
pdb: 1c47A04
pdb: 1c47B04
pdb: 1c4gA04
pdb: 1c4gB04
pdb: 1jdyA04
pdb: 1jdyB04

Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 3
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.120.10
catalytic domain: index.html

TATA-Binding Protein
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.310.50

Glycolysis / Gluconeogenesis
type: KeggPathway
references: KEGG:MAP00010

Pentose phosphate pathway
type: KeggPathway
references: KEGG:MAP00030

Galactose metabolism
type: KeggPathway
references: KEGG:MAP00052

Starch and sucrose metabolism
type: KeggPathway
references: KEGG:MAP00500

Streptomycin biosynthesis
type: KeggPathway
references: KEGG:MAP00521

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

alpha-D-Glucose 1-phosphate
type: KeggSubstrate
references: KEGG:C00103
references: CHEBI:29042
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: carbohydrate
compound type: phosphate group/phosphate ion

alpha-D-Ribose 1-phosphate
type: KeggSubstrate
references: KEGG:C00620
references: CHEBI:16300
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: carbohydrate
compound type: phosphate group/phosphate ion

alpha-D-Hexose 1-phosphate
type: KeggSubstrate
references: KEGG:C01171
references: CHEBI:16326
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: carbohydrate
compound type: phosphate group/phosphate ion

alpha-D-Glucose 6-phosphate
type: KeggProduct
references: KEGG:C00668
references: CHEBI:17665
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: carbohydrate
compound type: phosphate group/phosphate ion

alpha-D-Ribose 5-phosphate
type: KeggProduct
references: KEGG:C03736
references: CHEBI:18189
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: carbohydrate
compound type: phosphate group/phosphate ion

alpha-D-Hexose 6-phosphate
type: KeggProduct
references: KEGG:C03735
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
compound type: carbohydrate
compound type: phosphate group/phosphate ion

D-Glucose 1,6-bisphosphate
type: KeggIntermediate
references: KEGG:C00660

1c47A01
type: Pdb
references: 1c47
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c47
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)

1c47B01
type: Pdb
references: 1c47
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c47
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)

1c4gA01
type: Pdb
references: 1c4g
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4g
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)

1c4gB01
type: Pdb
references: 1c4g
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4g
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)

1jdyA01
type: Pdb
references: 1jdy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jdy
catalytic residue: ARG 22; ;HIS 117;LYS 129
cofactor binding residue: SEP 116(Magnesium binding)
modified residue: SEP 116(Phosphonoserine)

1jdyB01
type: Pdb
references: 1jdy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jdy
catalytic residue: ARG 22; ;HIS 117;LYS 129
cofactor binding residue: SEP 116(Magnesium binding)
modified residue: SEP 116(Phosphonoserine)

1lxtA01
type: Pdb
references: 1lxt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lxt
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)

1lxtB01
type: Pdb
references: 1lxt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lxt
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)

1vklA01
type: Pdb
references: 1vkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vkl
catalytic residue: ARG 22; ;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)
modified residue: SEP 116(Phosphonoserine)

1vklB01
type: Pdb
references: 1vkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vkl
catalytic residue: ARG 22; ;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)
modified residue: SEP 116(Phosphonoserine)

2pmgA01
type: Pdb
references: 2pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2pmg
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)

2pmgB01
type: Pdb
references: 2pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2pmg
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)

3pmgA01
type: Pdb
references: 3pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3pmg
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)
modified residue: SEP 116(Phosphorylation)

3pmgB01
type: Pdb
references: 3pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3pmg
catalytic residue: ARG 22;SER 116;HIS 117;LYS 129
cofactor binding residue: SER 116(Magnesium binding)
modified residue: SEP 116(Phosphorylation)

1kfiA01
type: Pdb
references: 1kfi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfi
catalytic residue: ARG 27;SER 126;HIS 127;LYS 140
cofactor binding residue: SER 126(Magnesium binding)
modified residue: SER 126(Phosphorylation)

1kfiB01
type: Pdb
references: 1kfi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfi
catalytic residue: ARG 27;SER 126;HIS 127;LYS 140
cofactor binding residue: SER 126(Magnesium binding)
modified residue: SER 126(Phosphorylation)

1kfqA01
type: Pdb
references: 1kfq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfq
catalytic residue: ARG 27;SER 126;HIS 127;LYS 140
cofactor binding residue: SER 126(Magnesium binding)
modified residue: SER 126(Phosphorylation)

1kfqB01
type: Pdb
references: 1kfq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfq
catalytic residue: ARG 27;SER 126;HIS 127;LYS 140
cofactor binding residue: SER 126(Magnesium binding)
modified residue: SER 126(Phosphorylation)

1c47A02
type: Pdb
references: 1c47
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c47
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)

1c47B02
type: Pdb
references: 1c47
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c47
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)

1c4gA02
type: Pdb
references: 1c4g
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4g
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)

1c4gB02
type: Pdb
references: 1c4g
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4g
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)

1jdyA02
type: Pdb
references: 1jdy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jdy
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)

1jdyB02
type: Pdb
references: 1jdy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jdy
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)

1lxtA02
type: Pdb
references: 1lxt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lxt
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)

1lxtB02
type: Pdb
references: 1lxt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lxt
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)

1vklA02
type: Pdb
references: 1vkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vkl
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)

1vklB02
type: Pdb
references: 1vkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vkl
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)

2pmgA02
type: Pdb
references: 2pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2pmg
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)

2pmgB02
type: Pdb
references: 2pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2pmg
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)

3pmgA02
type: Pdb
references: 3pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3pmg
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)

3pmgB02
type: Pdb
references: 3pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3pmg
catalytic residue: ARG 292
cofactor binding residue: ASP 287;ASP 289;ASP 291(Magnesium binding)

1kfiA02
type: Pdb
references: 1kfi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfi
catalytic residue: ARG 313
cofactor binding residue: ASP 308;ASP 310;ASP 312(Magnesium binding)

1kfiB02
type: Pdb
references: 1kfi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfi
catalytic residue: ARG 313
cofactor binding residue: ASP 308;ASP 310;ASP 312(Magnesium binding)

1kfqA02
type: Pdb
references: 1kfq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfq
catalytic residue: ARG 313
cofactor binding residue: ASP 308;ASP 310;ASP 312(Magnesium binding)

1kfqB02
type: Pdb
references: 1kfq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfq
catalytic residue: ARG 313
cofactor binding residue: ASP 308;ASP 310;ASP 312(Magnesium binding)

1c47A03
type: Pdb
references: 1c47
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c47
catalytic residue: LYS 388

1c47B03
type: Pdb
references: 1c47
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c47
catalytic residue: LYS 388

1c4gA03
type: Pdb
references: 1c4g
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4g
catalytic residue: LYS 388

1c4gB03
type: Pdb
references: 1c4g
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1c4g
catalytic residue: LYS 388

1jdyA03
type: Pdb
references: 1jdy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jdy
catalytic residue: LYS 388

1jdyB03
type: Pdb
references: 1jdy
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jdy
catalytic residue: LYS 388

1lxtA03
type: Pdb
references: 1lxt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lxt
catalytic residue: LYS 388

1lxtB03
type: Pdb
references: 1lxt
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1lxt
catalytic residue: LYS 388

1vklA03
type: Pdb
references: 1vkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vkl
catalytic residue: LYS 388

1vklB03
type: Pdb
references: 1vkl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1vkl
catalytic residue: LYS 388

2pmgA03
type: Pdb
references: 2pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2pmg
catalytic residue: LYS 388

2pmgB03
type: Pdb
references: 2pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:2pmg
catalytic residue: LYS 388

3pmgA03
type: Pdb
references: 3pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3pmg
catalytic residue: LYS 388

3pmgB03
type: Pdb
references: 3pmg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:3pmg
catalytic residue: LYS 388

1kfiA03
type: Pdb
references: 1kfi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfi
catalytic residue: LYS 405

1kfiB03
type: Pdb
references: 1kfi
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfi
catalytic residue: LYS 405

1kfqA03
type: Pdb
references: 1kfq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfq
catalytic residue: LYS 405

1kfqB03
type: Pdb
references: 1kfq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kfq
catalytic residue: LYS 405

Analogue
compound: alpha-D-Glucose 1-phosphate
pdb: 1jdyA04
ligand het code: SO4

Analogue
compound: alpha-D-Glucose 1-phosphate
pdb: 1jdyB04
ligand het code: SO4

Analogue
compound: alpha-D-Glucose 1-phosphate
pdb: 1kfiA04
ligand het code: SO4

Analogue
compound: alpha-D-Glucose 1-phosphate
pdb: 1kfiB04
ligand het code: SO4

Analogue
compound: Magnesium
pdb: 1c47A02
ligand het code: _CD

Analogue
compound: Magnesium
pdb: 1c47B02
ligand het code: _CD

Analogue
compound: Magnesium
pdb: 1c4gA02
ligand het code: _CO

Analogue
compound: Magnesium
pdb: 1jdyA02
ligand het code: _CD

Analogue
compound: Magnesium
pdb: 1jdyB02
ligand het code: _CD

Analogue
compound: Magnesium
pdb: 1lxtA02
ligand het code: _CD

Analogue
compound: Magnesium
pdb: 1lxtB02
ligand het code: _CD

Analogue
compound: Magnesium
pdb: 1vklA02
ligand het code: _NI

Analogue
compound: Magnesium
pdb: 1vklB02
ligand het code: _NI

Analogue
compound: Magnesium
pdb: 1kfiA02
ligand het code: _ZN

Analogue
compound: Magnesium
pdb: 1kfiB02
ligand het code: _ZN

Analogue
compound: Magnesium
pdb: 1kfqA02
ligand het code: _CA

Analogue
compound: Magnesium
pdb: 1kfqB02
ligand het code: _CA

IntermediateBound
compound: D-Glucose 1,6-bisphosphate
pdb: 1c47A03
ligand het code: G16

TransitionStateAnalogue
pdb: 1c4gA03
ligand het code: VG1

Functional diversity of the phosphoglucomutase superfamily: structural implications.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10506283
journal: Protein Eng
volume: 12
pages: 737-46
published year: 1999
authors:
  item: Levin S
  item: Almo SC
  item: Satir BH

Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11839312
journal: Structure (Camb)
volume: 10
pages: 269-79
published year: 2002
authors:
  item: Regni C
  item: Tipton PA
  item: Beamer LJ

Roles of active site residues in Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12924943
journal: Biochemistry
volume: 42
pages: 9946-51
published year: 2003
authors:
  item: Naught LE
  item: Regni C
  item: Beamer LJ
  item: Tipton PA

ReferenceForCatalyticMechanism
reference index: 9
reference section: Scheme II, p.504

ReferenceForCatalyticMechanism
reference index: 10
reference section: p.511-512

ReferenceForCatalyticMechanism
reference index: 11
reference section: p.6328-6329

ReferenceForCatalyticMechanism
reference index: 12
reference section: p.52-55

ReferenceForCatalyticMechanism
reference index: 14
reference section: p.404-405

ReferenceForCatalyticMechanism
reference index: 16
reference section: p.148

ReferenceForCatalyticMechanism
reference index: 17
reference section: Fig.5, p.275-277

ReferenceForCatalyticMechanism
reference index: 18
reference section: Chart 1, p.9948-9950

ReferenceForCatalyticMechanism
reference index: 19
reference section: Fig.1, p.60-61

A tryptic peptide containing a unique serine phosphate residue in rabbit phosphoglucomutase.
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comment: ACTIVE SITE
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Cobalt (II) and nickel (II) complexes of phosphoglucomutase.
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journal: Biochemistry
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pages: 2800-4
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Mechanism of action of rabbit muscle phosphoglucomutase. Rate of enzyme phosphate turnover studied with a rapid mixing technique.
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  item: Ray WJ Jr

The structure of rabbit muscle phosphoglucomutase at intermediate resolution.
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Mechanism-based inactivation of rabbit muscle phosphoglucomutase by nojirimycin 6-phosphate.
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Removal of salt from a salt-induced protein crystal without cross-linking. Preliminary examination of "desalted" crystals of phosphoglucomutase by X-ray crystallography at low temperature.
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journal: Biochemistry
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Formation of substrate and transition-state analogue complexes in crystals of phosphoglucomutase after removing the crystallization salt.
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journal: Biochemistry
volume: 30
pages: 6875-85
published year: 1991
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Binding energy and catalysis: deoxyfluoro sugars as probes of hydrogen bonding in phosphoglucomutase.
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journal: Biochemistry
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pages: 498-505
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19F NMR investigations of the catalytic mechanism of phosphoglucomutase using fluorinated substrates and inhibitors.
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journal: Biochemistry
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The crystal structure of muscle phosphoglucomutase refined at 2.7-angstrom resolution.
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comment: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS)
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Structural changes at the metal ion binding site during the phosphoglucomutase reaction.
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Reaction of the isosteric methylenephosphonate analog of alpha-D-glucose 1-phosphate with phosphoglucomutase. Induced-fit specificity revisited.
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journal: Biochemistry
volume: 32
pages: 38-47
published year: 1993
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Structure of rabbit muscle phosphoglucomutase refined at 2.4-A
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comment: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)
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Crystal structure analysis of the exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutase), from Paramecium reveals significant conformational variability.
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Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa.
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references: http://www.ncbi.nlm.nih.gov/pubmed/14725765
journal: Structure (Camb)
volume: 12
pages: 55-63
published year: 2004
authors:
  item: Regni C
  item: Naught L
  item: Tipton PA
  item: Beamer LJ

glucose phosphomutase
type: KeggEnzyme

phosphoglucose mutase
type: KeggEnzyme