EzCatDB: S00367

DB codeS00367
CATH domainDomain 13.40.50.1360Catalytic domain
E.C.3.5.99.6
CSA1cd5
MACiEM0060


Enzyme Name
Swiss-protKEGG

P46926P0A759
Protein nameGlucosamine-6-phosphate isomerase 1Glucosamine-6-phosphate deaminaseglucosamine-6-phosphate deaminase
glucosaminephosphate isomerase
glucosamine-6-phosphate isomerase
phosphoglucosaminisomerase
glucosamine phosphate deaminase
aminodeoxyglucosephosphate isomerase
phosphoglucosamine isomerase
SynonymsEC 3.5.99.6
Glucosamine-6-phosphate deaminase 1
GlcN6P deaminase 1
GNPDA 1
Oscillin
EC 3.5.99.6
Glucosamine-6-phosphate isomerase
GlcN6P deaminase
GNPDA

KEGG pathways
MAP codePathways
MAP00530Aminosugars metabolism

Swiss-prot:Accession NumberP46926P0A759
Entry nameGNPI1_HUMANNAGB_ECOLI
ActivityD-glucosamine 6-phosphate + H(2)O = D-fructose 6-phosphate + NH(3).D-glucosamine 6-phosphate + H(2)O = D-fructose 6-phosphate + NH(3).
SubunitHomohexamer.Homohexamer, trimer of disulfide-linked dimers.
Subcellular locationCytoplasm (By similarity).
Cofactor



SubstratesProducts
KEGG-idC00001C00352C00014C00085
CompoundH2OD-Glucosamine 6-phosphateNH3D-Fructose 6-phosphate
TypeH2Oamine group,carbohydrate,phosphate group/phosphate ionamine group,organic ioncarbohydrate,phosphate group/phosphate ion
1cd5A
UnboundUnboundUnbound
1deaA
UnboundUnboundUnbound
1deaB
UnboundUnboundUnbound
1horA
Bound:AGPUnboundUnbound
1horB
Bound:AGPUnboundUnbound
1hotA
UnboundUnboundUnbound
1hotB
UnboundUnboundUnbound
1fqoA
UnboundUnboundBound:FPC
1fqoB
UnboundUnboundBound:FPC
1frzA
UnboundUnboundUnbound
1frzB
UnboundUnboundUnbound
1fs5A
UnboundUnboundUnbound
1fs5B
UnboundUnboundUnbound
1fs6A
UnboundUnboundUnbound
1fsfA
UnboundUnboundUnbound
1jt9A
UnboundUnboundUnbound
1ne7A
Bound:AGPUnboundUnbound
1ne7B
Bound:AGPUnboundUnbound
1ne7C
Bound:AGPUnboundUnbound
1ne7D
Bound:AGPUnboundUnbound
1ne7E
Bound:AGPUnboundUnbound
1ne7F
Bound:AGPUnboundUnbound

Active-site residues
resource
Swiss-prot P0A759, P46926 & literature [7], [9]
pdbCatalytic residues
1cd5AASP 72;ASP 141;HIS 143;GLU 148
1deaAASP 72;ASP 141;HIS 143;GLU 148
1deaBASP 72;ASP 141;HIS 143;GLU 148
1horAASP 72;ASP 141;HIS 143;GLU 148
1horBASP 72;ASP 141;HIS 143;GLU 148
1hotAASP 72;ASP 141;HIS 143;GLU 148
1hotBASP 72;ASP 141;HIS 143;GLU 148
1fqoAASP 72;ASP 141;HIS 143;GLU 148
1fqoBASP 72;ASP 141;HIS 143;GLU 148
1frzAASP 72;ASP 141;HIS 143;GLU 148
1frzBASP 72;ASP 141;HIS 143;GLU 148
1fs5AASP 72;ASP 141;HIS 143;GLU 148
1fs5BASP 72;ASP 141;HIS 143;GLU 148
1fs6AASP 72;ASP 141;HIS 143;GLU 148
1fsfAASP 72;ASP 141;HIS 143;GLU 148
1jt9AASP 72;ASP 141;HIS 143;GLU 148
1ne7AASP 72;ASP 141;HIS 143;GLU 148
1ne7BASP 72;ASP 141;HIS 143;GLU 148
1ne7CASP 72;ASP 141;HIS 143;GLU 148
1ne7DASP 72;ASP 141;HIS 143;GLU 148
1ne7EASP 72;ASP 141;HIS 143;GLU 148
1ne7FASP 72;ASP 141;HIS 143;GLU 148

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[7]Fig.5, p.1329-13307
[10]p.222
[12]Fig.1, p.10194-101967

references
[1]
PubMed ID2821923
JournalArch Biochem Biophys
Year1987
Volume258
Pages95-100
AuthorsAltamirano MM, Mulliert G, Calcagno M
TitleSulfhydryl groups of glucosamine-6-phosphate isomerase deaminase from Escherichia coli.
[2]
PubMed ID2111170
JournalBiochim Biophys Acta
Year1990
Volume1038
Pages291-4
AuthorsAltamirano MM, Calcagno M
TitleZinc binding and its trapping by allosteric transition in glucosamine-6-phosphate deaminase from Escherichia coli.
[3]
CommentsMUTAGENESIS OF CYS-118 AND CYS-239.
Medline ID92135199
PubMed ID1734962
JournalBiochemistry
Year1992
Volume31
Pages1153-8
AuthorsAltamirano MM, Plumbridge JA, Calcagno ML
TitleIdentification of two cysteine residues forming a pair of vicinal thiols in glucosamine-6-phosphate deaminase from Escherichia coli and a study of their functional role by site-directed mutagenesis.
Related Swiss-protP0A759
[4]
PubMed ID1518057
JournalJ Mol Biol
Year1992
Volume226
Pages1283-6
AuthorsHorjales E, Altamirano MM, Calcagno ML, Dauter Z, Wilson K, Garratt RC, Oliva G
TitleCrystallization and preliminary crystallographic studies of glucosamine-6-phosphate deaminase from Escherichia coli K12.
[5]
CommentsDISULFIDE BONDS.
Medline ID94059012
PubMed ID8240271
JournalBiochem J
Year1993
Volume295
Pages645-8
AuthorsAltamirano MM, Plumbridge JA, Barba HA, Calcagno ML
TitleGlucosamine-6-phosphate deaminase from Escherichia coli has a trimer of dimers structure with three intersubunit disulphides.
Related Swiss-protP0A759
[6]
PubMed ID8125098
JournalEur J Biochem
Year1994
Volume220
Pages409-13
AuthorsAltamirano MM, Hernandez-Arana A, Tello-Solis S, Calcagno ML
TitleSpectrochemical evidence for the presence of a tyrosine residue in the allosteric site of glucosamine-6-phosphate deaminase from Escherichia coli.
[7]
CommentsX-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH THE INHIBITOR 2-AMINO-2-DEOXY-D-GLUCITOL-6-PHOSPHATE.
Medline ID96363670
PubMed ID8747459
JournalStructure
Year1995
Volume3
Pages1323-32
AuthorsOliva G, Fontes MR, Garratt RC, Altamirano MM, Calcagno ML, Horjales E
TitleStructure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution.
Related PDB1dea,1hor,1hot
Related Swiss-protP0A759
[8]
PubMed ID9601045
JournalBiochemistry
Year1998
Volume37
Pages7844-9
AuthorsMontero-Moran GM, Horjales E, Calcagno ML, Altamirano MM
TitleTyr254 hydroxyl group acts as a two-way switch mechanism in the coupling of heterotropic and homotropic effects in Escherichia coli glucosamine-6-phosphate deaminase.
[9]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID99306035
PubMed ID10378272
JournalStructure Fold Des
Year1999
Volume7
Pages527-37
AuthorsHorjales E, Altamirano MM, Calcagno ML, Garratt RC, Oliva G
TitleThe allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3 A resolution.
Related PDB1cd5
Related Swiss-protP0A759
[10]
PubMed ID10926504
JournalJ Mol Biol
Year2000
Volume301
Pages219-27
AuthorsLara-Gonzalez S, Dixon HB, Mendoza-Hernandez G, Altamirano MM, Calcagno ML
TitleOn the role of the N-terminal group in the allosteric function of glucosamine-6-phosphate deaminase from Escherichia coli.
[11]
PubMed ID11594728
JournalArch Biochem Biophys
Year2001
Volume394
Pages156-60
AuthorsBustos-Jaimes I, Calcagno ML
TitleAllosteric transition and substrate binding are entropy-driven in glucosamine-6-phosphate deaminase from Escherichia coli.
[12]
CommentsACTIVE SITES, AND MUTAGENESIS OF ASP-141; HIS-143 AND GLU-148.
Medline ID21404989
PubMed ID11513596
JournalBiochemistry
Year2001
Volume40
Pages10187-96
AuthorsMontero-Moran GM, Lara-Gonzalez S, Alvarez-Anorve LI, Plumbridge JA, Calcagno ML
TitleOn the multiple functional roles of the active site histidine in catalysis and allosteric regulation of Escherichia coli glucosamine 6-phosphate deaminase.
Related Swiss-protP0A759
[13]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES WITH FRUCTOSE-6-PHOSPHATE AND N-ACETYLGLUCOSAMINE-6-PHOSPHATE.
Medline ID21620768
PubMed ID11752775
JournalActa Crystallogr D Biol Crystallogr
Year2002
Volume58
Pages10-20
AuthorsRudino-Pinera E, Morales-Arrieta S, Rojas-Trejo SP, Horjales E
TitleStructural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase.
Related PDB1fqo,1frz,1fs5,1fs6,1fsf
Related Swiss-protP0A759
[14]
CommentsX-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF MUTANT F174A.
Medline ID22047883
PubMed ID12051945
JournalJ Mol Biol
Year2002
Volume319
Pages183-9
AuthorsBustos-Jaimes I, Sosa-Peinado A, Rudino-Pinera E, Horjales E, Calcagno ML
TitleOn the role of the conformational flexibility of the active-site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase.
Related PDB1jt9
Related Swiss-protP0A759
[15]
PubMed ID12965206
JournalFEBS Lett
Year2003
Volume551
Pages63-70
AuthorsArreola R, Valderrama B, Morante ML, Horjales E
TitleTwo mammalian glucosamine-6-phosphate deaminases: a structural and genetic study.
[16]
PubMed ID14678787
JournalArch Biochem Biophys
Year2004
Volume421
Pages77-84
AuthorsCisneros DA, Montero-Moran GM, Lara-Gonzalez S, Calcagno ML
TitleInversion of the allosteric response of Escherichia coli glucosamine-6-P deaminase to N-acetylglucosamine 6-P, by single amino acid replacements.

comments
Although this enzyme is classified into hydrolases, it does not catalyzes ordinary "hydrolysis" reaction.
According to the literature [7] & [12], this enzyme catalyzes the following reactions.
(A) Isomerization (open ring), or Elimination of hydroxyl group accompanied by double-bond formation
(B) Isomerization (change in the position of double-bond), to form Schiff-base (adlimine),
(C) Schiff-base dehydration,
(D) Isomerization (close ring), or addition to double-bond.

createdupdated
2004-08-132009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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