EzCatDB: D00243

DB codeD00243
CATH domainDomain 13.40.50.1170Catalytic domain
Domain 23.40.50.40Catalytic domain
E.C.3.5.1.38
CSA1djo
MACiEM0029


Enzyme Name
Swiss-protKEGG

P10172P10182
Protein nameGlutaminase-asparaginaseGlutaminase-asparaginaseglutamin-(asparagin-)ase
SynonymsEC 3.5.1.38
L-ASNase/L-GLNase
L-asparagine/L-glutamine amidohydrolase
EC 3.5.1.38
L-ASNase/L-GLNase
L-asparagine/L-glutamine amidohydrolase
PGA

KEGG pathways
MAP codePathways
MAP00251Glutamate metabolism
MAP00252Alanine and aspartate metabolism
MAP00471D-Glutamine and D-glutamate metabolism
MAP00910Nitrogen metabolism

Swiss-prot:Accession NumberP10172P10182
Entry nameASPQ_ACIGLASPQ_PSES7
ActivityL-glutamine + H(2)O = L-glutamate + NH(3).,L-asparagine + H(2)O = L-aspartate + NH(3).L-glutamine + H(2)O = L-glutamate + NH(3).,L-asparagine + H(2)O = L-aspartate + NH(3).
SubunitHomotetramer.Homotetramer.
Subcellular locationPeriplasm (By similarity).Periplasm.
Cofactor



SubstratesProductsintermediates
KEGG-idC00064C00152C00001C00025C00049C00014
CompoundL-GlutamineL-AsparagineH2OL-GlutamateL-AspartateNH3
Typeamino acids,amide groupamino acids,amide groupH2Oamino acids,carboxyl groupamino acids,carboxyl groupamine group,organic ion
1agxA01UnboundUnbound
UnboundUnboundUnboundUnbound
1djoA01UnboundUnbound
UnboundUnboundUnboundIntermediate-analogue:CAB
1djoB01UnboundUnbound
UnboundUnboundUnboundIntermediate-analogue:CAB
1djpA01UnboundUnbound
UnboundUnboundUnboundIntermediate-analogue:DO2
1djpB01UnboundUnbound
UnboundUnboundUnboundIntermediate-analogue:DO2
3pga101UnboundUnbound
UnboundUnboundUnboundUnbound
3pga201UnboundUnbound
UnboundUnboundUnboundUnbound
3pga301UnboundUnbound
UnboundUnboundUnboundUnbound
3pga401UnboundUnbound
UnboundUnboundUnboundUnbound
4pgaA01UnboundUnbound
UnboundAnalogue:SO4-NH4UnboundUnbound
4pgaB01UnboundUnbound
UnboundAnalogue:SO4-NH4UnboundUnbound
1agxA02UnboundUnbound
UnboundUnboundUnboundUnbound
1djoA02UnboundUnbound
UnboundUnboundUnboundUnbound
1djoB02UnboundUnbound
UnboundUnboundUnboundUnbound
1djpA02UnboundUnbound
UnboundUnboundUnboundUnbound
1djpB02UnboundUnbound
UnboundUnboundUnboundUnbound
3pga102UnboundUnbound
UnboundUnboundUnboundUnbound
3pga202UnboundUnbound
UnboundUnboundUnboundUnbound
3pga302UnboundUnbound
UnboundUnboundUnboundUnbound
3pga402UnboundUnbound
UnboundUnboundUnboundUnbound
4pgaA02UnboundUnbound
UnboundUnboundUnboundUnbound
4pgaB02UnboundUnbound
UnboundUnboundUnboundUnbound

Active-site residues
resource
PDB;3pga,4pga & Swiss-prot;P10172,P10182 & Leterature [7],[10]
pdbCatalytic residues
1agxA01THR   12;TYR   26;THR   92;ASP   93;LYS  165
1djoA01THR 1020;TYR 1034;THR 1100;ASP 1101;LYS 1173
1djoB01THR 3020;TYR 3034;THR 3100;ASP 3101;LYS 3173
1djpA01THR 1020;TYR 1034;THR 1100;ASP 1101;LYS 1173
1djpB01THR 3020;TYR 3034;THR 3100;ASP 3101;LYS 3173
3pga101THR   20;TYR   34;THR  100;ASP  101;LYS  173
3pga201THR   20;TYR   34;THR  100;ASP  101;LYS  173
3pga301THR   20;TYR   34;THR  100;ASP  101;LYS  173
3pga401THR   20;TYR   34;THR  100;ASP  101;LYS  173
4pgaA01THR   20;TYR   34;THR  100;ASP  101;LYS  173
4pgaB01THR   20;TYR   34;THR  100;ASP  101;LYS  173
1agxA02GLU  288
1djoA02GLU 1294
1djoB02GLU 3294
1djpA02GLU 1294
1djpB02GLU 3294
3pga102GLU  294
3pga202GLU  294
3pga302GLU  294
3pga402GLU  294
4pgaA02GLU  294
4pgaB02GLU  294

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[7]p.831-832
[8]p.10262-10264
[9]p.928-930
[10]Scheme 3, p.1203-1204

references
[1]
PubMed ID5017769
JournalJ Biol Chem
Year1972
Volume247
Pages84-90
AuthorsRoberts J, Holcenberg JS, Dolowy WC
TitleIsolation, crystallization, and properties of Achromobacteraceae glutaminase-asparaginase with antitumor activity.
[2]
PubMed ID5441
JournalJ Biol Chem
Year1976
Volume251
Pages2119-23
AuthorsRoberts J
TitlePurification and properties of a highly potent antitumor glutaminase-asparaginase from Pseudomonas 7Z.
[3]
PubMed ID875029
JournalJ Mol Biol
Year1977
Volume112
Pages515-9
AuthorsWlodawer A, Roberts J, Holcenberg JS
TitleCharacterization of crystals of L-glutaminase-asparaginase from Acinetobacter glutaminasificans and Pseudomonas 7A.
[4]
PubMed ID619999
JournalBiochemistry
Year1978
Volume17
Pages411-7
AuthorsHolcenberg JS, Ericsson L, Roberts J
TitleAmino acid sequence of the diazooxonorleucine binding site of Acinetobacter and Pseudomonas 7A glutaminase--asparaginase enzymes.
[5]
PubMed ID3275637
JournalJ Biol Chem
Year1988
Volume263
Pages150-6
AuthorsAmmon HL, Weber IT, Wlodawer A, Harrison RW, Gilliland GL, Murphy KC, Sjolin L, Roberts J
TitlePreliminary crystal structure of Acinetobacter glutaminasificans glutaminase-asparaginase.
[6]
CommentsPROTEIN SEQUENCE
PubMed ID3379033
JournalJ Biol Chem
Year1988
Volume263
Pages8583-91
AuthorsTanaka S, Robinson EA, Appella E, Miller M, Ammon HL, Roberts J, Weber IT, Wlodawer A
TitleStructures of amidohydrolases. Amino acid sequence of a glutaminase-asparaginase from Acinetobacter glutaminasificans and preliminary crystallographic data for an asparaginase from Erwinia chrysanthemi.
[7]
CommentsX-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS)
PubMed ID15299349
JournalActa Crystallogr D Biol Crystallogr
Year1994
Volume50
Pages826-32
AuthorsLubkowski J, Wlodawer A, Housset D, Weber IT, Ammon HL, Murphy KC, Swain AL
TitleRefined crystal structure of Acinetobacter glutaminasificans glutaminase-asparaginase.
Related PDB1agx
Related Swiss-protP10172
[8]
CommentsPROTEIN SEQUENCE, AND X-ray crystallography (2.0 ANGSTROMS)
PubMed ID8068664
JournalBiochemistry
Year1994
Volume33
Pages10257-65
AuthorsLubkowski J, Wlodawer A, Ammon HL, Copeland TD, Swain AL
TitleStructural characterization of Pseudomonas 7A glutaminase-asparaginase.
Related PDB3pga
[9]
CommentsX-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS)
Medline ID9020792
PubMed ID9020792
JournalBiochemistry
Year1997
Volume36
Pages923-31
AuthorsJakob CG, Lewinski K, LaCount MW, Roberts J, Lebioda L
TitleIon binding induces closed conformation in Pseudomonas 7A glutaminase-asparaginase (PGA): crystal structure of the PGA-SO4(2-)-NH4+ complex at 1.7 A resolution.
Related PDB4pga
Related Swiss-protP10182
[10]
CommentsX-ray crystallography
PubMed ID10684596
JournalBiochemistry
Year2000
Volume39
Pages1199-204
AuthorsOrtlund E, Lacount MW, Lewinski K, Lebioda L
TitleReactions of Pseudomonas 7A glutaminase-asparaginase with diazo analogues of glutamine and asparagine result in unexpected covalent inhibitions and suggests an unusual catalytic triad Thr-Tyr-Glu.
Related PDB1djo,1djp

comments
This enzyme catalyzes hydrolysis of amide bond.
According to the literature [10], Thr20 (of 3pga) acts as a nuclephile, whereas there are two sets of acid-base/modulator, Tyr34/Glu294' (from the adjacent subunit) and Lys173/Asp101. (Thr100 might be a proton shuttle.)

createdupdated
2004-03-242009-02-26


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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
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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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