Enzyme

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     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.1 In linear amides
ID:3.5.1.1
Description:Asparaginase.
Alternative Name: L-asparagine amidohydrolase.
L-asparaginase.
Prosite: PDOC00132;
PDB:
PDBScop
5I48 8031697; 8044075; 8031697; 8044075; 8031697; 8044075; 8031697; 8044075;
5I3Z 8031697; 8044075; 8031697; 8044075; 8031697; 8044075; 8031697; 8044075;
5HW0 8031697; 8044075; 8031697; 8044075; 8031697; 8044075; 8031697; 8044075;
5F52 8031697; 8044075; 8031697; 8044075; 8031697; 8044075; 8031697; 8044075;
1O7J 8031697; 8044075; 8031697; 8044075; 8031697; 8044075; 8031697; 8044075;
 » show all

Cath: 3.10.450.50; 3.40.50.40; 3.40.50.1170;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.1.1
BRENDA Enzyme Link: BRENDA 3.5.1.1
KEGG Enzyme Link: KEGG3.5.1.1
BioCyc Enzyme Link: BioCyc 3.5.1.1
ExPASy Enzyme Link: ExPASy3.5.1.1
EC2PDB Enzyme Link: EC2PDB 3.5.1.1
ExplorEnz Enzyme Link: ExplorEnz 3.5.1.1
PRIAM enzyme-specific profiles Link: PRIAM 3.5.1.1
IntEnz Enzyme Link: IntEnz 3.5.1.1
MEDLINE Enzyme Link: MEDLINE 3.5.1.1
MSA:

3.5.1.1;

Phylogenetic Tree:

3.5.1.1;

Uniprot:
M-CSA:
RHEA:21016 H2O + L-asparagine = L-aspartate + NH4(+)
RULE(radius=1) [*:1]-[C;H0;+0:2](=[*:3])-[NH2;+0:4].[OH2;+0:5]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:5].[NH3;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Cloning and expression of cDNA encoding rat liver 60-kDa lysophospholipase containing an asparaginase-like region and ankyrin repeat.Sugimoto H, Odani S, Yamashita S1998 May 159575212
Structural characterization of Pseudomonas 7A glutaminase-asparaginase.Lubkowski J, Wlodawer A, Ammon HL, Copeland TD, Swain AL1994 Aug 308068664
Structures of amidohydrolases. Amino acid sequence of a glutaminase-asparaginase from Acinetobacter glutaminasificans and preliminary crystallographic data for an asparaginase from Erwinia chrysanthemi.Tanaka S, Robinson EA, Appella E, Miller M, Ammon HL, Roberts J, Weber IT, Wlodawer A1988 Jun 253379033
Uncoupling intramolecular processing and substrate hydrolysis in the N-terminal nucleophile hydrolase hASRGL1 by circular permutation.Li W, Cantor JR, Yogesha SD, Yang S, Chantranupong L, Liu JQ, Agnello G, Georgiou G, Stone EM, Zhang Y2012 Nov 1622891768
The human asparaginase-like protein 1 hASRGL1 is an Ntn hydrolase with beta-aspartyl peptidase activity.Cantor JR, Stone EM, Chantranupong L, Georgiou G2009 Nov 2419839645
Crystal structure and allosteric regulation of the cytoplasmic Escherichia coli L-asparaginase I.Yun MK, Nourse A, White SW, Rock CO, Heath RJ2007 Jun 817451745
Gliap--a novel untypical L-asparaginase localized to rat brain astrocytes.Dieterich DC, Landwehr M, Reissner C, Smalla KH, Richter K, Wolf G, Böckers TM, Gundelfinger ED, Kreutz MR2003 Jun12753071
Reactions 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.Ortlund E, Lacount MW, Lewinski K, Lebioda L2000 Feb 1510684596