KEGG   ENZYME: 3.5.1.38Help
Entry
EC 3.5.1.38                 Enzyme                                 

Name
glutamin-(asparagin-)ase;
glutaminase-asparaginase;
ansB (gene name);
L-asparagine/L-glutamine amidohydrolase;
L-ASNase/L-GLNase
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
BRITE hierarchy
Sysname
L-glutamine(L-asparagine) amidohydrolase
Reaction(IUBMB)
(1) L-glutamine + H2O = L-glutamate + NH3 [RN:R00256];
(2) L-asparagine + H2O = L-aspartate + NH3 [RN:R00485]
Reaction(KEGG)
Substrate
L-glutamine [CPD:C00064];
H2O [CPD:C00001];
L-asparagine [CPD:C00152]
Product
L-glutamate [CPD:C00025];
NH3 [CPD:C00014];
L-aspartate [CPD:C00049]
Comment
The enzyme from the bacterium Achromobacter hydrolyses L-asparagine at 0.8 of the rate of L-glutamine; the D-isomers are also hydrolysed, but more slowly. cf. EC 3.5.1.2, glutaminase and EC 3.5.1.1, asparaginase.
History
EC 3.5.1.38 created 1976
Pathway
Alanine, aspartate and glutamate metabolism
Arginine and proline metabolism
D-Glutamine and D-glutamate metabolism
Metabolic pathways
Biosynthesis of secondary metabolites
Orthology
K05597  
glutamin-(asparagin-)ase
Genes
PAE: 
PA1337(ansB)
PAEV: 
N297_1377(ansB)
PAEI: 
N296_1377(ansB)
PAU: 
PAP: 
PAG: 
PAF: 
PNC: 
PDK: 
PSG: 
PRP: 
PAEP: 
PAER: 
PAEM: 
PAEL: 
PAES: 
PAEU: 
PAEG: 
PAEC: 
M802_1374(ansB)
PAEO: 
M801_1376(ansB)
PPU: 
PP_2453(ansA)
PPF: 
PPG: 
PPW: 
PPT: 
PPB: 
PPI: 
PPX: 
T1E_3434(ansA)
PPUH: 
PPUT: 
PPUN: 
PP4_19030(ansB)
PMOS: 
PPUU: 
PFL: 
PFL_2099(ansB)
PPRC: 
PFO: 
PFS: 
PFC: 
PPZ: 
PEN: 
PSEEN1951(aspQ)
PBA: 
PBC: 
PSV: 
PSK: 
PMON: 
PMOT: 
PCH: 
PALK: 
AVN: 
AVL: 
AVD: 
ACI: 
ACIAD2088(aspQ)
ACD: 
ACB: 
ABM: 
ABSDF2183(aspQ)
ABY: 
ABAYE2188(aspQ)
ABC: 
ABN: 
ABB: 
ABX: 
ABZ: 
ABR: 
ABD: 
ABH: 
ABAD: 
ABJ: 
ABAB: 
ABAJ: 
ABAZ: 
ACC: 
RPJ: 
REU: 
REH: 
H16_A1910(ansA)
CNC: 
RME: 
Rmet_1583(ansB)
CTI: 
BXE: 
BXB: 
BPY: 
BGD: 
POL: 
PNA: 
AAV: 
AJS: 
DIA: 
AAA: 
ACK: 
DAC: 
DEL: 
VAP: 
VPE: 
VPD: 
CTT: 
CTES: 
MPT: 
HSE: 
LCH: 
AZO: 
azo0438(ansB2)
AZA: 
AZKH_3046(ansB2)
APP: 
MRD: 
MET: 
MNO: 
MOR: 
 » show all
Taxonomy
Reference
1  [PMID:5017769]
  Authors
Roberts J, Holcenberg JS, Dolowy WC.
  Title
Isolation, crystallization, and properties of Achromobacteraceae glutaminase-asparaginase with antitumor activity.
  Journal
J. Biol. Chem. 247 (1972) 84-90.
Reference
2  [PMID:3379033]
  Authors
Tanaka S, Robinson EA, Appella E, Miller M, Ammon HL, Roberts J, Weber IT, Wlodawer A
  Title
Structures of amidohydrolases. Amino acid sequence of a glutaminase-asparaginase  from Acinetobacter glutaminasificans and preliminary crystallographic data for an asparaginase from Erwinia chrysanthemi.
  Journal
J. Biol. Chem. 263 (1988) 8583-91.
  Sequence
[up:P10172]
Reference
3  [PMID:8068664]
  Authors
Lubkowski J, Wlodawer A, Ammon HL, Copeland TD, Swain AL
  Title
Structural characterization of Pseudomonas 7A glutaminase-asparaginase.
  Journal
Biochemistry. 33 (1994) 10257-65.
  Sequence
Reference
4  [PMID:10684596]
  Authors
Ortlund E, Lacount MW, Lewinski K, Lebioda L
  Title
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.
  Journal
Biochemistry. 39 (2000) 1199-204.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
39335-03-0

DBGET integrated database retrieval system