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.
Pathway
Alanine, aspartate and glutamate metabolism
Arginine and proline metabolism
D-Glutamine and D-glutamate metabolism
Nitrogen metabolism
Metabolic pathways
Biosynthesis of secondary metabolites
Microbial metabolism in diverse environments
Orthology
K05597  
glutamin-(asparagin-)ase
Genes
PAE: 
PA1337(ansB)
PAU: 
PAP: 
PAG: 
PAF: 
PNC: 
PDK: 
PSG: 
PPU: 
PP_2453(ansA)
PPF: 
PPG: 
PputGB1_3493
PPW: 
PputW619_1955
PPT: 
PPS_2020
PPB: 
PPUBIRD1_3225
PPI: 
YSA_00932
PPX: 
T1E_3434(ansA)
PPUH: 
B479_09975
PPUU: 
PputUW4_03404(ansB)
PFL: 
PFL_2099(ansB)
PFO: 
Pfl01_1917
PFS: 
PFLU4161
PFC: 
PflA506_3470(ansB)
PPZ: 
H045_12070
PEN: 
PSEEN1951(aspQ)
PBA: 
PSEBR_a2109 PSEBR_a744
AVN: 
Avin_07280
AVL: 
AvCA_07280
AVD: 
AvCA6_07280
ACI: 
ACIAD2088(aspQ)
ACD: 
AOLE_11355
ACB: 
A1S_1466
ABM: 
ABSDF2183(aspQ)
ABY: 
ABAYE2188(aspQ)
ABC: 
ACICU_01504
ABN: 
AB57_1697
ABB: 
ABBFA_002021
ABX: 
ABK1_1959
ABZ: 
ABZJ_01665
ABR: 
ABTJ_02205
ABD: 
ABTW07_1665
ABH: 
M3Q_1853
ABAD: 
ABD1_14640(aspQ)
ACC: 
BDGL_000847(aspQ)
REU: 
Reut_A1812
REH: 
H16_A1910(ansA)
RME: 
Rmet_1583(ansB)
CTI: 
RALTA_A1603(ansB1)
CNC: 
CNE_1c18890(ansB2)
BXE: 
Bxe_B2492
BPY: 
Bphyt_4228
BGD: 
bgla_1g07120
POL: 
Bpro_4206
PNA: 
Pnap_0442
AAV: 
Aave_4182
AJS: 
Ajs_3863
DIA: 
Dtpsy_3136
AAA: 
Acav_4052
ACK: 
C380_03010
DAC: 
Daci_0564
DEL: 
DelCs14_0508
VAP: 
Vapar_4748
VPE: 
Varpa_5398
CTT: 
CtCNB1_0406
MPT: 
Mpe_A1913
HSE: 
Hsero_1444(ansB)
LCH: 
Lcho_2689
AZO: 
azo0438(ansB2)
AZA: 
AZKH_3046(ansB2)
APP: 
CAP2UW1_1093
MRD: 
Mrad2831_3427
MET: 
M446_5042
MNO: 
Mnod_5349
 » 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.
  Organism
Achromobacferaceae sp.
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.
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.
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.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
39335-03-0
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