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
ec00220  Arginine biosynthesis
ec00250  Alanine, aspartate and glutamate metabolism
ec00471  D-Glutamine and D-glutamate metabolism
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K05597  glutamin-(asparagin-)ase
Genes
PAE: PA1337(ansB)
PAEV: N297_1377(ansB)
PAEI: N296_1377(ansB)
PAU: PA14_46970(ansB)
PAP: PSPA7_4048(ansB)
PAG: PLES_38441(ansB)
PAF: PAM18_3565(ansB)
PNC: NCGM2_2225(ansB)
PAEB: NCGM1900_5234(ansB)
PDK: PADK2_18955
PAEP: PA1S_19220
PAEM: U769_19065
PAEL: T223_19670
PAEU: BN889_01444(ansB)
PAEG: AI22_15380
PAEC: M802_1374(ansB)
PAEO: M801_1376(ansB)
PPU: PP_2453(ansB)
PPF: Pput_3237
PPT: PPS_2020
PPI: YSA_00932
PPX: T1E_3434(ansA)
PPUH: B479_09975
PPUT: L483_21245
PPUN: PP4_19030(ansB)
PPUD: DW66_2273
PMON: X969_08385
PMOT: X970_08045
PFL: PFL_2099(ansB)
PPRC: PFLCHA0_c21450(ansB)
PPRO: PPC_2112(ansB)
PFS: PFLU_4161
PFC: PflA506_3470(ansB)
PFW: PF1751_v1c36680(ansB)
PFB: VO64_1240
PMAN: OU5_5665(ansB)
PEN: PSEEN1951(aspQ)
PPUU: PputUW4_03404(ansB)
PSEM: TO66_10680
PSEC: CCOS191_2092(ansB)
PSOS: POS17_2054(ansB)
PANR: A7J50_3841
PSIL: PMA3_09280
ACB: A1S_1466
ABM: ABSDF2183(aspQ)
ABY: ABAYE2188(aspQ)
ABN: AB57_1697
ABX: ABK1_1959
ABH: M3Q_1853
ABAD: ABD1_14640(aspQ)
ABAZ: P795_9890
ABAU: IX87_02900
ABAA: IX88_09280
ACC: BDGL_000847(aspQ)
ACI: ACIAD2088(aspQ)
REH: H16_A1910(ansA)
CNC: CNE_1c18890(ansB2)
RME: Rmet_1583(ansB)
CTI: RALTA_A1603(ansB1)
CGD: CR3_4545(aspQ)
BMUL: NP80_1014(ansB)
BGP: BGL_1c06540(ansB1)
BGO: BM43_2101(ansB)
BXE: Bxe_B2492
BXB: DR64_4819
POL: Bpro_4206
PNA: Pnap_0442
AAV: Aave_4182
AJS: Ajs_3863
AAA: Acav_4052
ACRA: BSY15_2021(ansB)
DAC: Daci_0564
VPD: VAPA_1c49020(ansB)
CTES: O987_02085
MPT: Mpe_A1913
HSE: Hsero_1444(ansB)
LCH: Lcho_2689
PBH: AAW51_1003(aspQ)
AZO: azo0438(ansB2)
AZA: AZKH_3046(ansB2)
AOA: dqs_0449
MET: M446_5042
MNO: Mnod_5349
MOR: MOC_3938
MAQU: Maq22A_c08785(ansB)
 » 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 247:84-90 (1972)
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 263:8583-91 (1988)
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 33:10257-65 (1994)
  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 39:1199-204 (2000)
DOI:10.1021/bi991797d
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 3.5.1.38
IUBMB Enzyme Nomenclature: 3.5.1.38
ExPASy - ENZYME nomenclature database: 3.5.1.38
BRENDA, the Enzyme Database: 3.5.1.38
CAS: 39335-03-0

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