KEGG   ENZYME: 3.5.1.38
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
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)
R00256 R00485;
(other) R01579 R06134
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
ec00470  D-Amino acid 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
PSG: G655_18480
PRP: M062_07255
PAEP: PA1S_19220
PAER: PA1R_gp4945
PAEM: U769_19065
PAEL: T223_19670
PAES: SCV20265_4073
PAEU: BN889_01444(ansB)
PAEG: AI22_15380
PAEC: M802_1374(ansB)
PAEO: M801_1376(ansB)
PPAA: B7D75_18480
PPU: PP_2453(ansB)
PPF: Pput_3237
PPG: PputGB1_3493
PPW: PputW619_1955
PPT: PPS_2020
PPB: PPUBIRD1_3225
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
PPJ: RK21_03012
PMOL: CLJ08_23235
PALD: LU682_018685
PIX: RIN61_21515
PMOS: O165_012770
PFL: PFL_2099(ansB)
PPRC: PFLCHA0_c21450(ansB)
PPRO: PPC_2112(ansB)
PFN: HZ99_07380
PFO: Pfl01_1917
PFS: PFLU_4161
PFC: PflA506_3470(ansB)
PPZ: H045_12070
PFB: VO64_1240
PMAN: OU5_5665(ansB)
PTV: AA957_24170
PVR: PverR02_21410
PAZO: AYR47_27360
POI: BOP93_16805
PRX: HRH33_18005
PKR: AYO71_12555
PMUD: NCTC8068_03428(ansB)
PTOL: I7845_19005
PFW: PF1751_v1c36680(ansB)
PFF: PFLUOLIPICF717940
PFX: A7318_17450
PEN: PSEEN1951(aspQ)
PBA: PSEBR_a2109 PSEBR_a744
PBC: CD58_10640
PPUU: PputUW4_03404(ansB)
PSV: PVLB_15760
PSK: U771_21775
PCH: EY04_09895
PCZ: PCL1606_39600
PCP: JM49_20000
PCHP: C4K32_2137
PFZ: AV641_14720
PLQ: AA042_01470
PALK: PSAKL28_19380
PSW: LK03_16270
PPV: NJ69_05435
PSEM: TO66_10680
PSEC: CCOS191_2092(ansB)
PPSY: AOC04_11755
PSOS: POS17_2054(ansB)
PFK: PFAS1_21525
PANR: A7J50_3841
PSIL: PMA3_09280
PYM: AK972_3826
PKE: DLD99_10450
PUM: HGP31_11100
PPSH: G5J76_18175
PGY: AWU82_02625
PATA: JWU58_17720
PDW: BV82_3721
PZE: HU754_019400
PMOE: HV782_010850
PSEP: C4K39_2145
PPII: QL104_11025
PTRT: HU722_0019275
PXA: KSS93_19540
PSAM: HU731_005840
PTZ: HU718_010935
PQI: KH389_17985
PSHH: HU773_018315
PXN: HU772_010615
PHV: HU739_007940
PPRG: HU725_013390
PASG: KSS96_19140
PFAK: KSS94_17280
PMUY: KSS95_13400
PMAM: KSS90_16255
PAZE: KSS91_09885
PORY: EJA05_18500
PTK: EXN22_17680
PIE: HU724_010745
PWY: HU734_010800
PTAE: NCTC10697_02838(ansB_2)
PGF: J0G10_11110
PCAV: D3880_09660
PJU: L1P09_10010
PIZ: LAB08_R18240
PPEG: KUA23_20155
PSII: NF676_10295
PSIH: LOY51_17885
PFIT: KJY40_11005
PASI: LG197_14960
PKM: PZ739_17715
PNB: NK667_16435
PTAI: ICN73_16370
PKK: QQ992_17205
PKJ: Q1W70_00615
PHOM: KJF94_06845
PCUC: PSH97_10100
PPAE: LDL65_01140
PSJY: AA098_11080
AVN: Avin_07280
AVL: AvCA_07280
AVD: AvCA6_07280
ACX: Achr_33940
ACB: A1S_1466
ABM: ABSDF2183(aspQ)
ABY: ABAYE2188(aspQ)
ABC: ACICU_01504
ABN: AB57_1697
ABB: ABBFA_01996(ansB)
ABX: ABK1_1959
ABZ: ABZJ_01665
ABR: ABTJ_02205
ABD: ABTW07_1665
ABH: M3Q_1853
ABAD: ABD1_14640(aspQ)
ABJ: BJAB07104_02254
ABAB: BJAB0715_01686
ABAJ: BJAB0868_01620
ABAZ: P795_9890
ABK: LX00_07445
ABAU: IX87_02900
ABAA: IX88_09280
ABW: BL01_02660
ABAL: ABLAC_22980
ACC: BDGL_000847(aspQ)
ANO: RR32_10605
ALC: OTEC02_10815
ACAL: BUM88_07695
ASEI: I8T81_11255
ACD: AOLE_11355
ACI: ACIAD2088(aspQ)
ATT: AMQ28_09070
AEI: AOY20_12600
AJO: RZ95_08805
ACW: A0J50_10115
ACV: AMD27_06455
AHL: AHTJS_08975
AJN: BVL33_11525
ASOL: BEN76_06565
ALA: BFG52_08885
ADV: DJ533_12280
ARJ: DOM24_13475
AWU: BEN71_12000
AGU: AS4_18910(aspQ)
AUG: URS_2403
ABER: BSR55_09015
ATN: FM020_08250
ALJ: G8D99_09425
ASHA: G8E00_06805
APOT: MZO21_07805
ATZ: M5E07_08305
ACIE: KIP84_10155
MBAH: HYN46_08425
HAA: A5892_07125
VFF: VITFI_CDS3260
CARI: FNU76_07130
RPJ: N234_11060
REH: H16_A1910(ansA)
CNC: CNE_1c18890(ansB2)
CUH: BJN34_10105
REU: Reut_A1812
RME: Rmet_1583(ansB)
CTI: RALTA_A1603(ansB1)
CBW: RR42_s1098
CGD: CR3_4545(aspQ)
CCUP: BKK81_10095
CUP: BKK80_10540
CUU: BKK79_02570
CPAU: EHF44_13380
COX: E0W60_19255 E0W60_32055
CCAM: M5D45_08370
CCAX: KZ686_19645
CUK: KB879_21845
CNAN: A2G96_12260
BMUL: NP80_1014(ansB)
BGD: bgla_1g07120
BGO: BM43_2101(ansB)
BGP: BGL_1c06540(ansB1)
BPLA: bpln_1g06460
BUM: AXG89_12855
BUI: AX768_06655
BXE: Bxe_B2492
BXB: DR64_4819
BPY: Bphyt_4228
PSPW: BJG93_31510
PCAF: DSC91_000094
PBRY: NDK50_28210
HYF: DTO96_101665(ansB_2)
PACR: FXN63_16035
RHY: RD110_23305
RHOA: HZ993_23170
POL: Bpro_4206
PNA: Pnap_0442
POS: DT070_09140
POO: F7R28_00275
AJS: Ajs_3863
ACK: C380_03010
ACRA: BSY15_2021(ansB)
ACIO: EAG14_18810
ARAD: KI609_03230
AAV: Aave_4182
AAA: Acav_4052
AMON: H9L24_18175
DAC: Daci_0564
DEL: DelCs14_0508
DTS: BI380_24470
DHK: BO996_00440
DLA: I6G47_24845
VAP: Vapar_4748
VPE: Varpa_5398
VPD: VAPA_1c49020(ansB)
VAA: AX767_13165
VBO: CKY39_29475
VAM: C4F17_22310
CTT: CtCNB1_0406
CTES: O987_02085
CSER: CCO03_11225
CAQT: KAQ61_18045
CODO: LAD35_18455
CTEZ: CT3_03740(ansB)
AANT: HUK68_17505
CRJ: QMY55_01980
OTO: ADJ79_11650
OTK: C6570_11915 C6570_15760
OTD: J1M35_06600
DIH: G7047_27185
DAER: H9K75_15760
DRG: H9K76_22610
DIA: Dtpsy_3136
MELM: C7H73_03415
PBH: AAW51_1003(aspQ)
MPT: Mpe_A1913
METP: C1M51_18050
ATER: MW290_07125
LCH: Lcho_2689
RGU: A4W93_04140
HSE: Hsero_1444(ansB)
HSZ: ACP92_07245
HHT: F506_08165
HEE: hmeg3_17630
HHF: E2K99_07295
HFR: G5S34_07620
AON: DEH84_13150
XYK: GT347_15600
XYG: R9X41_04770
ETB: N7L95_19465
ARES: IWH25_18190
APET: ToN1_12480(ansB)
DDEN: KI615_03910
DECH: GBK02_15345
QAU: KI612_08430
FLE: KI610_03125
AZO: azo0438(ansB2)
AOA: dqs_0449
AZA: AZKH_3046(ansB2)
AZI: AzCIB_3394
AZD: CDA09_06580
AZR: CJ010_02915
THK: CCZ27_16325
APP: CAP2UW1_1093
MRD: Mrad2831_3427
MET: M446_5042
MNO: Mnod_5349
MOR: MOC_3938
MAQU: Maq22A_c08785(ansB)
MPHY: MCBMB27_02915
MEE: DA075_09085
METX: A3862_14320
METI: DK427_14455
MMES: MMSR116_12420
MTEA: DK419_23660
MIND: mvi_32290(ansB)
MTAD: M6G65_31390
CMET: K6K41_27075
SECH: B18_18425
DTR: RSDT_0924(ansB)
PARH: I5S86_10635
 » show all
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)
DOI:10.1021/bi00200a005
  Sequence
[psv:PVLB_15760]
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
[psv:PVLB_15760]
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
LinkDB

DBGET integrated database retrieval system