KEGG   ENZYME: 1.14.11.39
Entry
EC 1.14.11.39               Enzyme                                 

Name
L-asparagine hydroxylase;
L-asparagine 3-hydroxylase;
AsnO
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
Sysname
L-asparagine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Reaction(IUBMB)
L-asparagine + 2-oxoglutarate + O2 = (2S,3S)-3-hydroxyasparagine + succinate + CO2 [RN:R10446]
Reaction(KEGG)
R10446
Substrate
L-asparagine [CPD:C00152];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007]
Product
(2S,3S)-3-hydroxyasparagine [CPD:C20631];
succinate [CPD:C00042];
CO2 [CPD:C00011]
Comment
Requires Fe2+. The enzyme is only able to hydroxylate free L-asparagine. It is not active toward D-asparagine. The beta-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non-ribosomally synthesized acidic lipopeptide lactone.
History
EC 1.14.11.39 created 2013
Orthology
K18058  L-asparagine oxygenase
Genes
ENC: ECL_03968
ECLG: EC036_33910
SMAC: SMDB11_0605 SMDB11_1104
SRR: SerAS9_0274
SPLY: Q5A_006790(asnO)
SRS: SerAS12_0274
SRA: SerAS13_0273
SFG: AV650_20270
SERA: Ser39006_015050
SERQ: CWC46_15045
ETA: ETA_15700
HAEG: NCTC8502_01634(asnO)
VAQ: FIV01_12890(mppO)
VSR: Vspart_00116(asnO_1) Vspart_02171(asnO_2)
PPUT: L483_02555
PPUN: PP4_05200
PFB: VO64_2148
PSA: PST_3923
PSZ: PSTAB_3884(mppO)
PSOS: POS17_3974(PputW619_0540)
LLO: LLO_3359
NCI: NCTC10296_01180(asnO)
BCN: Bcen_5513
BCJ: BCAS0290
BCEO: I35_7306
BCED: DM42_6785
BSEM: WJ12_20955
BMEC: WJ16_18780
THI: THI_1730
RBE: RBE_0478
RBO: A1I_02770
KVU: EIO_3104
PABS: JIR001_15040(asnO_1)
CPL: Cp3995_0633(tauD)
CPP: CpP54B96_0633(tauD)
CPZ: CpPAT10_0623(tauD)
COR: Cp267_0650(tauD)
COD: Cp106_0606(tauD)
COS: Cp4202_0616(tauD)
CPSE: CPTA_01173
CPSU: CPTB_00359
CPSF: CPTC_01163
CUL: CULC22_00672(ogs)
CUC: CULC809_00665(ogs)
CUE: CULC0102_0775(ogs)
CUN: Cul210932_0700(tauD)
CUS: CulFRC11_0669(tauD)
CUQ: Cul210931_0669(tauD)
CUZ: Cul05146_0718(tauD)
CUJ: CUL131002_0678c(tauD)
NFA: NFA_48610
NFR: ERS450000_05049(asnO)
NSR: NS506_01690(asnO)
NAD: NCTC11293_06239(asnO_2)
GOM: D7316_02856(mppO)
SRT: Srot_0774
SCO: SCO2693(SCC61A.14) SCO3236(SCE29.05c)
SALB: XNR_0986
SGB: WQO_12245
SHY: SHJG_1397
SCT: SCAT_2689(asnO) SCAT_p1377
SALS: SLNWT_6835
STRP: F750_6418
SFI: SFUL_5831
SALU: DC74_5997
SALL: SAZ_31060
SLV: SLIV_21510(asnO1) SLIV_24200(asnO2)
STRE: GZL_01725
SPRI: SPRI_3466
SRW: TUE45_06291(mppO_1) TUE45_06409(asnO_5) TUE45_06920(mppO_2) TUE45_pSRc_0447(vioC)
SLAU: SLA_5783
SLX: SLAV_05480(mppO) SLAV_07260(asnO)
SFK: KY5_0486c
SGE: DWG14_08222(mppO)
SGZ: C0216_32755(vioC)
NCA: Noca_1042
SRO: Sros_3755
FAL: FRAAL4688
KRA: Krad_3958
AOI: AORI_3167
AMYY: YIM_25785(asnO3)
ALO: CRK62029
ASE: ACPL_2187(cs1)
ACTN: L083_4621
ACTS: ACWT_2065
PLK: CIK06_09170(vioC)
PSUU: Psuf_065540(asnO)
RXY: Rxyl_1155
CYB: CYB_1854
LET: O77CONTIG1_00553(cs2)
GES: VT84_06800(asnO)
CPI: Cpin_2834
FLN: FLA_1331
FJO: Fjoh_3169
CGLE: NCTC11432_00670(asnO)
 » show all
Reference
1  [PMID:17373765]
  Authors
Strieker M, Kopp F, Mahlert C, Essen LO, Marahiel MA
  Title
Mechanistic and structural basis of stereospecific Cbeta-hydroxylation in calcium-dependent antibiotic, a daptomycin-type lipopeptide.
  Journal
ACS Chem Biol 2:187-96 (2007)
DOI:10.1021/cb700012y
  Sequence
[sco:SCO3236]
Other DBs
ExplorEnz - The Enzyme Database: 1.14.11.39
IUBMB Enzyme Nomenclature: 1.14.11.39
ExPASy - ENZYME nomenclature database: 1.14.11.39
BRENDA, the Enzyme Database: 1.14.11.39

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