KEGG   ENZYME: 2.1.1.303
Entry
EC 2.1.1.303                Enzyme                                 
Name
2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase;
NcsB1;
neocarzinostatin O-methyltransferase
Class
Transferases;
Transferring one-carbon groups;
Methyltransferases
Sysname
S-adenosyl-L-methionine:2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase
Reaction(IUBMB)
S-adenosyl-L-methionine + 2,7-dihydroxy-5-methyl-1-naphthoate = S-adenosyl-L-homocysteine + 2-hydroxy-7-methoxy-5-methyl-1-naphthoate [RN:R10963]
Reaction(KEGG)
R10963
Substrate
S-adenosyl-L-methionine [CPD:C00019];
2,7-dihydroxy-5-methyl-1-naphthoate [CPD:C20857]
Product
S-adenosyl-L-homocysteine [CPD:C00021];
2-hydroxy-7-methoxy-5-methyl-1-naphthoate [CPD:C20841]
Comment
The enzyme from the bacterium Streptomyces carzinostaticus is involved in the biosynthesis of 2-hydroxy-7-methoxy-5-methyl-1-naphthoate. This compound is part of the enediyne chromophore of the antitumor antibiotic neocarzinostatin. In vivo the enzyme catalyses the regiospecific methylation at the 7-hydroxy group of its native substrate 2,7-dihydroxy-5-methyl-1-naphthoate. In vitro it also recognizes other dihydroxynaphthoic acids and catalyses their regiospecific O-methylation.
History
EC 2.1.1.303 created 2014
Pathway
ec01059  Biosynthesis of enediyne antibiotics
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K20421  2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase
Genes
CLIAC3E79_07185
NCYNOCYR_3137(dnrK)
NNONONO_c58190
NTPCRH09_14165 CRH09_23690 CRH09_25100 CRH09_33960
NODFOH10_15005 FOH10_16430
NAHF5544_21445
NIEKV110_22915
NHUH0264_26770
NSPUIFM12276_29470
RHUA3Q40_00430(rdmB)
DTMBJL86_2741
SMASAVERM_2382
SSXSACTE_5196 SACTE_6329
SHYSHJG_8512 SHJG_8515
SHOSHJGH_8272 SHJGH_8275
SSOII1A49_00935
SCWTU94_01395
SXISXIM_36010
SPRISPRI_3765
SLEsle_66100(sle_66100)
SPHWNFX46_33070
SLSSLINC_1337 SLINC_5831
SALUDC74_6556
SALLSAZ_34135
SAUOBV401_01185
SGVB1H19_02505
STIRDDW44_27895
SKACP970_39755
SGZC0216_12105
SGALCP966_11160
SRIMCP984_35640
SCINCP977_27955
STSUB7R87_22010
SCOECP976_32885
STUIGCM10017668_37980
SCHFIPT68_15470
SFEUIM697_24295
SROIIAG44_38680
SDDD9753_27325
STAALDH80_10680
SROCRGF97_06890
MIHBJP65_10025
SKESked_14480
CELZE5225_16810
NROK8W59_02610
KFLKfla_6058
KQIF1D05_14965
NALB005_2465(dnrK)
NEXNE857_03915
AMAZLUW76_34080
NOABKM31_13620 BKM31_42290
SENSACE_4650
SACGFDZ84_19175 FDZ84_28800 FDZ84_37280
AMDAMED_3230
AMNRAM_16420
AMMAMES_3195
AMZB737_3195
AOIAORI_6472
AJAAJAP_06605
AMYCCU254_34420
AMYBBKN51_25805
AABA4R43_20175
AMYYYIM_09465(dnrK1) YIM_15125(dnrK2)
AORISD37_05090 SD37_08075
APRTMUY14_19315
AROONQK81_33475
ARHDVSH64_37120
PDXPsed_0831
PSEEFRP1_29540 FRP1_30105
PECQAD017_32745 AD017_33050
PHHAFB00_04185 AFB00_16770
PBROHOP40_34045
APRECNX65_21955
AMIAmir_4382
SESPBN6_04400
SSYIEKG83_21075 EKG83_31050
KUTJJ691_03700
KPHYAOZ06_09075
LEDBBK82_29280
AHMTL08_06695
ACTIUA75_06455
ACADUA74_06455
AHGAHOG_06225(dnrK1)
PMADBAY61_07660 BAY61_19805
SACEGIY23_05190
CROSN8J89_23865 N8J89_31400
STPStrop_2214
SAQSare_4955
MAUMicau_3716
MILML5_4683
MICBMicB006_2815
MICHFJK98_09300
MCHLPVK74_09000
MFEUH1D33_24645
MPRNQ3V37_18365
AMSAMIS_34740
PRYPrubr_63830
DVCDvina_22655
NHYJQS43_20915
CCAZCOUCH_30655
KBSEPA93_15280
KBBccbrp13_13680
SUSAcid_5654
PFERIRI77_02260
 » show all
Reference
1  [PMID:18387946]
  Authors
Luo Y, Lin S, Zhang J, Cooke HA, Bruner SD, Shen B
  Title
Regiospecific O-methylation of naphthoic acids catalyzed by NcsB1, an O-methyltransferase involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin.
  Journal
J Biol Chem 283:14694-702 (2008)
DOI:10.1074/jbc.M802206200
  Sequence
Reference
2  [PMID:19702337]
  Authors
Cooke HA, Guenther EL, Luo Y, Shen B, Bruner SD
  Title
Molecular basis of substrate promiscuity for the SAM-dependent O-methyltransferase NcsB1, involved in the biosynthesis of the enediyne antitumor antibiotic neocarzinostatin.
  Journal
Biochemistry 48:9590-8 (2009)
DOI:10.1021/bi901257q
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.1.1.303
IUBMB Enzyme Nomenclature: 2.1.1.303
ExPASy - ENZYME nomenclature database: 2.1.1.303
BRENDA, the Enzyme Database: 2.1.1.303

DBGET integrated database retrieval system