• Je něco špatně v tomto záznamu ?

Lincomycin biosynthesis involves a tyrosine hydroxylating heme protein of an unusual enzyme family

J. Novotna, J. Olsovska, P. Novak, P. Mojzes, R. Chaloupkova, Z. Kamenik, J. Spizek, E. Kutejova, M. Mareckova, P. Tichy, J. Damborsky, J. Janata,

. 2013 ; 8 (12) : e79974.

Jazyk angličtina Země Spojené státy americké

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc14074423

The gene lmbB2 of the lincomycin biosynthetic gene cluster of Streptomyces lincolnensis ATCC 25466 was shown to code for an unusual tyrosine hydroxylating enzyme involved in the biosynthetic pathway of this clinically important antibiotic. LmbB2 was expressed in Escherichia coli, purified near to homogeneity and shown to convert tyrosine to 3,4-dihydroxyphenylalanine (DOPA). In contrast to the well-known tyrosine hydroxylases (EC 1.14.16.2) and tyrosinases (EC 1.14.18.1), LmbB2 was identified as a heme protein. Mass spectrometry and Soret band-excited Raman spectroscopy of LmbB2 showed that LmbB2 contains heme b as prosthetic group. The CO-reduced differential absorption spectra of LmbB2 showed that the coordination of Fe was different from that of cytochrome P450 enzymes. LmbB2 exhibits sequence similarity to Orf13 of the anthramycin biosynthetic gene cluster, which has recently been classified as a heme peroxidase. Tyrosine hydroxylating activity of LmbB2 yielding DOPA in the presence of (6R)-5,6,7,8-tetrahydro-L-biopterin (BH4) was also observed. Reaction mechanism of this unique heme peroxidases family is discussed. Also, tyrosine hydroxylation was confirmed as the first step of the amino acid branch of the lincomycin biosynthesis.

Citace poskytuje Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc14074423
003      
CZ-PrNML
005      
20200814104443.0
007      
ta
008      
141006s2013 xxu f 000 0|eng||
009      
AR
024    7_
$a 10.1371/journal.pone.0079974 $2 doi
035    __
$a (PubMed)24324587
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a xxu
100    1_
$a Novotna, Jitka $u Institute of Microbiology, Academy of Sciences of the Czech Republic, Prague, Czech Republic ; Central-European Technology Institute, Brno, Czech Republic ; Crop Research Institute, Drnovska Prague, Czech Republic.
245    10
$a Lincomycin biosynthesis involves a tyrosine hydroxylating heme protein of an unusual enzyme family / $c J. Novotna, J. Olsovska, P. Novak, P. Mojzes, R. Chaloupkova, Z. Kamenik, J. Spizek, E. Kutejova, M. Mareckova, P. Tichy, J. Damborsky, J. Janata,
520    9_
$a The gene lmbB2 of the lincomycin biosynthetic gene cluster of Streptomyces lincolnensis ATCC 25466 was shown to code for an unusual tyrosine hydroxylating enzyme involved in the biosynthetic pathway of this clinically important antibiotic. LmbB2 was expressed in Escherichia coli, purified near to homogeneity and shown to convert tyrosine to 3,4-dihydroxyphenylalanine (DOPA). In contrast to the well-known tyrosine hydroxylases (EC 1.14.16.2) and tyrosinases (EC 1.14.18.1), LmbB2 was identified as a heme protein. Mass spectrometry and Soret band-excited Raman spectroscopy of LmbB2 showed that LmbB2 contains heme b as prosthetic group. The CO-reduced differential absorption spectra of LmbB2 showed that the coordination of Fe was different from that of cytochrome P450 enzymes. LmbB2 exhibits sequence similarity to Orf13 of the anthramycin biosynthetic gene cluster, which has recently been classified as a heme peroxidase. Tyrosine hydroxylating activity of LmbB2 yielding DOPA in the presence of (6R)-5,6,7,8-tetrahydro-L-biopterin (BH4) was also observed. Reaction mechanism of this unique heme peroxidases family is discussed. Also, tyrosine hydroxylation was confirmed as the first step of the amino acid branch of the lincomycin biosynthesis.
650    _2
$a antibakteriální látky $x biosyntéza $7 D000900
650    _2
$a bakteriální proteiny $x genetika $x metabolismus $7 D001426
650    _2
$a vysokoúčinná kapalinová chromatografie $7 D002851
650    _2
$a cirkulární dichroismus $7 D002942
650    _2
$a dihydroxyfenylalanin $x metabolismus $7 D004295
650    _2
$a Escherichia coli $x enzymologie $x genetika $7 D004926
650    _2
$a exprese genu $7 D015870
650    _2
$a hem $x chemie $x metabolismus $7 D006418
650    _2
$a hemoproteiny $x genetika $x metabolismus $7 D006420
650    _2
$a hydroxylace $7 D006900
650    _2
$a železo $x chemie $x metabolismus $7 D007501
650    _2
$a linkomycin $x biosyntéza $7 D008034
650    _2
$a multigenová rodina $7 D005810
650    _2
$a rekombinantní proteiny $x genetika $x metabolismus $7 D011994
650    _2
$a Streptomyces $x enzymologie $x genetika $7 D013302
650    _2
$a tyrosin $x metabolismus $7 D014443
650    _2
$a tyrosin-3-monooxygenasa $x genetika $x metabolismus $7 D014446
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Olsovska, Jana
700    1_
$a Novak, Petr
700    1_
$a Mojzes, Peter
700    1_
$a Chaloupkova, Radka
700    1_
$a Kamenik, Zdenek
700    1_
$a Spizek, Jaroslav
700    1_
$a Kutejova, Eva
700    1_
$a Ságová-Marečková, Markéta $7 xx0095954
700    1_
$a Tichy, Pavel
700    1_
$a Damborsky, Jiri
700    1_
$a Janata, Jiri
773    0_
$w MED00180950 $t PloS one $x 1932-6203 $g Roč. 8, č. 12 (2013), s. e79974
856    41
$u https://pubmed.ncbi.nlm.nih.gov/24324587 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y a $z 0
990    __
$a 20141006 $b ABA008
991    __
$a 20200814104441 $b ABA008
999    __
$a ok $b bmc $g 1042306 $s 873335
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2013 $b 8 $c 12 $d e79974 $i 1932-6203 $m PLoS One $n PLoS One $x MED00180950
LZP    __
$a Pubmed-20141006

Najít záznam

Citační ukazatele

Možnosti archivace