Lactococcus lactis TrxD represents a subgroup of thioredoxins prevalent in Gram-positive bacteria containing WCXDC active site motifs
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
Lactococcus lactis TrxD represents a subgroup of thioredoxins prevalent in Gram-positive bacteria containing WCXDC active site motifs. / Björnberg, Olof; Efler, Petr; Ebong, Epie Denis; Svensson, Birte; Hägglund, Per.
In: Archives of Biochemistry and Biophysics, Vol. 564, 2014, p. 164-172.Research output: Contribution to journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Lactococcus lactis TrxD represents a subgroup of thioredoxins prevalent in Gram-positive bacteria containing WCXDC active site motifs
AU - Björnberg, Olof
AU - Efler, Petr
AU - Ebong, Epie Denis
AU - Svensson, Birte
AU - Hägglund, Per
PY - 2014
Y1 - 2014
N2 - Three protein disulfide reductases of the thioredoxin superfamily from the industrially important Gram-positive Lactococcus lactis (LlTrxA, LlTrxD and LlNrdH) are compared to the "classical" thioredoxin from Escherichia coli (EcTrx1). LlTrxA resembles EcTrx1 with a WCGPC active site motif and other key residues conserved. By contrast, LlTrxD is more distantly related and contains a WCGDC motif. Bioinformatics analysis suggests that LlTrxD represents a subgroup of thioredoxins from Gram-positive bacteria. LlNrdH is a glutaredoxin-like electron donor for ribonucleotide reductase class Ib. Based on protein-protein equilibria LlTrxA (E°′ = -259 mV) and LlNrdH (E°′ = -238 mV) show approximately 10 mV higher standard state redox potentials than the corresponding E. coli homologues, while E°′ of LlTrxD is -243 mV, more similar to glutaredoxin than "classical" thioredoxin. EcTrx1 and LlTrxA have high capacity to reduce insulin disulfides and their exposed active site thiol is alkylated at a similar rate at pH 7.0. LlTrxD on the other hand, is alkylated by iodoacetamide at almost 100 fold higher rate and shows no activity towards insulin disulfides. LlTrxA, LlTrxD and LlNrdH are all efficiently reduced by NADPH dependent thioredoxin reductase (TrxR) from L. lactis and good cross-reactivity towards E. coli TrxR was observed with LlTrxD as the notable exception.
AB - Three protein disulfide reductases of the thioredoxin superfamily from the industrially important Gram-positive Lactococcus lactis (LlTrxA, LlTrxD and LlNrdH) are compared to the "classical" thioredoxin from Escherichia coli (EcTrx1). LlTrxA resembles EcTrx1 with a WCGPC active site motif and other key residues conserved. By contrast, LlTrxD is more distantly related and contains a WCGDC motif. Bioinformatics analysis suggests that LlTrxD represents a subgroup of thioredoxins from Gram-positive bacteria. LlNrdH is a glutaredoxin-like electron donor for ribonucleotide reductase class Ib. Based on protein-protein equilibria LlTrxA (E°′ = -259 mV) and LlNrdH (E°′ = -238 mV) show approximately 10 mV higher standard state redox potentials than the corresponding E. coli homologues, while E°′ of LlTrxD is -243 mV, more similar to glutaredoxin than "classical" thioredoxin. EcTrx1 and LlTrxA have high capacity to reduce insulin disulfides and their exposed active site thiol is alkylated at a similar rate at pH 7.0. LlTrxD on the other hand, is alkylated by iodoacetamide at almost 100 fold higher rate and shows no activity towards insulin disulfides. LlTrxA, LlTrxD and LlNrdH are all efficiently reduced by NADPH dependent thioredoxin reductase (TrxR) from L. lactis and good cross-reactivity towards E. coli TrxR was observed with LlTrxD as the notable exception.
KW - Disulfide reduction
KW - Lactic acid bacteria
KW - Redox potential
KW - Thiol-disulfide exchange
KW - Thioredoxin
U2 - 10.1016/j.abb.2014.09.010
DO - 10.1016/j.abb.2014.09.010
M3 - Journal article
C2 - 25255970
AN - SCOPUS:84908315260
VL - 564
SP - 164
EP - 172
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
ER -
ID: 240158208