BRENDA - Enzyme Database
show all sequences of 2.8.1.7

Bacterial cysteine desulfurases: their function and mechanisms

Mihara, H.; Esaki, N.; Appl. Microbiol. Biotechnol. 60, 12-23 (2002)

Data extracted from this reference:

Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrial matrix
-
Homo sapiens
5759
-
mitochondrial matrix
-
Mus musculus
5759
-
mitochondrial matrix
-
Saccharomyces cerevisiae
5759
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-cysteine + [enzyme]-cysteine
Escherichia coli
-
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
?
L-cysteine + [enzyme]-cysteine
Azotobacter vinelandii
-
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
?
L-cysteine + [enzyme]-cysteine
Synechocystis sp.
-
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
?
L-cysteine + [enzyme]-cysteine
Synechocystis sp. PCC6714
-
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
?
additional information
Saccharomyces cerevisiae
-
?
-
-
-
additional information
Azotobacter vinelandii
enzyme catalyzes the formation of Fe-S clusters in a component protein of nitrogenase in the presence of cysteine and ferrous iron in vitro
?
-
-
-
additional information
Haemophilus influenzae
isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
?
-
-
-
additional information
Escherichia coli
isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
?
-
-
-
additional information
Pseudomonas aeruginosa
isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
?
-
-
-
additional information
Escherichia coli
enzyme is involved in selenoprotein biosynthesis
?
-
-
-
additional information
Azotobacter vinelandii
enzyme is involved in selenoprotein biosynthesis
?
-
-
-
additional information
Escherichia coli
involved in thiamine biosynthesis, molybdopterin biosynthesis and tRNA modification
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Azotobacter vinelandii
-
-
-
Escherichia coli
-
-
-
Haemophilus influenzae
-
-
-
Homo sapiens
-
-
-
Mus musculus
-
-
-
Pseudomonas aeruginosa
-
-
-
Saccharomyces cerevisiae
-
-
-
Synechocystis sp.
-
PCC6714
-
Synechocystis sp. PCC6714
-
PCC6714
-
Reaction
Reaction
Commentary
Organism
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
mechanism
Escherichia coli
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
mechanism
Azotobacter vinelandii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-cysteine
unlike other cysteine desulfurases the L-cysteine C-S-lyase from Synechocystis does not have a conserved cysteine residue at the active site
645615
Synechocystis sp.
pyruvate + sulfide
-
645615
Synechocystis sp.
?
L-cysteine
unlike other cysteine desulfurases the L-cysteine C-S-lyase from Synechocystis does not have a conserved cysteine residue at the active site
645615
Synechocystis sp. PCC6714
pyruvate + sulfide
-
645615
Synechocystis sp. PCC6714
?
L-cysteine + [enzyme]-cysteine
-
645615
Escherichia coli
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
-
645615
Azotobacter vinelandii
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
-
645615
Synechocystis sp.
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
catalyzes the conversion of cysteine to alanine and sulfane sulfur via the formation of a protein-bound cysteine persulfide intermediate on a conserved cysteine residue
645615
Azotobacter vinelandii
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
iscS has cysteine desulfurase activity and mobilizes sulfur from cysteine for the repair of the [4Fe-4S] cluster in apo-dihydroxyacid dehydratase
645615
Escherichia coli
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
-
645615
Synechocystis sp. PCC6714
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-selenocysteine
-
645615
Escherichia coli
L-alanine + selenium
-
-
-
?
L-selenocysteine
-
645615
Azotobacter vinelandii
L-alanine + selenium
-
-
-
?
L-selenocysteine
-
645615
Synechocystis sp.
L-alanine + selenium
-
-
-
?
L-selenocysteine
-
645615
Synechocystis sp. PCC6714
L-alanine + selenium
-
-
-
?
additional information
-
645615
Saccharomyces cerevisiae
?
-
-
-
-
additional information
enzyme catalyzes the formation of Fe-S clusters in a component protein of nitrogenase in the presence of cysteine and ferrous iron in vitro
645615
Azotobacter vinelandii
?
-
-
-
-
additional information
isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
645615
Haemophilus influenzae
?
-
-
-
-
additional information
isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
645615
Escherichia coli
?
-
-
-
-
additional information
isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
645615
Pseudomonas aeruginosa
?
-
-
-
-
additional information
enzyme is involved in selenoprotein biosynthesis
645615
Escherichia coli
?
-
-
-
-
additional information
enzyme is involved in selenoprotein biosynthesis
645615
Azotobacter vinelandii
?
-
-
-
-
additional information
involved in thiamine biosynthesis, molybdopterin biosynthesis and tRNA modification
645615
Escherichia coli
?
-
-
-
-
Cofactor
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
-
Azotobacter vinelandii
pyridoxal 5'-phosphate
-
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
pyridoxal 5'-phosphate
-
Azotobacter vinelandii
pyridoxal 5'-phosphate
-
Escherichia coli
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrial matrix
-
Homo sapiens
5759
-
mitochondrial matrix
-
Mus musculus
5759
-
mitochondrial matrix
-
Saccharomyces cerevisiae
5759
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-cysteine + [enzyme]-cysteine
Escherichia coli
-
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
?
L-cysteine + [enzyme]-cysteine
Azotobacter vinelandii
-
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
?
L-cysteine + [enzyme]-cysteine
Synechocystis sp.
-
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
?
L-cysteine + [enzyme]-cysteine
Synechocystis sp. PCC6714
-
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
?
additional information
Saccharomyces cerevisiae
-
?
-
-
-
additional information
Azotobacter vinelandii
enzyme catalyzes the formation of Fe-S clusters in a component protein of nitrogenase in the presence of cysteine and ferrous iron in vitro
?
-
-
-
additional information
Haemophilus influenzae
isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
?
-
-
-
additional information
Escherichia coli
isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
?
-
-
-
additional information
Pseudomonas aeruginosa
isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
?
-
-
-
additional information
Escherichia coli
enzyme is involved in selenoprotein biosynthesis
?
-
-
-
additional information
Azotobacter vinelandii
enzyme is involved in selenoprotein biosynthesis
?
-
-
-
additional information
Escherichia coli
involved in thiamine biosynthesis, molybdopterin biosynthesis and tRNA modification
?
-
-
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-cysteine
unlike other cysteine desulfurases the L-cysteine C-S-lyase from Synechocystis does not have a conserved cysteine residue at the active site
645615
Synechocystis sp.
pyruvate + sulfide
-
645615
Synechocystis sp.
?
L-cysteine
unlike other cysteine desulfurases the L-cysteine C-S-lyase from Synechocystis does not have a conserved cysteine residue at the active site
645615
Synechocystis sp. PCC6714
pyruvate + sulfide
-
645615
Synechocystis sp. PCC6714
?
L-cysteine + [enzyme]-cysteine
-
645615
Escherichia coli
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
-
645615
Azotobacter vinelandii
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
-
645615
Synechocystis sp.
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
catalyzes the conversion of cysteine to alanine and sulfane sulfur via the formation of a protein-bound cysteine persulfide intermediate on a conserved cysteine residue
645615
Azotobacter vinelandii
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
iscS has cysteine desulfurase activity and mobilizes sulfur from cysteine for the repair of the [4Fe-4S] cluster in apo-dihydroxyacid dehydratase
645615
Escherichia coli
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
-
645615
Synechocystis sp. PCC6714
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-selenocysteine
-
645615
Escherichia coli
L-alanine + selenium
-
-
-
?
L-selenocysteine
-
645615
Azotobacter vinelandii
L-alanine + selenium
-
-
-
?
L-selenocysteine
-
645615
Synechocystis sp.
L-alanine + selenium
-
-
-
?
L-selenocysteine
-
645615
Synechocystis sp. PCC6714
L-alanine + selenium
-
-
-
?
additional information
-
645615
Saccharomyces cerevisiae
?
-
-
-
-
additional information
enzyme catalyzes the formation of Fe-S clusters in a component protein of nitrogenase in the presence of cysteine and ferrous iron in vitro
645615
Azotobacter vinelandii
?
-
-
-
-
additional information
isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
645615
Haemophilus influenzae
?
-
-
-
-
additional information
isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
645615
Escherichia coli
?
-
-
-
-
additional information
isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
645615
Pseudomonas aeruginosa
?
-
-
-
-
additional information
enzyme is involved in selenoprotein biosynthesis
645615
Escherichia coli
?
-
-
-
-
additional information
enzyme is involved in selenoprotein biosynthesis
645615
Azotobacter vinelandii
?
-
-
-
-
additional information
involved in thiamine biosynthesis, molybdopterin biosynthesis and tRNA modification
645615
Escherichia coli
?
-
-
-
-
Other publictions for EC 2.8.1.7
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
739090
Grosshennig
Hydrogen sulfide is a novel po ...
Mycoplasma pneumoniae
Mol. Microbiol.
100
42-54
2016
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739453
Blauenburg
Crystal structure of Bacillus ...
Bacillus subtilis
PLoS ONE
11
e0158749
2016
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1
1
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737712
Dai
SufE D74R substitution alters ...
Escherichia coli
Biochemistry
54
4824-4833
2015
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739655
Liu
A novel cysteine desulfurase i ...
Lentinula edodes
Sci. Rep.
5
10047
2015
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1
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4
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1
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1
1
728340
Hidese
Cysteine desulphurase plays an ...
Thermococcus kodakarensis
Mol. Microbiol.
93
331-345
2014
-
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1
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5
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3
3
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737375
Roret
X-ray structures of Nfs2, the ...
Arabidopsis thaliana
Acta Crystallogr. Sect. F
70
1180-1185
2014
1
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1
1
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1
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737643
Rybniker
The cysteine desulfurase IscS ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis Rv3025c
Biochem. J.
459
467-478
2014
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2
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738144
Kovarova
Mitochondrial and nucleolar lo ...
Trypanosoma brucei
Eukaryot. Cell
13
353-362
2014
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739016
Bhubhanil
Cysteine desulphurase-encoding ...
Agrobacterium tumefaciens
Microbiology
160
79-90
2014
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2
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724811
Yamanaka
Crystal structure and function ...
Archaeoglobus fulgidus
Dalton Trans.
42
3092-3099
2013
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725215
Kim
[2Fe-2S]-Ferredoxin binds dire ...
Escherichia coli
J. Am. Chem. Soc.
135
8117-8120
2013
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726333
Marelja
The L-cysteine desulfurase NFS ...
Homo sapiens
PLoS ONE
8
e60869
2013
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1
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5
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5
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737594
Terali
The effect of the adaptor prot ...
Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
440
235-240
2013
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Modifications of the lipoamide ...
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Mechanism of cysteine desulfur ...
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Yeast Nfs1p is involved in thi ...
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Substitutions in an active sit ...
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Crystal structure of IscS, a c ...
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Formation of iron-sulfur clust ...
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645620
Kambampati
MnmA and IscS are required for ...
Escherichia coli
Biochemistry
42
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645634
Outten
The SufE protein and the SufBC ...
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645638
Kurihara
Assembly of iron-sulfur cluste ...
Escherichia coli
Biochim. Biophys. Acta
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645639
LaGier
Mitochondrial-type iron-sulfur ...
Cryptosporidium parvum
Microbiology
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2003
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1
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1
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645615
Mihara
Bacterial cysteine desulfurase ...
Azotobacter vinelandii, Escherichia coli, Haemophilus influenzae, Homo sapiens, Mus musculus, Pseudomonas aeruginosa, Saccharomyces cerevisiae, Synechocystis sp., Synechocystis sp. PCC6714
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Lima
Analysis of the E. coli NifS C ...
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1
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645618
Leon
The AtNFS2 gene from Arabidops ...
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Lauhon
Requirement for IscS in biosyn ...
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Mihara
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Nilsson
The cysteine desulfurase IscS ...
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645635
Yang
Repair of nitric oxide-modifie ...
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Kiyasu
Contribution of cysteine desul ...
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Kato
Gene cloning, purification, an ...
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8
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Mihara
Kinetic and mutational studies ...
Escherichia coli
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559-567
2000
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4
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645637
Schwartz
The cysteine desulfurase, IscS ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
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9009-9014
2000
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645622
Kispal
The mitochondrial proteins Atm ...
Saccharomyces cerevisiae
EMBO J.
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3981-3989
1999
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645624
Lacourciere
The NIFS protein can function ...
Azotobacter vinelandii
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30921-30926
1998
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645625
Land
Targeting of a human iron-sulf ...
Homo sapiens
Mol. Cell
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807-815
1998
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6
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645640
Kirby
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A cysteine desulphurase gene f ...
Ruminococcus flavefaciens
Biochim. Biophys. Acta
1368
233-237
1998
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645636
Zheng
Mechanism for the desulfurizat ...
Azotobacter vinelandii
Biochemistry
33
4714-4720
1994
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645631
Zheng
Cysteine desulfurase activity ...
Azotobacter vinelandii
Proc. Natl. Acad. Sci. USA
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2754-2758
1993
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