Information on EC 2.5.1.43 - nicotianamine synthase

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The expected taxonomic range for this enzyme is: Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
2.5.1.43
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RECOMMENDED NAME
GeneOntology No.
nicotianamine synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3 S-adenosyl-L-methionine = 3 S-methyl-5'-thioadenosine + nicotianamine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alkenyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2'-deoxymugineic acid phytosiderophore biosynthesis
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L-nicotianamine biosynthesis
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methionine metabolism
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:S-adenosyl-L-methionine:S-adenosyl-Lmethionine 3-amino-3-carboxypropyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
161515-44-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene AtNAS4
TREMBL
Manually annotated by BRENDA team
var. xiaojinensis, gene MxNAS2
UniProt
Manually annotated by BRENDA team
strain CBS 195.57
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Manually annotated by BRENDA team
strain CBS 195.57
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + glutamate
2 S-methyl-5'-thioadenosine + thermoNicotianamine + 2 H+
show the reaction diagram
3 S-adenosyl-L-methionine
3 S-methyl-5'-thioadenosine + nicotianamine
show the reaction diagram
p-amidinophenyl methanesulfonyl fluoride
?
show the reaction diagram
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?
S-adenosyl-L-methionine
5'-S-methyl-5'-thioadenosine + nicotianamine
show the reaction diagram
S-adenosyl-L-methionine
?
show the reaction diagram
additional information
?
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the enzyme condenses three aminopropyl moieties of S-adenosylmethionine and the autocyclization of one moiety leads to the formation of an azetidine ring
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + glutamate
2 S-methyl-5'-thioadenosine + thermoNicotianamine + 2 H+
show the reaction diagram
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the archaeal product analogue thermoNicotianamine differs from nicotianamine in the carboxy azetidine moiety of nicotianamine that is replaced by a glutamate moiety in thermoNicotianamine, overview
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?
3 S-adenosyl-L-methionine
3 S-methyl-5'-thioadenosine + nicotianamine
show the reaction diagram
S-adenosyl-L-methionine
5'-S-methyl-5'-thioadenosine + nicotianamine
show the reaction diagram
S-adenosyl-L-methionine
?
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 10
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pH 7.5: about 20% of maximal activity, pH 10.0: about 50% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.18
sequence calculation
5.49
A0A096Q911, A0A096QLY8, A0A096S1K7, A0A096TT70, B4FAC0, K7VEJ7, K7VIY6, K7WE51, Q8S9C5
sequence calculation
5.68
A0A096Q911, A0A096QLY8, A0A096S1K7, A0A096TT70, B4FAC0, K7VEJ7, K7VIY6, K7WE51, Q8S9C5
sequence calculation
5.89
A0A096Q911, A0A096QLY8, A0A096S1K7, A0A096TT70, B4FAC0, K7VEJ7, K7VIY6, K7WE51, Q8S9C5
sequence calculation
5.99
A0A096Q911, A0A096QLY8, A0A096S1K7, A0A096TT70, B4FAC0, K7VEJ7, K7VIY6, K7WE51, Q8S9C5
sequence calculation; sequence calculation
6.08
A0A096Q911, A0A096QLY8, A0A096S1K7, A0A096TT70, B4FAC0, K7VEJ7, K7VIY6, K7WE51, Q8S9C5
sequence calculation; sequence calculation
6.09
A0A096Q911, A0A096QLY8, A0A096S1K7, A0A096TT70, B4FAC0, K7VEJ7, K7VIY6, K7WE51, Q8S9C5
sequence calculation
6.15
A0A096Q911, A0A096QLY8, A0A096S1K7, A0A096TT70, B4FAC0, K7VEJ7, K7VIY6, K7WE51, Q8S9C5
sequence calculation
6.22
A0A096Q911, A0A096QLY8, A0A096S1K7, A0A096TT70, B4FAC0, K7VEJ7, K7VIY6, K7WE51, Q8S9C5
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
A0A096Q911, A0A096QLY8, A0A096S1K7, A0A096TT70, B4FAC0, K7VIY6, K7WE51, Q8S9C5
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Manually annotated by BRENDA team
A0A096Q911, A0A096QLY8, A0A096S1K7, A0A096TT70, B4FAC0, K7VIY6, K7WE51, Q8S9C5
of roots; of roots
Manually annotated by BRENDA team
A0A096Q911, A0A096QLY8, A0A096S1K7, A0A096TT70, B4FAC0, K7VIY6, K7WE51, Q8S9C5
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Manually annotated by BRENDA team
low enzyme levels
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
isozyme MxNAS2 is preferentially localized in vesicles and cytoplasmic membrane
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
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gel filtration
40000 - 50000
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gel filtration
60000
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and 30000, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
at 20°C using the hanging drop vapor diffusion method
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diffraction to 1.7 A resolution, space group P212121
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purified NAS mutant E81Q complexed with both substrates, S-adenosyl-L-methionine and/or glutamate, or with reaction intermediate N-(3-amino-3-carboxypropyl)glutamic acid, X-ray diffraction structure determination and analysis
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
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overnight in 50 mM Tris, 1 mM EDTA, 3 mM dithiothreitol, pH 8.7 with HCl, 90% loss of activity
639734
5.5
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overnight in 50 mM Tris, 1 mM EDTA, 3 mM dithiothreitol, pH 8.7 with HCl, 80% loss of activity
639734
7
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activity is almost completely recovered after overnight exposure in 50 mM Tris, 1 mM EDTA, 3 mM dithiothreitol, pH 8.7 with HCl
639734
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
thiol proteases such as papain might digest nicotianamide synthase in crude extracts
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, in 50 mM Tris, 1 mM EDTA, 3 mM dithiothreitol, pH 8.7 with HCl, stable for about 1 week
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant, His-tagged protein
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
analysis of upstream region of nicotianamide synthase gene from Arabidopsis thaliana: presence of putative ERE-like sequence
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complementation of the Lycopersicon esculentum mutant chloronerva that is free of nicotinamine due to a defect in nicotinamide synthase
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expressed in Lolium perenne after particle bombardment transformation
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expressed in Nicotiana tabacum
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expressed in Nicotiana tabacum, expression is highly induced by Fe-deficiency in roots
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expressed in Nicotiana tabacum, expression is highly induced by Fe-deficiency in roots and in leaves
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expressed in Oryza sativa cv. Tsukinohikari under control of the pGluB-1 promoter after transformation with Agrobacterium tumefaciens
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expressed in Oryza sativa ssp. japonica cv. Taipei 309 under control of the 35S promoter from cauliflower mosaic virus after transformation by Agrobacterium tumefaciens
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expressed in Saccharomyces cerevisiae; expressed in Saccharomyces cerevisiae
expressed in Schizosaccharomyces pombe zhf cells
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expression in Escherichia coli
expression of a barley HvNAS1 nicotinamine synthase gene promoter-gus fusion gene in transgenic tobacco is induced by Fe-deficiency in root
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expression of nicotianamine synthase in Oryza sativa seeds under the control of the maize ubiquitin promoter
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gene AtNAS4, overexpression of AtNAS4 both in the Salk 135507 mutant and the wild-type genetic backgrounds
gene MxNAS2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time PCR expression analysis, recombinant expression in transgenic Nicotiana tabacum cv. Xanthi under control of the CaMV 35S promoter, recombinant isozyme MxNAS2 promotes the synthesis of NAS and increases nicotinamine and chlorophyll contents in the tobacco cells. Overexpression of MxNAS2 improves the tolerance to Fe stress in transgenic tobacco, but leads to delayed flowering. Higher levels of MxNAS2 expression in transgenic tobacco contribute to misshapen flowers and increased levels of Fe, Mn, Cu and Zn in leaf and flower. A MxNAS2-GFP fusion protein is targeted into vesicles and cytoplasmic membrane
gene OsNAS2, overexpresion in Oryza sativa plants
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gene OsNAS2, recombinant expression of GFP-tagged isozyme NAS2 in transgenic Oryza sativa plants under the control of its own promoter. The recombinant GFP-tagged enzyme moves moving dynamically within root cells, phhenotype, ooverview
gene ZmNAS10, promoter identification, genotyping and isozyme sequence comparisons, phylogenetic analysis, quantitative RT-PCR expression analysis; gene ZmNAS1, promoter identification, genotyping and isozyme sequence comparisons, phylogenetic analysis, quantitative RT-PCR expression analysis; gene ZmNAS2, promoter identification, genotyping and isozyme sequence comparisons, phylogenetic analysis, quantitative RT-PCR expression analysis; gene ZmNAS3, promoter identification, genotyping and isozyme sequence comparisons, phylogenetic analysis, quantitative RT-PCR expression analysis, recombinant expression of C-terminally GFP-tagged ZmNAS3 in the cytoplasm of transgenic Arabidopsis leaf protoplasts; gene ZmNAS4, promoter identification, genotyping and isozyme sequence comparisons, phylogenetic analysis, quantitative RT-PCR expression analysis; gene ZmNAS5, promoter identification, genotyping and isozyme sequence comparisons, phylogenetic analysis, quantitative RT-PCR expression analysis; gene ZmNAS6, promoter identification, genotyping and isozyme sequence comparisons, phylogenetic analysis, quantitative RT-PCR expression analysis; gene ZmNAS7, promoter identification, genotyping and isozyme sequence comparisons, phylogenetic analysis, quantitative RT-PCR expression analysis; gene ZmNAS8, promoter identification, genotyping and isozyme sequence comparisons, phylogenetic analysis, quantitative RT-PCR expression analysis; gene ZmNAS9, promoter identification, genotyping and isozyme sequence comparisons, phylogenetic analysis, quantitative RT-PCR expression analysis
A0A096Q911, A0A096QLY8, A0A096S1K7, A0A096TT70, B4FAC0, K7VEJ7, K7VIY6, K7WE51, Q8S9C5
gene ZmNAS1;1, located on chromosome 9, genotying and phylogenetic analysis, sequence comparisons, expression analysis; gene ZmNAS1;2, located on chromosome 9, genotying and phylogenetic analysis, sequence comparisons, expression analysis; gene ZmNAS2;1, located on chromosome 1, genotying and phylogenetic analysis, sequence comparisons, expression analysis; gene ZmNAS2;2, located on chromosome 1, genotying and phylogenetic analysis, sequence comparisons, expression analysis; gene ZmNAS3, located on chromosome 1, genotying and phylogenetic analysis, sequence comparisons, expression analysis; gene ZmNAS4, located on chromosome 5, genotying and phylogenetic analysis, sequence comparisons, expression analysis; gene ZmNAS5, located on chromosome 7, genotying and phylogenetic analysis, sequence comparisons, expression analysis; gene ZmNAS6;1, located on chromosome 9, genotying and phylogenetic analysis, sequence comparisons, expression analysis; gene ZmNAS6;2, located on chromosome 9, genotying and phylogenetic analysis, sequence comparisons, expression analysis
A0A096Q911, A0A096QLY8, A0A096S1K7, A0A096TT70, B4FAC0, K7VIY6, K7WE51, Q8S9C5
overexpressed as a C-terminal His tag protein in Escherichia coli BL21 (DE3)
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recombinant expression of GFP-tagged isozyme OsNAS2 in Oryza sativa roots. OsNAS2-sGFP vesicles move dynamically in the cells. Fe homeostasis is disturbed in the GFP-tagged OsNAS2 plants, and these plants receive Fe-deficiency signals even under Fe-sufficient conditions, this is probably due to to the overproduction of deocxymugineic acid and nicotinamine, which increases the chelating capacity of Fe and disrupts an unknown Fe-sensing mechanism
three cDNA clones osnas1, asnas2 and osnas3 from Fe-deficient rotts and a genomic fragment containing both OsNAS1 and OsNAS2
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three nicotianamine synthase genes: ZmNAS1, ZmNAS2 and ZmNAS3, fusion to the maltose-binding protein and production of the resulting fusion protein in Escherichia coli, ZmNAS1 and ZmNAS3 show nicotianamine synthase activity, ZmNAs2 does not
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transgenic Arabidopsis and tobacco plants constitutively overexpress the enzyme from Hordeum vulgare. Nicotianamine synthase overexpression results in increased biosynthesis of nicotianamine in transgenic plants, which conferrs enhanced tolerance of high levels of metals, particularly nickel, to plants. Promoter activities of four nicotianamine synthase genes in Arabidopsis are all increased in response to excess nickel, suggesting that nicotianamine plays an important role in the detoxification of nickel in plants. Transgenic tobacco plants with a high level of nicotianamine grew well in a nickel-enriched serpentine soil without developing any symptoms of nickel toxicity
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
all ZmNAS genes are responsive to heavy metal ions (Ni, Fe, Cu, Mn, Zn, and Cd). ZmNAS gene expression of maize seedlings is regulated by jasmonic acid, abscisic acid, and salicylic acid; all ZmNAS genes are responsive to heavy metal ions (Ni, Fe, Cu, Mn, Zn, and Cd). ZmNAS gene expression of maize seedlings is regulated by jasmonic acid, abscisic acid, and salicylic acid; all ZmNAS genes are responsive to heavy metal ions (Ni, Fe, Cu, Mn, Zn, and Cd). ZmNAS gene expression of maize seedlings is regulated by jasmonic acid, abscisic acid, and salicylic acid; all ZmNAS genes are responsive to heavy metal ions (Ni, Fe, Cu, Mn, Zn, and Cd). ZmNAS gene expression of maize seedlings is regulated by jasmonic acid, abscisic acid, and salicylic acid; ZmNAS gene expression of maize seedlings is regulated by jasmonic acid, abscisic acid, and salicylic acid; ZmNAS gene expression of maize seedlings is regulated by jasmonic acid, abscisic acid, and salicylic acid; ZmNAS gene expression of maize seedlings is regulated by jasmonic acid, abscisic acid, and salicylic acid; ZmNAS gene expression of maize seedlings is regulated by jasmonic acid, abscisic acid, and salicylic acid; ZmNAS gene expression of maize seedlings is regulated by jasmonic acid, abscisic acid, and salicylic acid; ZmNAS gene expression of maize seedlings is regulated by jasmonic acid, abscisic acid, and salicylic acid
class I ZmNAS genes are induced under Fe deficiency and are suppressed under Fe excessive conditions, while the expression pattern of class II genes are opposite to class I. Expression patterns of ZmNAS genes in response to fluctuating metal status. Class II genes are induced under excessive Zn and deficient Cu/Mn conditions; class I ZmNAS genes are induced under Fe deficiency and are suppressed under Fe excessive conditions, while the expression pattern of class II genes are opposite to class I. Expression patterns of ZmNAS genes in response to fluctuating metal status. Class II genes are induced under excessive Zn and deficient Cu/Mn conditions; class I ZmNAS genes are induced under Fe deficiency and are suppressed under Fe excessive conditions, while the expression pattern of class II genes are opposite to class I. Expression patterns of ZmNAS genes in response to fluctuating metal status. Class II genes are induced under excessive Zn and deficient Cu/Mn conditions; class I ZmNAS genes are induced under Fe deficiency and are suppressed under Fe excessive conditions, while the expression pattern of class II genes are opposite to class I. Expression patterns of ZmNAS genes in response to fluctuating metal status. Class I ZmNAS genes are stimulated under Zn deficiency; class I ZmNAS genes are induced under Fe deficiency and are suppressed under Fe excessive conditions, while the expression pattern of class II genes are opposite to class I. Expression patterns of ZmNAS genes in response to fluctuating metal status. Class I ZmNAS genes are stimulated under Zn deficiency; class I ZmNAS genes are induced under Fe deficiency and are suppressed under Fe excessive conditions, while the expression pattern of class II genes are opposite to class I. Expression patterns of ZmNAS genes in response to fluctuating metal status. Class I ZmNAS genes are stimulated under Zn deficiency; class I ZmNAS genes are induced under Fe deficiency and are suppressed under Fe excessive conditions, while the expression pattern of class II genes are opposite to class I. Expression patterns of ZmNAS genes in response to fluctuating metal status. Class I ZmNAS genes are stimulated under Zn deficiency; class I ZmNAS genes are induced under Fe deficiency and are suppressed under Fe excessive conditions, while the expression pattern of class II genes are opposite to class I. Expression patterns of ZmNAS genes in response to fluctuating metal status. Class I ZmNAS genes are stimulated under Zn deficiency; class I ZmNAS genes are induced under Fe deficiency and are suppressed under Fe excessive conditions, while the expression pattern of class II genes are opposite to class I. Expression patterns of ZmNAS genes in response to fluctuating metal status. Class I ZmNAS genes are stimulated under Zn deficiency
A0A096Q911, A0A096QLY8, A0A096S1K7, A0A096TT70, B4FAC0, K7VIY6, K7WE51, Q8S9C5
class I ZmNAS genes are induced under Fe deficiency and are suppressed under Fe excessive conditions, while the expression pattern of class II genes are opposite to class I. Expression patterns of ZmNAS genes in response to fluctuating metal status; class I ZmNAS genes are induced under Fe deficiency and are suppressed under Fe excessive conditions, while the expression pattern of class II genes are opposite to class I. Expression patterns of ZmNAS genes in response to fluctuating metal status; class I ZmNAS genes are induced under Fe deficiency and are suppressed under Fe excessive conditions, while the expression pattern of class II genes are opposite to class I. Expression patterns of ZmNAS genes in response to fluctuating metal status; class I ZmNAS genes are induced under Fe deficiency and are suppressed under Fe excessive conditions, while the expression pattern of class II genes are opposite to class I. Expression patterns of ZmNAS genes in response to fluctuating metal status. Class I genes are suppressed in response to Zn excess and Cu/Mn deficiency; class I ZmNAS genes are induced under Fe deficiency and are suppressed under Fe excessive conditions, while the expression pattern of class II genes are opposite to class I. Expression patterns of ZmNAS genes in response to fluctuating metal status. Class I genes are suppressed in response to Zn excess and Cu/Mn deficiency; class I ZmNAS genes are induced under Fe deficiency and are suppressed under Fe excessive conditions, while the expression pattern of class II genes are opposite to class I. Expression patterns of ZmNAS genes in response to fluctuating metal status. Class I genes are suppressed in response to Zn excess and Cu/Mn deficiency; class I ZmNAS genes are induced under Fe deficiency and are suppressed under Fe excessive conditions, while the expression pattern of class II genes are opposite to class I. Expression patterns of ZmNAS genes in response to fluctuating metal status. Class I genes are suppressed in response to Zn excess and Cu/Mn deficiency; class I ZmNAS genes are induced under Fe deficiency and are suppressed under Fe excessive conditions, while the expression pattern of class II genes are opposite to class I. Expression patterns of ZmNAS genes in response to fluctuating metal status. Class I genes are suppressed in response to Zn excess and Cu/Mn deficiency; class I ZmNAS genes are induced under Fe deficiency and are suppressed under Fe excessive conditions, while the expression pattern of class II genes are opposite to class I. Expression patterns of ZmNAS genes in response to fluctuating metal status. Class I genes are suppressed in response to Zn excess and Cu/Mn deficiency
A0A096Q911, A0A096QLY8, A0A096S1K7, A0A096TT70, B4FAC0, K7VIY6, K7WE51, Q8S9C5
in leaves and roots, NAS4 were up-regulated 2- to 3fold by Ni treatment; in leaves, NAS3 is up-regulated 3fold by Ni treatment; in roots, NAS1 is up-regulated twice by Ni treatment; iron deficiency markedly increases expression of NAS4 in leaves; iron deficiency slightly increases expression of NAS2 in roots
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iron deficiency significantly decreases expression of NAS3 in leaves
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OsNAS2 is iron deficiency-inducible, while Zn-, Cu-, and Mn-deficiencies have no effect on the gene expression
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the expression of MxNAS2 is highly affected by Fe stress and indoleacetic acid treatment, whereas, weakly affected by abscisic acid treatment in seedlings
ZmNAS10 is downregulated by Ni; ZmNAS1 gene is suppressed by heavy metal ions Ni, Fe, Cu, Mn, Zn, and Cd; ZmNAS2 gene is suppressed by heavy metal ions Ni, Fe, Cu, Mn, Zn, and Cd; ZmNAS3 gene is uppressed by heavy metal ions Ni, Fe, Cu, Mn, Zn, and Cd; ZmNAS5 is downregulated by Cd, Cu, Ni, and Mn; ZmNAS6 is downregulated by Ni; ZmNAS7 is downregulated by Cu and Ni; ZmNAS8 gene is responsive to heavy metal ions Ni, Fe, Cu, Mn, Zn, and Cd; ZmNAS9 is downregulated by Ni, Mn, Fe, and Zn
ZmNAS4 gene is induced by heavy metal ions Ni, Fe, Cu, Mn, Zn, and Cd; ZmNAS7 gene is induced by Fe
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E81Q/Y107F
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inactive mutant
L115A/L116A
isozyme OsNAS2 mutated in the LL motif resulting in mutant m7-sGFP, which does not localize to the vesicles. Mutant m7–sGFP does not show NAS enzyme activity
Y105A
isozyme OsNAS2 mutated in the YXXphi motif resulting in mutant m6-sGFP, which is localized to the vesicles. These vesicles stuck together and are immobile. Mutant m6-sGFP converts S-adenosyl methionine into nicotinamine in vitro
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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the nicotianamine synthase gene may be a suitable candidate for making a transgenic plant tolerant to Fe-deficiency