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IUBMB Comments The enzyme participates in an L -arginine biosynthesis pathway in certain species of archaea and bacteria. In some organisms the enzyme is bifunctional and also catalyses the activity of EC 1.2.1.103 , [amino-group carrier protein]-6-phospho-L -2-aminoadipate reductase.
Reaction Schemes
an [amino-group carrier protein]-C-terminal-gamma-(L-glutamate 5-semialdehyde-2-yl)-L-glutamate
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+
=
an [amino-group carrier protein]-C-terminal-gamma-(5-phospho-L-glutamyl)-L-glutamate
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Synonyms lysY , Saci_0750, TK0277 , [LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase,
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[LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase
lysY
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Saci_0750
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TK0277
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[LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase
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[LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase
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[LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase
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[LysW]-L-2-aminoadipate/[LysW]-L-glutamate phosphate reductase
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an [amino-group carrier protein]-C-terminal-gamma-(L-glutamate 5-semialdehyde-2-yl)-L-glutamate + phosphate + NADP+ = an [amino-group carrier protein]-C-terminal-gamma-(5-phospho-L-glutamyl)-L-glutamate + NADPH + H+
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MetaCyc
L-arginine biosynthesis IV (archaea)
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[amino-group carrier protein]-C-terminal-gamma-(L-glutamate 5-semialdehyde-2-yl)-L-glutamate:NADP+ 5-oxidoreductase (phosphorylating)
The enzyme participates in an L-arginine biosynthesis pathway in certain species of archaea and bacteria. In some organisms the enzyme is bifunctional and also catalyses the activity of EC 1.2.1.103, [amino-group carrier protein]-6-phospho-L-2-aminoadipate reductase.
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[amino-group carrier protein LysW]-C-terminal-gamma-(alpha-aminoadipate) phosphate + NADPH + H+
[amino-group carrier protein LysW]-C-terminal-gamma-aminoadipic semialdehyde + phosphate + NADP+
[amino-group carrier protein LysW]-C-terminal-gamma-aminoadipic semialdehyde + phosphate + NADP+
[amino-group carrier protein LysW]-C-terminal-gamma-(alpha-aminoadipate) phosphate + NADPH + H+
Substrates: -
r
[amino-group carrier protein LysW]-C-terminal-gamma-(alpha-aminoadipate) phosphate + NADPH + H+
[amino-group carrier protein LysW]-C-terminal-gamma-aminoadipic semialdehyde + phosphate + NADP+
Substrates: -
r
[amino-group carrier protein LysW]-C-terminal-gamma-(alpha-aminoadipate) phosphate + NADPH + H+
[amino-group carrier protein LysW]-C-terminal-gamma-aminoadipic semialdehyde + phosphate + NADP+
Substrates: -
r
[amino-group carrier protein LysW]-C-terminal-gamma-(alpha-aminoadipate) phosphate + NADPH + H+
[amino-group carrier protein LysW]-C-terminal-gamma-aminoadipic semialdehyde + phosphate + NADP+
Substrates: -
r
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[amino-group carrier protein LysW]-C-terminal-gamma-(alpha-aminoadipate) phosphate + NADPH + H+
[amino-group carrier protein LysW]-C-terminal-gamma-aminoadipic semialdehyde + phosphate + NADP+
Substrates: -
r
[amino-group carrier protein LysW]-C-terminal-gamma-aminoadipic semialdehyde + phosphate + NADP+
[amino-group carrier protein LysW]-C-terminal-gamma-(alpha-aminoadipate) phosphate + NADPH + H+
Substrates: -
r
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additional information
no cofactor: NADH
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12
phosphate
pH 9.5, 60°C
0.0098
[amino-group carrier protein LysW]-C-terminal-gamma-aminoadipic semialdehyde
pH 9.5, 60°C
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1.1
phosphate
pH 9.5, 60°C
0.96
[amino-group carrier protein LysW]-C-terminal-gamma-aminoadipic semialdehyde
pH 9.5, 60°C
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0.0089
phosphate
pH 9.5, 60°C
98
[amino-group carrier protein LysW]-C-terminal-gamma-aminoadipic semialdehyde
pH 9.5, 60°C
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10.1
NADPH oxidation, pH 8, 60°C
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UniProt
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UniProt
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UniProt
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UniProt
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cf. EC 1.2.1.103
UniProt
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Highest Expressing Human Cell Lines
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metabolism
for lysine biosynthesis, amino group-carrier protein LysW-gamma-aminoadipic acid is phosphorylated by LysZ to form LysW-gamma-aminoadipic acid phosphate, which is subsequently reduced to LysW-gamma-aminoadipic semialdehyde through a reaction catalyzed by LysY
physiological function
in Sulfolobus acidocaldarius, after LysW modification, alpha-aminoadipate and glutamate are converted to lysine and ornithine, respectively, by a single set of enzymes with dual functions. LyxY cataxadlyzes the phosphorylation of LysW-modified alpha-aminoadipate (cf. EC 1.2.1.103) and glutamate
physiological function
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in Sulfolobus acidocaldarius, after LysW modification, alpha-aminoadipate and glutamate are converted to lysine and ornithine, respectively, by a single set of enzymes with dual functions. LyxY cataxadlyzes the phosphorylation of LysW-modified alpha-aminoadipate (cf. EC 1.2.1.103) and glutamate
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structures of LysY complexed with amino group-carrier protein LysW-gamma-aminoadipic semialdehyde and LysW-gamma-alpha-aminoadipate, respectively. In both structures, the globular domain of LysW is recognized by positively charged residues on helix 9 and the beta11-alpha10 loop of LysY through conformational changes
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expression in Escherichia coli
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Yoshida, A.; Tomita, T.; Atomi, H.; Kuzuyama, T.; Nishiyama, M.
Lysine biosynthesis of Thermococcus kodakarensis with the capacity to function as an ornithine biosynthetic system
J. Biol. Chem.
291
21630-21643
2016
Thermococcus kodakarensis (Q5JFW1), Thermococcus kodakarensis ATCC BAA-918 (Q5JFW1)
brenda
Ouchi, T.; Tomita, T.; Horie, A.; Yoshida, A.; Takahashi, K.; Nishida, H.; Lassak, K.; Taka, H.; Mineki, R.; Fujimura, T.; Kosono, S.; Nishiyama, C.; Masui, R.; Kuramitsu, S.; Albers, S.V.; Kuzuyama, T.; Nishiyama, M.
Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus
Nat. Chem. Biol.
9
277-283
2013
Sulfolobus acidocaldarius (Q4JAQ3), Sulfolobus acidocaldarius DSM 639 (Q4JAQ3)
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Shimizu, T.; Tomita, T.; Kuzuyama, T.; Nishiyama, M.
Crystal structure of the LysY.LysW complex from Thermus thermophilus
J. Biol. Chem.
291
9948-9959
2016
Thermus thermophilus (O50146)
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