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IUBMB Comments The enzyme, found in some actinobacterial species, is a non-ribosomal peptide synthase (NRPS). Adenylation and thiolation domains of the enzyme activate a lysine residue and load it on the enzyme (this activity is described separately as EC 6.2.1.77 , L -lysine—[L -lysyl-carrier protein] ligase). A condensation domain catalyses the condensation of two isonitrile-containing moieties to both amino groups of the lysine, a rare activity in non-ribosomal peptide biosynthesis. A reductase domain catalyses a four-electron reduction, releasing the product from the NRPS with a terminal alcohol group.
Reaction Schemes
2
(3R)-3-isocyanobutanoyl-[acyl-carrier protein]
+
L-lysyl-[L-lysyl-carrier protein]
+
2
=
(3R)-N-[(2S)-1-hydroxy-6-[(3R)-3-isocyanobutanamido]hexan-2-yl]-3-isocyanobutanamide
+
[L-lysyl-carrier protein]
+
2
+
2
Synonyms mmaA , non-ribosomal peptide synthetase, NrPS, RNRP, ScoA ,
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non-ribosomal peptide synthetase
non-ribosomal peptide synthetase
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non-ribosomal peptide synthetase
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NrPS
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RNRP
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ScoA
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-
-
-
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2 (3R)-3-isocyanobutanoyl-[acyl-carrier protein] + L-lysyl-[L-lysyl-carrier protein] + 2 NADPH = (3R)-N-[(2S)-1-hydroxy-6-[(3R)-3-isocyanobutanamido]hexan-2-yl]-3-isocyanobutanamide + [L-lysyl-carrier protein] + 2 [acyl-carrier protein] + 2 NADP+
-
-
-
-
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(3R)-3-isocyano-fatty acyl-[acyl-carrier protein]:L-lysyl-[L-lysyl-carrier protein] (3R)-3-isocyano-fatty acyltransferase (hydrolysing)
The enzyme, found in some actinobacterial species, is a non-ribosomal peptide synthase (NRPS). Adenylation and thiolation domains of the enzyme activate a lysine residue and load it on the enzyme (this activity is described separately as EC 6.2.1.77, L-lysine---[L-lysyl-carrier protein] ligase). A condensation domain catalyses the condensation of two isonitrile-containing moieties to both amino groups of the lysine, a rare activity in non-ribosomal peptide biosynthesis. A reductase domain catalyses a four-electron reduction, releasing the product from the NRPS with a terminal alcohol group.
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2 (3R)-3-isocyanobutanoyl-[acyl-carrier protein] + D-lysyl-[L-lysyl-carrier protein] + 2 NADPH
(3R)-N-[(2S)-1-hydroxy-6-[(3R)-3-isocyanobutanamido]hexan-2-yl]-3-isocyanobutanamide + [L-lysyl-carrier protein] + 2 [acyl-carrier protein] + 2 NADP+
2 (3R)-3-isocyanobutanoyl-[acyl-carrier protein] + L-lysyl-[L-lysyl-carrier protein] + 2 NADPH
(3R)-N-[(2S)-1-hydroxy-6-[(3R)-3-isocyanobutanamido]hexan-2-yl]-3-isocyanobutanamide + [L-lysyl-carrier protein] + 2 [acyl-carrier protein] + 2 NADP+
L-Val-D-Phe-D-Thr-D-Ala-L-Ala-CoA + NADPH
?
L-Val-L-Phe-L-Thr-L-Ala-L-Ala-CoA + NADPH
L-Val-L-Phe-L-Thr-L-Ala-alaninol + L-Val-L-Phe-L-Thr-L-Ala-alaninal + L-Val-L-Phe-L-Thr-L-Ala-L-Ala + ?
additional information
?
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2 (3R)-3-isocyanobutanoyl-[acyl-carrier protein] + D-lysyl-[L-lysyl-carrier protein] + 2 NADPH
(3R)-N-[(2S)-1-hydroxy-6-[(3R)-3-isocyanobutanamido]hexan-2-yl]-3-isocyanobutanamide + [L-lysyl-carrier protein] + 2 [acyl-carrier protein] + 2 NADP+
-
Substrates: 40% activity compared to L-lysyl-[L-lysyl-carrier protein]
?
2 (3R)-3-isocyanobutanoyl-[acyl-carrier protein] + D-lysyl-[L-lysyl-carrier protein] + 2 NADPH
(3R)-N-[(2S)-1-hydroxy-6-[(3R)-3-isocyanobutanamido]hexan-2-yl]-3-isocyanobutanamide + [L-lysyl-carrier protein] + 2 [acyl-carrier protein] + 2 NADP+
-
Substrates: 10% activity compared to L-lysyl-[L-lysyl-carrier protein]
?
2 (3R)-3-isocyanobutanoyl-[acyl-carrier protein] + L-lysyl-[L-lysyl-carrier protein] + 2 NADPH
(3R)-N-[(2S)-1-hydroxy-6-[(3R)-3-isocyanobutanamido]hexan-2-yl]-3-isocyanobutanamide + [L-lysyl-carrier protein] + 2 [acyl-carrier protein] + 2 NADP+
-
Substrates: 100% activity
?
2 (3R)-3-isocyanobutanoyl-[acyl-carrier protein] + L-lysyl-[L-lysyl-carrier protein] + 2 NADPH
(3R)-N-[(2S)-1-hydroxy-6-[(3R)-3-isocyanobutanamido]hexan-2-yl]-3-isocyanobutanamide + [L-lysyl-carrier protein] + 2 [acyl-carrier protein] + 2 NADP+
-
Substrates: 100% activity
?
L-Val-D-Phe-D-Thr-D-Ala-L-Ala-CoA + NADPH
?
Substrates: -
?
L-Val-D-Phe-D-Thr-D-Ala-L-Ala-CoA + NADPH
?
Substrates: -
?
L-Val-L-Phe-L-Thr-L-Ala-L-Ala-CoA + NADPH
L-Val-L-Phe-L-Thr-L-Ala-alaninol + L-Val-L-Phe-L-Thr-L-Ala-alaninal + L-Val-L-Phe-L-Thr-L-Ala-L-Ala + ?
Substrates: -
?
L-Val-L-Phe-L-Thr-L-Ala-L-Ala-CoA + NADPH
L-Val-L-Phe-L-Thr-L-Ala-alaninol + L-Val-L-Phe-L-Thr-L-Ala-alaninal + L-Val-L-Phe-L-Thr-L-Ala-L-Ala + ?
Substrates: -
?
additional information
?
-
-
Substrates: the enzyme shows no activity with L-ornithine, L-arginine, L-asparagine, L-alanine, L-phenylalanine, and L-glutamine
-
additional information
?
-
-
Substrates: the enzyme shows no activity with L-ornithine, L-arginine, L-asparagine, L-alanine, L-phenylalanine, and L-glutamine
-
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Mg2+
-
2 mM used in assay conditions
Mg2+
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2 mM used in assay conditions
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SwissProt
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SwissProt
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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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metabolism
the enzyme is a 4e- reductase which can convert p-pant-tethered lipopeptide to lipopeptide alcohol during GPL biosynthesis. The enzyme also performs 4e- reductions to synthesize lipopeptide alcohol
metabolism
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the enzyme is a 4e- reductase which can convert p-pant-tethered lipopeptide to lipopeptide alcohol during GPL biosynthesis. The enzyme also performs 4e- reductions to synthesize lipopeptide alcohol
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INLPA_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
2512
0
269409
Swiss-Prot
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?
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x * 152000, SDS-PAGE
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sitting drop vapor diffusion method, using 2.5 M ammonium sulfate, 100 mM MES at pH 7.0
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Ni-NTA agarose resin column chromatography
Ni-NTA column chromatography and Superdex 200 gel filtration
Ni-NTA agarose resin column chromatography
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Ni-NTA agarose resin column chromatography
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
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Harris, N.; Sato, M.; Herman, N.; Twigg, F.; Cai, W.; Liu, J.; Zhu, X.; Downey, J.; Khalaf, R.; Martin, J.; Koshino, H.; Zhang, W.
Biosynthesis of isonitrile lipopeptides by conserved nonribosomal peptide synthetase gene clusters in Actinobacteria
Proc. Natl. Acad. Sci. USA
114
7025-7030
2017
Mycobacterium marinum, Streptomyces coeruleorubidus
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Chhabra, A.; Haque, A.S.; Pal, R.K.; Goyal, A.; Rai, R.; Joshi, S.; Panjikar, S.; Pasha, S.; Sankaranarayanan, R.; Gokhale, R.S.
Nonprocessive [2 + 2]e- off-loading reductase domains from mycobacterial nonribosomal peptide synthetases
Proc. Natl. Acad. Sci. USA
109
5681-5686
2012
Mycobacterium tuberculosis (Q10896), Mycobacterium tuberculosis H37Rv (Q10896)
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