PDBsum entry 6dch

Oxidoreductase

PDB id

6dch

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Contents

			Protein chain

					296 a.a.

			Ligands

					ACT


					CHT

			Metals

					_CL


					_ZN

			Waters ×331

PDB id:

6dch

Links

Name:

Oxidoreductase

Title:

Structure of isonitrile biosynthesis enzyme scoe

Structure:

Scoe protein. Chain: a. Engineered: yes

Source:

Streptomyces coeruleorubidus. Organism_taxid: 116188. Gene: scoe. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.80Å

R-factor:

0.181

R-free:

0.207

Authors:

D.A.Born,C.L.Drennan

Key ref:

N.C.Harris et al. (2018). Isonitrile Formation by a Non-Heme Iron(II)-Dependent Oxidase/Decarboxylase. Angew Chem Int Ed Engl, 57, 9707-9710. PubMed id: 29906336 DOI: 10.1002/anie.201804307

Date:

07-May-18

Release date:

27-Jun-18

PROCHECK

	Headers

	References

Protein chain

A0A3B6UEU3 (INLPE_STRC4) - (3R)-3-[(carboxymethyl)amino]fatty acid oxygenase/decarboxylase from Streptomyces coeruleorubidus

Seq: Struc:					296 a.a. 296 a.a.

Key:

Secondary structure



		Enzyme reactions

Enzyme class:

E.C.1.14.11.78 - (R)-3-[(carboxymethyl)amino]fatty acid dioxygenase/decarboxylase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

a (3R)-3-[(carboxymethyl)amino]fatty acid + 2 2-oxoglutarate + 2 O2 = a (3R)-3-isocyanyl-fatty acid + 2 succinate + 3 CO2 + 2 H2O

(3R)-3-[(carboxymethyl)amino]fatty acid	+	2 × 2-oxoglutarate	+	2 × O2	=	(3R)-3-isocyanyl-fatty acid	+	2 × succinate	+	3 × CO2	+	2 × H2O

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1002/anie.201804307	Angew Chem Int Ed Engl 57:9707-9710 (2018)
PubMed id: 29906336

Isonitrile Formation by a Non-Heme Iron(II)-Dependent Oxidase/Decarboxylase.
N.C.Harris, D.A.Born, W.Cai, Y.Huang, J.Martin, R.Khalaf, C.L.Drennan, W.Zhang.

ABSTRACT

The electron-rich isonitrile is an important functionality in bioactive natural products, but its biosynthesis has been restricted to the IsnA family of isonitrile synthases. We herein provide the first structural and biochemical evidence of an alternative mechanism for isonitrile formation. ScoE, a putative non-heme iron(II)-dependent enzyme from Streptomyces coeruleorubidus, was shown to catalyze the conversion of (R)-3-((carboxymethyl)amino)butanoic acid to (R)-3-isocyanobutanoic acid through an oxidative decarboxylation mechanism. This work further provides a revised scheme for the biosynthesis of a unique class of isonitrile lipopeptides, of which several members are critical for the virulence of pathogenic mycobacteria.