PDBsum entry 5hft

Transferase

PDB id

5hft

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Contents

			Protein chains

					305 a.a.


					149 a.a.


					154 a.a.

PDB id:

5hft

Links

Name:

Transferase

Title:

Crystal structure of hpxw

Structure:

Gamma-glutamyltranspeptidase. Chain: a, c. Fragment: residues 1-341. Engineered: yes. Gamma-glutamyltranspeptidase. Chain: b, d. Fragment: residues 342-528. Engineered: yes

Source:

Klebsiella pneumoniae subsp. Pneumoniae. Organism_taxid: 272620. Strain: atcc 700721 / mgh 78578. Gene: kpn_01768. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562

Resolution:

2.65Å

R-factor:

0.257

R-free:

0.298

Authors:

S.E.Ealick,K.A.Hicks

Key ref:

K.A.Hicks and S.E.Ealick (2016). Biochemical and structural characterization of Klebsiella pneumoniae oxamate amidohydrolase in the uric acid degradation pathway. Acta Crystallogr D Struct Biol, 72, 808-816. PubMed id: 27303801 DOI: 10.1107/S2059798316007099

Date:

07-Jan-16

Release date:

29-Jun-16

PROCHECK

	Headers

	References

Protein chains

A6T9C8 (HPXW_KLEP7) - Oxamate amidohydrolase proenzyme from Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)

Seq: Struc:

Seq: Struc:					528 a.a. 305 a.a.

Protein chain

A6T9C8 (HPXW_KLEP7) - Oxamate amidohydrolase proenzyme from Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)

Seq: Struc:

Seq: Struc:					528 a.a. 149 a.a.

Protein chain

A6T9C8 (HPXW_KLEP7) - Oxamate amidohydrolase proenzyme from Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)

Seq: Struc:

Seq: Struc:					528 a.a. 154 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

Chains A, C, B, D: E.C.3.5.1.126 - oxamate amidohydrolase.

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

Reaction:

oxamate + H2O = oxalate + NH4⁺

oxamate	+	H2O	=	oxalate	+	NH4(+)

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

Added reference

DOI no: 10.1107/S2059798316007099	Acta Crystallogr D Struct Biol 72:808-816 (2016)
PubMed id: 27303801

Biochemical and structural characterization of Klebsiella pneumoniae oxamate amidohydrolase in the uric acid degradation pathway.
K.A.Hicks, S.E.Ealick.

ABSTRACT

HpxW from the ubiquitous pathogen Klebsiella pneumoniae is involved in a novel uric acid degradation pathway downstream from the formation of oxalurate. Specifically, HpxW is an oxamate amidohydrolase which catalyzes the conversion of oxamate to oxalate and is a member of the Ntn-hydrolase superfamily. HpxW is autoprocessed from an inactive precursor to form a heterodimer, resulting in a 35.5 kDa α subunit and a 20 kDa β subunit. Here, the structure of HpxW is presented and the substrate complex is modeled. In addition, the steady-state kinetics of this enzyme and two active-site variants were characterized. These structural and biochemical studies provide further insight into this class of enzymes and allow a mechanism for catalysis consistent with other members of the Ntn-hydrolase superfamily to be proposed.