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In enzymology, an anthranilate phosphoribosyltransferase (EC 2.4.2.18) is an enzyme that catalyzes the chemical reaction

anthranilate + 5-phospho-alpha-D-ribose 1-diphosphate N-(5-phospho-D-ribosyl)-anthranilate +diphosphate

Thus, the two substrates of this enzyme are anthranilate and 5-phospho-alpha-D-ribose 1-diphosphate, whereas its two products are N-(5-phospho-D-ribosyl)-anthranilate and diphosphate.

This enzyme participates in aromatic amino acid biosynthesis and two-component system - general.

Nomenclature

This enzyme belongs to the family of glycosyltransferases, specifically the pentosyltransferases. The systematic name of this enzyme class is N-(5-phospho-D-ribosyl)-anthranilate:diphosphate phospho-alpha-D-ribosyltransferase. Other names in common use include:

anthranilate 5-phosphoribosylpyrophosphate
anthranilate phosphoribosylpyrophosphate phosphoribosyltransferase
anthranilate-PP-ribose-P phosphoribosyltransferase
phosphoribosyl-anthranilate pyrophosphorylase
phosphoribosylanthranilate pyrophosphorylase
phosphoribosylanthranilate transferase
phosphoribosyltransferase
PRT

Function

Anthranilate phosphoribosyltransferase (AnPRT) is a transferase enzyme which catalyses one of the most fundamental biochemical reactions: the transfer of a ribose group between an aromatic base and phosphate groups.^[1] More specifically, AnPRT facilitates the formation of a carbon-nitrogen bond between 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) and anthranilate.^[1]

Reaction

In the aromatic amino acid biosynthesis pathway specifically the tryptophan synthesis portion, AnPRT draws anthranilate and 5-phospho-alpha-D-ribose 1-diphosphate into the active site of the protein. Through the Sn1 mechanism below, AnPRT transfers the 5-phospho-alpha-D-ribose group (shown in blue) to the antranilate (shown in red) from the diphosphate molecule (shown in black).^[1]

AnPRT reaction in vivo

Structure

As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1GXB, 1KGZ, 1KHD, 1O17, 1V8G, 1VQU, 1ZVW, 1ZXY, 1ZYK, 2BPQ, 2ELC, and 2GVQ.

AnPRT has four domains and its quaternary structure consists of two identical protein structures.^[1] Each domain of AnPRT contains a magnesium ion and a pyrophosphate molecule as the active site.^[1] The secondary structure of AnPRT consists mainly of alpha helices with a beta sheet within each domain.

Homologues

There are homologues of AnPRT within Saccharomyces cerevisiae, Kluyveromyces lactis, Schizosaccharomyces pombe, Magnaporthe grisea, Neurospora crassa, Arabidopsis thaliana, and Oryza sativa.^[2] All of these organisms are alike in the sense that they make all of the amino acids needed for proper protein formation (also called autotrophs).

AnPRT is vital in these organisms because it is a vital step in the pathway to synthesis tryptophan, an essential amino acid in humans, which humans take from eating plants or other fungi.

Mutations in AnPRT

(This entire section comes from the paper written by Dr. Robert Last and his collaborators, referenced here:^[3])

An experiment was conducted on the varying mutations in the gene which codes for AnPRT in Arabidopsis. This study focused on the observed fluorescence of Arabidopsis plants when the gene which coded for AnPRT was mutated. It was found that there were nine mutations of the gene all with varying auxotrophic and prototrophic capabilities.

It was discovered that there was an increased level of anthranilate in the cells of Arabidopsis which were mutated. This was concluded to be linked to the fluorescence of the plants.

This study's relevance comes from the applications of the conclusions found by the scientists. The auxotrophic mutant could be used as a selectable marker in plant transformations. This can lead to a better way to engineer plants and find new ways to develop their systems to work for humanities purposes.

References

^ ^a ^b ^c ^d ^e Mayans O, Ivens A, Nissen LJ, Kirschner K, Wilmanns M (July 2002). "Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry". EMBO J. 21 (13): 3245–54. doi:10.1093/emboj/cdf298. PMC 126076. PMID 12093726.
^ HomoloGene. National Center for Biological Information. BLAST of Anthranilate phosphoribosyltransferase.http://www.ncbi.nlm.nih.gov/homologene/5712
^ Last, R.L, Li, J, & Rose, A.B. (January, 1997). An allelic series of blue fluorescent trpl mutants of arabidopsis thaliana. Genetics Society of America, (145), 197-205.

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English Journal

The Substrate Capture Mechanism of Mycobacterium tuberculosis Anthranilate Phosphoribosyltransferase Provides a Mode for Inhibition.

Castell A, Short FL, Evans GL, Cookson TV, Bulloch EM, Joseph DD, Lee CE, Parker EJ, Baker EN, Lott JS.SourceMaurice Wilkins Centre for Molecular Biodiscovery and School of Biological Sciences, University of Auckland , 3 Symonds Street, Auckland 1142, New Zealand.
Biochemistry.Biochemistry.2013 Feb 28. [Epub ahead of print]
Anthranilate phosphoribosyltransferase (AnPRT, EC 2.4.2.18) is a homodimeric enzyme that catalyzes the reaction between 5'-phosphoribosyl 1'-pyrophosphate (PRPP) and anthranilate, as part of the tryptophan biosynthesis pathway. Here we present the results of the first chemical screen for inhibitors
PMID 23363292

Anthranilate phosphoribosyl transferase (TrpD) generates phosphoribosylamine for thiamine synthesis from enamines and phosphoribosyl pyrophosphate.

Lambrecht JA, Downs DM.SourceDepartment of Bacteriology, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.
ACS chemical biology.ACS Chem Biol.2013 Jan 18;8(1):242-8. doi: 10.1021/cb300364k. Epub 2012 Nov 2.
Anthranilate phosphoribosyl transferase (TrpD) has been well characterized for its role in the tryptophan biosynthetic pathway. Here, we characterized a new reaction catalyzed by TrpD that resulted in the formation of the purine/thiamine intermediate metabolite phosphoribosylamine (PRA). The data sh
PMID 23101964

Experimental assessment of the importance of amino acid positions identified by an entropy-based correlation analysis of multiple-sequence alignments.

Dietrich S, Borst N, Schlee S, Schneider D, Janda JO, Sterner R, Merkl R.SourceInstitute of Biophysics and Physical Biochemistry, University of Regensburg, Universitätsstrasse 31, D-93053 Regensburg, Germany.
Biochemistry.Biochemistry.2012 Jul 17;51(28):5633-41. Epub 2012 Jul 6.
The analysis of a multiple-sequence alignment (MSA) with correlation methods identifies pairs of residue positions whose occupation with amino acids changes in a concerted manner. It is plausible to assume that positions that are part of many such correlation pairs are important for protein function
PMID 22737967

Japanese Journal

Growth inhibitory effects of anthranilic acid and its derivatives against Legionella pneumophila(MICROBIAL PHYSIOLOGY AND BIOTECHNOLOGY)

Journal of bioscience and bioengineering 113(6), 726-729, 2012-06
NAID 110009470593

Regulation of tryptophan biosynthesis by feedback inhibition of the second-step enzyme, anthranilate phosphoribosyltransferase, in Brevibacterium flavum.

Agricultural and Biological Chemistry 47(10), 2295-2305, 1983
NAID 130000027741

Altered regulatory mechanisms for tryptophan synthesis in fluorotryptophan-resistant mutants of Brevibacterium flavum.

The Journal of Biochemistry 83(3), 879-886, 1978
NAID 130003540579

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リンク元	「アントラニル酸ホスホリボシルトランスフェラーゼ」
関連記事	「phosphoribosyltransferase」「anthranilate」

「アントラニル酸ホスホリボシルトランスフェラーゼ」

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anthranilate phosphoribosyltransferase
	Anthranilate Phosphoribosyltransferase 3D rendering
Identifiers
EC number	2.4.2.18
CAS number	9059-35-2
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
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NCBI	proteins