Entry
Name
dihydroneopterin triphosphate aldolase;
PTPS-III
Class
Lyases;
Carbon-carbon lyases;
Aldehyde-lyases
BRITE hierarchy
Sysname
7,8-dihydroneopterin 3'-triphosphate glycolaldehyde phosphate-lyase [6-(hydroxymethyl)-7,8-dihydropterin-forming]
Reaction(IUBMB)
7,8-dihydroneopterin 3'-triphosphate = 6-(hydroxymethyl)-7,8-dihydropterin + glycolaldehyde triphosphate [RN:
R11719 ]
Reaction(KEGG)
Substrate
7,8-dihydroneopterin 3'-triphosphate [CPD:
C04895 ]
Product
6-(hydroxymethyl)-7,8-dihydropterin [CPD:
C01300 ];
glycolaldehyde triphosphate [CPD:
C21615 ]
Comment
The enzyme, which participates in a pathway for folate biosynthesis, is found in the Stramenopiles, a large group that includes oomycetes, various microalgae and brown algae, as well as in several bacterial phyla. It provides a bypass mechanism compensating for the lack of EC
4.1.2.25 , dihydroneopterin aldolase. In the malaria parasite Plasmodium falciparum the enzyme is bifunctional and also catalyses the activity of EC
4.2.3.12 , 6-pyruvoyltetrahydropterin synthase. cf. EC
4.1.2.59 , dihydroneopterin phosphate aldolase.
History
EC 4.1.2.60 created 2017
Pathway
Orthology
K22101 dihydroneopterin triphosphate aldolase (PTPS-III) / 6-pyruvoyltetrahydropterin synthase
Genes
PLAG : 39740896(PADL01_0626200)
PMAL : PMUG01_11035600(PTPS)
PBRS : 92371779(MKS88_003692)
PREL : PRELSG_1120300(PTPS)
» show all
Taxonomy
Reference
Authors
Dittrich S, Mitchell SL, Blagborough AM, Wang Q, Wang P, Sims PF, Hyde JE
Title
An atypical orthologue of 6-pyruvoyltetrahydropterin synthase can provide the missing link in the folate biosynthesis pathway of malaria parasites.
Journal
Sequence
Reference
Authors
Hyde JE, Dittrich S, Wang P, Sims PF, de Crecy-Lagard V, Hanson AD
Title
Plasmodium falciparum: a paradigm for alternative folate biosynthesis in diverse microorganisms?
Journal
Sequence
Reference
Authors
Pribat A, Jeanguenin L, Lara-Nunez A, Ziemak MJ, Hyde JE, de Crecy-Lagard V, Hanson AD
Title
6-pyruvoyltetrahydropterin synthase paralogs replace the folate synthesis enzyme dihydroneopterin aldolase in diverse bacteria.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 4.1.2.60
ExPASy - ENZYME nomenclature database: 4.1.2.60
LinkDB
All DBs