Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the mould Hypocrea jecorina

Janis Liepins, Satu Kuorelahti, Merja Penttilä, Peter Richard

Research output: Contribution to journalArticleScientificpeer-review

31 Citations (Scopus)

Abstract

The mould Hypocrea jecorina (Trichoderma reesei) has two genes coding for enzymes with high similarity to the NADP-dependent glycerol dehydrogenase. These genes, called gld1 and gld2, were cloned and expressed in a heterologous host. The encoded proteins were purified and their kinetic properties characterized. GLD1 catalyses the conversion of d-glyceraldehyde and l-glyceraldehyde to glycerol, whereas GLD2 catalyses the conversion of dihydroxyacetone to glycerol. Both enzymes are specific for NADPH as a cofactor. The properties of GLD2 are similar to those of the previously described NADP-dependent glycerol-2- dehydrogenases (EC 1.1.1.156) purified from different mould species. It is a reversible enzyme active with dihydroxyacetone or glycerol as substrates. GLD1 resembles EC 1.1.1.72. It is also specific for NADPH as a cofactor but has otherwise completely different properties. GLD1 reduces d-glyceraldehyde and l-glyceraldehyde with similar affinities for the two substrates and similar maximal rates. The activity in the oxidizing reaction with glycerol as substrate was under our detection limit. Although the role of GLD2 is to facilitate glycerol formation under osmotic stress conditions, we hypothesize that GLD1 is active in pathways for sugar acid catabolism such as d-galacturonate catabolism.

Original languageEnglish
Pages (from-to)4229-4235
JournalFEBS Journal
Volume273
Issue number18
DOIs
Publication statusPublished - 1 Sep 2006
MoE publication typeA1 Journal article-refereed

Fingerprint

Hypocrea
Dihydroxyacetone
Glyceraldehyde
NADP
Glycerol
glycerol 2-dehydrogenase (NADP+)
Fungi
Enzymes
glycerol dehydrogenase
Substrates
Sugar Acids
Genes
Trichoderma
Osmotic Pressure
Limit of Detection
Oxidoreductases
Kinetics
Proteins

Keywords

  • Dihydroxyacetone
  • Glycerol dehydrogenase
  • Hypocrea jecorina
  • L-glyceraldehyde
  • NADP-specific glycerol dehydrogenase

Cite this

@article{6db966adcd954153a9f925e3e264bac0,
title = "Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the mould Hypocrea jecorina",
abstract = "The mould Hypocrea jecorina (Trichoderma reesei) has two genes coding for enzymes with high similarity to the NADP-dependent glycerol dehydrogenase. These genes, called gld1 and gld2, were cloned and expressed in a heterologous host. The encoded proteins were purified and their kinetic properties characterized. GLD1 catalyses the conversion of d-glyceraldehyde and l-glyceraldehyde to glycerol, whereas GLD2 catalyses the conversion of dihydroxyacetone to glycerol. Both enzymes are specific for NADPH as a cofactor. The properties of GLD2 are similar to those of the previously described NADP-dependent glycerol-2- dehydrogenases (EC 1.1.1.156) purified from different mould species. It is a reversible enzyme active with dihydroxyacetone or glycerol as substrates. GLD1 resembles EC 1.1.1.72. It is also specific for NADPH as a cofactor but has otherwise completely different properties. GLD1 reduces d-glyceraldehyde and l-glyceraldehyde with similar affinities for the two substrates and similar maximal rates. The activity in the oxidizing reaction with glycerol as substrate was under our detection limit. Although the role of GLD2 is to facilitate glycerol formation under osmotic stress conditions, we hypothesize that GLD1 is active in pathways for sugar acid catabolism such as d-galacturonate catabolism.",
keywords = "Dihydroxyacetone, Glycerol dehydrogenase, Hypocrea jecorina, L-glyceraldehyde, NADP-specific glycerol dehydrogenase",
author = "Janis Liepins and Satu Kuorelahti and Merja Penttil{\"a} and Peter Richard",
note = "CA2: TK402",
year = "2006",
month = "9",
day = "1",
doi = "10.1111/j.1742-4658.2006.05423.x",
language = "English",
volume = "273",
pages = "4229--4235",
journal = "FEBS Journal",
issn = "1742-464X",
publisher = "Wiley",
number = "18",

}

Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the mould Hypocrea jecorina. / Liepins, Janis; Kuorelahti, Satu; Penttilä, Merja; Richard, Peter.

In: FEBS Journal, Vol. 273, No. 18, 01.09.2006, p. 4229-4235.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Enzymes for the NADPH-dependent reduction of dihydroxyacetone and D-glyceraldehyde and L-glyceraldehyde in the mould Hypocrea jecorina

AU - Liepins, Janis

AU - Kuorelahti, Satu

AU - Penttilä, Merja

AU - Richard, Peter

N1 - CA2: TK402

PY - 2006/9/1

Y1 - 2006/9/1

N2 - The mould Hypocrea jecorina (Trichoderma reesei) has two genes coding for enzymes with high similarity to the NADP-dependent glycerol dehydrogenase. These genes, called gld1 and gld2, were cloned and expressed in a heterologous host. The encoded proteins were purified and their kinetic properties characterized. GLD1 catalyses the conversion of d-glyceraldehyde and l-glyceraldehyde to glycerol, whereas GLD2 catalyses the conversion of dihydroxyacetone to glycerol. Both enzymes are specific for NADPH as a cofactor. The properties of GLD2 are similar to those of the previously described NADP-dependent glycerol-2- dehydrogenases (EC 1.1.1.156) purified from different mould species. It is a reversible enzyme active with dihydroxyacetone or glycerol as substrates. GLD1 resembles EC 1.1.1.72. It is also specific for NADPH as a cofactor but has otherwise completely different properties. GLD1 reduces d-glyceraldehyde and l-glyceraldehyde with similar affinities for the two substrates and similar maximal rates. The activity in the oxidizing reaction with glycerol as substrate was under our detection limit. Although the role of GLD2 is to facilitate glycerol formation under osmotic stress conditions, we hypothesize that GLD1 is active in pathways for sugar acid catabolism such as d-galacturonate catabolism.

AB - The mould Hypocrea jecorina (Trichoderma reesei) has two genes coding for enzymes with high similarity to the NADP-dependent glycerol dehydrogenase. These genes, called gld1 and gld2, were cloned and expressed in a heterologous host. The encoded proteins were purified and their kinetic properties characterized. GLD1 catalyses the conversion of d-glyceraldehyde and l-glyceraldehyde to glycerol, whereas GLD2 catalyses the conversion of dihydroxyacetone to glycerol. Both enzymes are specific for NADPH as a cofactor. The properties of GLD2 are similar to those of the previously described NADP-dependent glycerol-2- dehydrogenases (EC 1.1.1.156) purified from different mould species. It is a reversible enzyme active with dihydroxyacetone or glycerol as substrates. GLD1 resembles EC 1.1.1.72. It is also specific for NADPH as a cofactor but has otherwise completely different properties. GLD1 reduces d-glyceraldehyde and l-glyceraldehyde with similar affinities for the two substrates and similar maximal rates. The activity in the oxidizing reaction with glycerol as substrate was under our detection limit. Although the role of GLD2 is to facilitate glycerol formation under osmotic stress conditions, we hypothesize that GLD1 is active in pathways for sugar acid catabolism such as d-galacturonate catabolism.

KW - Dihydroxyacetone

KW - Glycerol dehydrogenase

KW - Hypocrea jecorina

KW - L-glyceraldehyde

KW - NADP-specific glycerol dehydrogenase

UR - http://www.scopus.com/inward/record.url?scp=33748289979&partnerID=8YFLogxK

U2 - 10.1111/j.1742-4658.2006.05423.x

DO - 10.1111/j.1742-4658.2006.05423.x

M3 - Article

VL - 273

SP - 4229

EP - 4235

JO - FEBS Journal

JF - FEBS Journal

SN - 1742-464X

IS - 18

ER -